text:
H. Loetscher, Y. E. Pan, H. Lahm, R. Gentz, M. Brockhaus et al., Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor, Cell, vol.61, issue.2, pp.351-359, 1990.
DOI : 10.1016/0092-8674(90)90815-V
&. Dixit and V. M. , Identification and functional characterization of DR6, a novel death domaincontaining TNF receptor, FEBS Letters, vol.431, pp.351-356, 1998.
B. Trauth, C. Klas, A. Peters, S. Matzku, P. Moller et al., Monoclonal antibody-mediated tumor regression by induction of apoptosis, Science, vol.245, issue.4915, pp.301-305, 1989.
DOI : 10.1126/science.2787530
T. Chtanova, S. G. Tangye, R. Newton, N. Frank, M. R. Hodge et al., T Follicular Helper Cells Express a Distinctive Transcriptional Profile, Reflecting Their Role as Non-Th1/Th2 Effector Cells That Provide Help for B Cells, The Journal of Immunology, vol.173, issue.1, pp.68-78, 2004.
DOI : 10.4049/jimmunol.173.1.68
R. Basu, D. B. O-'quinn, D. J. Silberger, T. R. Schoeb, L. Fouser et al., Th22 Cells Are an Important Source of IL-22 for Host Protection against Enteropathogenic Bacteria, Th22 Cells Are an Important Source of IL-22 for Host Protection against Enteropathogenic Bacteria, pp.1061-1075, 2012.
DOI : 10.1016/j.immuni.2012.08.024
K. Gerlach, Y. Hwang, A. Nikolaev, R. Atreya, H. Dornhoff et al., TH9 cells that express the transcription factor PU.1 drive T cell???mediated colitis via IL-9 receptor signaling in intestinal epithelial cells, TH9 cells that express the transcription factor PU.1 drive T cell?mediated colitis via IL-9 receptor signaling in intestinal epithelial cells, pp.676-686, 2014.
DOI : 10.1038/ni.2208
A. Strasser, P. J. Jost, and S. Nagata, The Many Roles of FAS Receptor Signaling in the Immune System, Immunity, vol.30, issue.2, pp.180-92, 2009.
S. A. Marsters, R. M. Pitti, C. J. Donahue, S. Ruppert, K. D. Bauer et al., Activation of apoptosis by Apo-2 ligand is independent of FADD but blocked by CrmA, Current Biology, vol.6, issue.6, pp.750-752, 1996.
DOI : 10.1016/S0960-9822(09)00456-4
A. Ratner and W. R. Clark, Role of TNF-alpha in CD8+ cytotoxic T lymphocyte-mediated lysis, J Immunol, vol.150, pp.4303-4317, 1993.
J. L. Chu, Massive upregulation of the Fas ligand in lpr and gld mice: implications for Fas regulation and the graft-versus-host disease-like wasting syndrome, Journal of Experimental Medicine, vol.181, issue.1, pp.393-398, 1995.
DOI : 10.1084/jem.181.1.393
S. Nagata and P. Golstein, The Fas death factor, Science, vol.165, issue.5, pp.1449-56, 1995.
DOI : 10.1084/jem.165.5.1371
Y. Yang, Fas and activation-induced Fas ligand mediate apoptosis of T cell hybridomas: inhibition of Fas ligand expression by retinoic acid and glucocorticoids, Journal of Experimental Medicine, vol.181, issue.5, pp.1673-1682, 1995.
M. Lu, D. A. Lawrence, S. Marsters, D. Acosta-alvear, P. Kimmig et al., Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis, Science, vol.1, issue.0, pp.98-101, 2014.
DOI : 10.7554/eLife.00048
E. S. Alnemri, D. J. Livingston, D. W. Nicholson, G. Salvesen, N. A. Thornberry et al., Human ICE/CED-3 Protease Nomenclature, Cell, vol.87, issue.2, p.171, 1996.
URL : https://doi.org/10.1016/s0092-8674(00)81334-3
G. Papoff, P. Hausler, A. Eramo, M. G. Pagano, G. Di-leve et al., Identification and Characterization of a Ligand-independent Oligomerization Domain in the Extracellular Region of the CD95 Death Receptor, Journal of Biological Chemistry, vol.2, issue.53, pp.38241-38250, 1999.
DOI : 10.1006/jmbi.1994.1371
R. M. Siegel, J. K. Frederiksen, D. A. Zacharias, F. K. Chan, M. Johnson et al., Fas Preassociation Required for Apoptosis Signaling and Dominant Inhibition by Pathogenic Mutations, Science, vol.288, issue.5475, pp.2354-2361, 2000.
DOI : 10.1126/science.288.5475.2354
V. Edmond, B. Ghali, A. Penna, J. Taupin, S. Daburon et al., Precise Mapping of the CD95 Pre-Ligand Assembly Domain, Precise Mapping of the CD95 Pre-Ligand Assembly Domain, p.46236, 2012.
DOI : 10.1371/journal.pone.0046236.g004
URL : https://hal.archives-ouvertes.fr/hal-00873708
M. P. Boldin, E. E. Varfolomeev, Z. Pancer, I. L. Mett, J. H. Camonis et al., A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain, Journal of Biological Chemistry, vol.211, issue.14, pp.7795-7798, 1995.
DOI : 10.1002/prot.340090107
A. M. Chinnaiyan, K. O-'rourke, M. Tewari, and V. M. Dixit, FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis, Cell, vol.81, issue.4, pp.505-512, 1995.
F. C. Kischkel, S. Hellbardt, I. Behrmann, M. Germer, M. Pawlita et al., Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor, Embo J, vol.14, pp.5579-88, 1995.
S. Horn, M. A. Hughes, R. Schilling, C. Sticht, T. Tenev et al., Caspase-10 Negatively Regulates Caspase-8-Mediated Cell Death, Switching the Response to CD95L in Favor of NF-??B Activation and Cell Survival, Cell Reports, vol.19, issue.4, pp.785-797, 2017.
DOI : 10.1016/j.celrep.2017.04.010
M. A. Hughes, N. Harper, M. Butterworth, K. Cain, G. M. Cohen et al., Reconstitution of the Death-Inducing Signaling Complex Reveals a Substrate Switch that Determines CD95-Mediated Death or Survival, Molecular Cell, vol.35, issue.3, pp.265-79, 2009.
DOI : 10.1016/j.molcel.2009.06.012
P. Li, D. Nijhawan, I. Budihardjo, S. M. Srinivasula, M. Ahmad et al., Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade, Cell, vol.91, issue.4, pp.479-89, 1997.
C. Scaffidi, Two CD95 (APO-1/Fas) signaling pathways, The EMBO Journal, pp.1675-1687, 1998.
A. Algeciras-schimnich, E. M. Pietras, B. C. Barnhart, P. Legembre, S. Vijayan et al., Two CD95 tumor classes with different sensitivities to antitumor drugs, Proceedings of the National Academy of Sciences, vol.9, issue.5, pp.11445-50, 2003.
B. Chaigne-delalande, W. Mahfouf, S. Daburon, J. F. Moreau, and P. Legembre, CD95 engagement mediates actin-independent and -dependent apoptotic signals, Cell Death & Differentiation, vol.181, issue.12, pp.1654-64, 2009.
DOI : 10.4049/jimmunol.181.11.7630
URL : http://www.nature.com/cdd/journal/v16/n12/pdf/cdd2009111a.pdf
C. Scaffidi, S. Fulda, A. Srinivasan, C. Friesen, F. Li et al., Two CD95 (APO-1/Fas) signaling pathways, The EMBO Journal, vol.17, issue.6, pp.1675-87, 1998.
DOI : 10.1093/emboj/17.6.1675
URL : http://emboj.embopress.org/content/embojnl/17/6/1675.full.pdf
X. M. Yin, Signal transduction mediated by Bid, a pro-death Bcl-2 family proteins, connects the death receptor and mitochondria apoptosis pathways, Cell Research, vol.21, issue.3, pp.161-168, 2000.
DOI : 10.1097/00003246-199310001-00002
X. M. Yin, K. Wang, A. Gross, Y. Zhao, S. Zinkel et al., Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis, Nature, vol.5, issue.6747, pp.886-91, 1999.
DOI : 10.1038/sj.cdd.4400449
P. J. Jost, S. Grabow, D. Gray, M. D. Mckenzie, U. Nachbur et al., XIAP discriminates between type I and type II FAS-induced apoptosis, Nature, vol.139, issue.7258, pp.1035-1044, 2009.
DOI : 10.1038/nature08229
URL : http://europepmc.org/articles/pmc2956120?pdf=render
N. Roy, Q. L. Deveraux, R. Takahashi, G. S. Salvesen, and J. C. Reed, The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases, The EMBO Journal, vol.16, issue.23, pp.6914-6939, 1997.
DOI : 10.1093/emboj/16.23.6914
Q. L. Deveraux, R. Takahashi, G. S. Salvesen, and J. C. Reed, X-linked IAP is a direct inhibitor of cell-death proteases, Nature, vol.384, issue.6639, pp.300-304, 1997.
DOI : 10.1038/384368a0
Q. L. Deveraux, N. Roy, H. R. Stennicke, T. Van-arsdale, Q. Zhou et al., IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases, The EMBO Journal, vol.17, issue.8, pp.2215-2238, 1998.
Y. Suzuki, Y. Nakabayashi, and R. Takahashi, Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death, Proceedings of the National Academy of Sciences, vol.18, issue.22, pp.8662-8669, 2001.
C. Du, M. Fang, Y. Li, L. Li, and X. Wang, Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition, Cell, pp.33-42, 2000.
X. M. Sun, S. B. Bratton, M. Butterworth, M. Macfarlane, and G. M. Cohen, Inhibit CD95-mediated Apoptosis by Preventing Mitochondrial Release of Smac/DIABLO and Subsequent Inactivation of X-linked Inhibitor-of-Apoptosis Protein, Journal of Biological Chemistry, vol.61, issue.13, pp.11345-51, 2002.
DOI : 10.1038/5517
M. Beneteau, M. Pizon, B. Chaigne-delalande, S. Daburon, P. Moreau et al., Localization of Fas/CD95 into the Lipid Rafts on Down-Modulation of the Phosphatidylinositol 3-Kinase Signaling Pathway, Molecular Cancer Research, vol.6, issue.4, pp.604-617, 2008.
DOI : 10.1158/1541-7786.MCR-07-0331
J. W. Peacock, J. Palmer, D. Fink, S. Ip, E. M. Pietras et al., PTEN Loss Promotes Mitochondrially Dependent Type II Fas-Induced Apoptosis via PEA-15, Molecular and Cellular Biology, vol.29, issue.5, pp.1222-1256, 2009.
DOI : 10.1128/MCB.01660-08
A. S. Varadhachary, M. Edidin, A. M. Hanlon, M. E. Peter, P. H. Krammer et al., Phosphatidylinositol 3'-Kinase Blocks CD95 Aggregation and Caspase-8 Cleavage at the Death-Inducing Signaling Complex by Modulating Lateral Diffusion of CD95, The Journal of Immunology, vol.166, issue.11, pp.6564-6573, 2001.
M. Pizon, H. Rampanarivo, S. Tauzin, B. Chaigne-delalande, S. Daburon et al., Actin-independent exclusion of CD95 by PI3K/AKT signalling: Implications for apoptosis, European Journal of Immunology, vol.9, issue.8, pp.2368-78, 2011.
G. Condorelli, G. Vigliotta, A. Cafieri, A. Trencia, P. Andalo et al., PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis, Oncogene, vol.18, issue.31, pp.4409-4424, 1999.
DOI : 10.1038/sj.onc.1202831
URL : http://www.nature.com/onc/journal/v18/n31/pdf/1202831a.pdf
H. Renganathan, H. Vaidyanathan, A. Knapinska, and J. W. Ramos, Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD, Biochemical Journal, vol.390, issue.3, pp.729-764, 2005.
DOI : 10.1042/BJ20050378
A. Trencia, A. Perfetti, A. Cassese, G. Vigliotta, C. Miele et al., Protein Kinase B/Akt Binds and Phosphorylates PED/PEA-15, Stabilizing Its Antiapoptotic Action, Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action, pp.4511-4532, 2003.
DOI : 10.1128/MCB.23.13.4511-4521.2003
A. Strasser, A. W. Harris, D. C. Huang, P. H. Krammer, and S. Cory, Bcl-2 and Fas/APO- 1 regulate distinct pathways to lymphocyte apoptosis, Embo J, vol.14, pp.6136-6183, 1995.
V. Lacronique, A. Mignon, M. Fabre, B. Viollet, N. Rouquet et al., Bcl???2 protects from lethal hepatic apoptosis induced by an ant???Fas antibody in mice, Nature Medicine, vol.128, issue.1, pp.80-86, 1996.
DOI : 10.1038/nm0196-80
S. M. Kang, D. B. Schneider, Z. Lin, D. Hanahan, D. A. Dichek et al., Fas ligand expression in islets of Langerhans does not confer immune privilege and instead targets them for rapid destruction, Nature Medicine, vol.26, issue.7, pp.738-781, 1997.
DOI : 10.1074/jbc.271.47.29969
J. J. Chen, Y. Sun, and G. J. Nabel, Regulation of the proinflammatory effects of Fas ligand (CD95L), Science, pp.1714-1721, 1998.
S. Buonocore, V. Flamand, N. Claessen, P. Heeringa, M. Goldman et al., Dendritic cells overexpressing Fas-ligand induce pulmonary vasculitis in mice, Clinical & Experimental Immunology, vol.166, issue.1, pp.74-80, 2004.
H. Matsuno, K. Yudoh, Y. Watanabe, F. Nakazawa, H. Aono et al., Stromelysin-1 (MMP-3) in synovial fluid of patients with rheumatoid arthritis has potential to cleave membrane bound Fas ligand, J Rheumatol, vol.28, pp.22-30, 2001.
T. Vargo-gogola, H. C. Crawford, B. Fingleton, and L. M. Matrisian, Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand, Archives of Biochemistry and Biophysics, vol.408, issue.2, pp.155-161, 2002.
M. Kiaei, K. Kipiani, N. Calingasan, E. Wille, J. Chen et al., Matrix metalloproteinase-9 regulates TNF-?? and FasL expression in neuronal, glial cells and its absence extends life in a transgenic mouse model of amyotrophic lateral sclerosis, Experimental Neurology, vol.205, issue.1, pp.74-81, 2007.
DOI : 10.1016/j.expneurol.2007.01.036
V. Kirkin, N. Cahuzac, F. Guardiola-serrano, S. Huault, K. Lückerath et al., The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells, Cell Death and Differentiation, pp.1678-1687, 2007.
M. Schulte, K. Reiss, M. Lettau, T. Maretzky, A. Ludwig et al., ADAM10 regulates FasL cell surface expression and modulates FasLinduced cytotoxicity and activation-induced cell death, Cell Death and Differentiation, 2007.
URL : http://www.nature.com/cdd/journal/v14/n5/pdf/4402101a.pdf
N. Holler, A. Tardivel, M. Kovacsovics-bankowski, S. Hertig, O. Gaide et al., Two Adjacent Trimeric Fas Ligands Are Required for Fas Signaling and Formation of a Death-Inducing Signaling Complex, Molecular and Cellular Biology, vol.23, issue.4, pp.1428-1440, 2003.
DOI : 10.1128/MCB.23.4.1428-1440.2003
P. Schneider, N. Holler, J. Bodmer, M. Hahne, K. Frei et al., Conversion of Membrane-bound Fas(CD95) Ligand to Its Soluble Form Is Associated with Downregulation of Its Proapoptotic Activity and Loss of Liver Toxicity, The Journal of Experimental Medicine, vol.8, issue.8, pp.1205-1213, 1998.
T. Suda, H. Hashimoto, M. Tanaka, T. Ochi, and S. Nagata, Membrane Fas Ligand Kills Human Peripheral Blood T Lymphocytes, and Soluble Fas Ligand Blocks the Killing, The Journal of Experimental Medicine, vol.54, issue.12, pp.2045-2050, 1997.
DOI : 10.1172/JCI118789
S. Tauzin, B. Chaigne-delalande, E. Selva, N. Khadra, S. Daburon et al., The Naturally Processed CD95L Elicits a c-Yes/Calcium/PI3K-Driven Cell Migration Pathway, PLoS Biology, vol.52, issue.Pt 3, 2011.
DOI : 10.1371/journal.pbio.1001090.s010
L. , O. R. Tai, L. Lee, L. Kruse, E. A. Grabow et al., Membranebound Fas ligand only is essential for Fas-induced apoptosis, Nature, vol.461, pp.659-63, 2009.
A. Poissonnier, D. Sanseau, L. Gallo, M. Malleter, M. Levoin et al., CD95-Mediated Calcium Signaling Promotes T Helper 17 Trafficking to Inflamed Organs in Lupus-Prone Mice, Immunity, vol.45, issue.1, pp.209-232, 2016.
S. P. Cullen, C. M. Henry, C. J. Kearney, S. E. Logue, M. Feoktistova et al., Fas/CD95-Induced Chemokines Can Serve as ???Find-Me??? Signals for Apoptotic Cells, Molecular Cell, vol.49, issue.6, pp.1034-1082, 2013.
D. R. Green, A. Oberst, C. P. Dillon, R. Weinlich, and G. S. Salvesen, RIPK-Dependent Necrosis and Its Regulation by Caspases: A Mystery in Five Acts, Molecular Cell, vol.44, issue.1, pp.9-16, 2011.
W. J. Kaiser, J. W. Upton, A. B. Long, D. Livingston-rosanoff, L. P. Daley-bauer et al., RIP3 mediates the embryonic lethality of caspase-8-deficient mice, Nature, vol.181, issue.7338, pp.368-72, 2011.
DOI : 10.4049/jimmunol.181.9.6427
A. Oberst, C. P. Dillon, R. Weinlich, L. L. Mccormick, P. Fitzgerald et al., Catalytic activity of the caspase-8???FLIPL complex inhibits RIPK3-dependent necrosis, Nature, vol.24, issue.7338, pp.363-370, 2011.
J. Senft, B. Helfer, and S. M. Frisch, Caspase-8 interacts with the p85 subunit of phosphatidylinositol 3-kinase to regulate cell adhesion and motility, Cancer Res, pp.11505-11514, 2007.
D. Finlay, A. Howes, and K. Vuori, Critical Role for Caspase-8 in Epidermal Growth Factor Signaling, Cancer Research, vol.69, issue.12, pp.5023-5032, 2009.
DOI : 10.1158/0008-5472.CAN-08-3731
C. M. Henry and S. J. Martin, Caspase-8 Acts in a Non-enzymatic Role as a Scaffold for Assembly of a Pro-inflammatory ???FADDosome??? Complex upon TRAIL Stimulation, Molecular Cell, vol.65, issue.4, pp.715-729, 2017.
T. Fernandes-alnemri, R. C. Armstrong, J. Krebs, S. M. Srinivasula, L. Wang et al., In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains., Proceedings of the National Academy of Sciences, vol.93, issue.15, pp.7464-7473, 1996.
DOI : 10.1073/pnas.93.15.7464
M. Muzio, A. M. Chinnaiyan, F. C. Kischkel, K. O-'rourke, A. Shevchenko et al., FLICE, A Novel FADD-Homologous ICE/CED-3???like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling Complex, Cell, vol.85, issue.6, pp.817-844, 1996.
P. J. Dupont and A. N. Warrens, Fas ligand exerts its pro-inflammatory effects via neutrophil recruitment but not activation, Immunology, vol.282, issue.1, pp.133-142, 2007.
URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2265864
A. Villalba, CD95-ligand on peripheral myeloid cells activates Syk kinase to trigger their recruitment to the inflammatory site, Immunity, vol.32, pp.240-52, 2010.
M. Malleter, S. Tauzin, A. Bessede, R. Castellano, A. Goubard et al., CD95L Cell Surface Cleavage Triggers a Prometastatic Signaling Pathway in Triple-Negative Breast Cancer, Cancer Research, vol.73, issue.22, pp.6711-6732, 2013.
L. Gao, G. S. Gulculer, L. Golbach, H. Block, A. Zarbock et al., Endothelial cell-derived CD95 ligand serves as a chemokine in induction of neutrophil slow rolling and adhesion, Elife, 2016.
M. Rescigno, V. Piguet, B. Valzasina, S. Lens, R. Zubler et al., FAS Engagement Induces the Maturation of Dendritic Cells (Dcs), the Release of Interleukin (Il)-1??, and the Production of Interferon ?? in the Absence of IL-12 during Dc???T Cell Cognate Interaction, The Journal of Experimental Medicine, vol.154, issue.11, pp.1661-1669, 2000.
DOI : 10.1073/pnas.94.8.3943
P. B. Stranges, J. Watson, C. J. Cooper, C. M. Choisy-rossi, A. C. Stonebraker et al., Elimination of Antigen-Presenting Cells and Autoreactive T Cells by Fas Contributes to Prevention of Autoimmunity, Immunity, vol.26, issue.5, pp.629-670, 2007.
I. Mabrouk, S. Buart, M. Hasmim, C. Michiels, E. Connault et al., Prevention of Autoimmunity and Control of Recall Response to Exogenous Antigen by Fas Death Receptor Ligand Expression on T Cells, Immunity, vol.29, issue.6, pp.922-955, 2008.
O. Reilly, L. A. Tai, L. Lee, L. Kruse, E. A. Grabow et al., Membrane-bound Fas ligand only is essential for Fas-induced apoptosis, Nature, vol.166, issue.7264, pp.659-63, 2009.
V. Varanasi, A. A. Khan, and A. V. Chervonsky, Loss of the death receptor CD95 (Fas) expression by dendritic cells protects from a chronic viral infection, Proceedings of the National Academy of Sciences, vol.323, issue.5913, pp.8559-64, 2014.
A. Lundqvist, T. Nagata, R. Kiessling, and P. Pisa, Mature dendritic cells are protected from Fas/CD95-mediated apoptosis by upregulation of Bcl-X(L), Cancer Immunol Immunother, pp.139-183, 2002.
S. T. Ju, D. J. Panka, H. Cui, R. Ettinger, M. Khatib et al., Fas(CD95)/FasL interactions required for programmed cell death after T-cell activation, Nature, vol.373, issue.6513, pp.444-452, 1995.
M. R. Alderson, R. J. Armitage, E. Maraskovsky, T. W. Tough, E. Roux et al., Fas transduces activation signals in normal human T lymphocytes, Journal of Experimental Medicine, vol.178, issue.6, pp.2231-2236, 1993.
N. J. Kennedy, T. Kataoka, J. Tschopp, and R. C. Budd, Caspase Activation Is Required for T Cell Proliferation, The Journal of Experimental Medicine, vol.14, issue.12, pp.1891-1897, 1999.
DOI : 10.1038/40657
A. Lepple-wienhues, C. Belka, T. Laun, A. Jekle, B. Walter et al., Stimulation of CD95 (Fas) blocks T lymphocyte calcium channels through sphingomyelinase and sphingolipids, Proceedings of the National Academy of Sciences, vol.180, issue.4, pp.13795-800, 1999.
A. Krueger, S. C. Fas, S. Baumann, and P. H. Krammer, The role of CD95 in the regulation of peripheral T-cell apoptosis, Immunological Reviews, vol.163, issue.1, pp.58-69, 2003.
DOI : 10.1002/(SICI)1521-4141(199903)29:03<1041::AID-IMMU1041>3.3.CO;2-R
P. H. Krammer, CD95's deadly mission in the immune system, Nature, vol.887, issue.6805, pp.789-95, 2000.
P. Bouillet, D. Metcalf, D. C. Huang, D. M. Tarlinton, T. W. Kay et al., Proapoptotic Bcl-2 Relative Bim Required for Certain Apoptotic Responses, Leukocyte Homeostasis, and to Preclude Autoimmunity, Science, vol.286, issue.5445, pp.1735-1743, 1999.
D. A. Hildeman, Y. Zhu, T. C. Mitchell, P. Bouillet, A. Strasser et al., Activated T Cell Death In Vivo Mediated by Proapoptotic Bcl-2 Family Member Bim, Immunity, vol.16, issue.6, pp.759-67, 2002.
A. Hennino, M. Berard, P. H. Krammer, and T. Defrance, Flice-Inhibitory Protein Is a Key Regulator of Germinal Center B Cell Apoptosis, The Journal of Experimental Medicine, vol.157, issue.4, pp.447-58, 2001.
D. Butt, T. D. Chan, K. Bourne, J. R. Hermes, A. Nguyen et al., FAS Inactivation Releases Unconventional Germinal Center B Cells that Escape Antigen Control and Drive IgE and Autoantibody Production, FAS Inactivation Releases Unconventional Germinal Center B Cells that Escape Antigen Control and Drive IgE and Autoantibody Production, pp.890-902, 2015.
URL : https://doi.org/10.1016/j.immuni.2015.04.010
L. Gattinoni, E. Lugli, Y. Ji, Z. Pos, C. M. Paulos et al., A human memory T cell subset with stem cell???like properties, Nature Medicine, vol.79, issue.10, pp.1290-1297, 2011.
DOI : 10.1002/cyto.a.21015
C. A. Klebanoff, C. D. Scott, A. J. Leonardi, T. N. Yamamoto, A. C. Cruz et al., Memory T cell???driven differentiation of naive cells impairs adoptive immunotherapy, M. & Restifo, N. P. (2016) Memory T cell-driven differentiation of naive cells impairs adoptive immunotherapy, pp.318-352
DOI : 10.1172/JCI81217DS1
E. Bettelli, T. Korn, and V. K. Kuchroo, Th17: the third member of the effector T cell trilogy, Current Opinion in Immunology, vol.19, issue.6, pp.652-659, 2007.
DOI : 10.1016/j.coi.2007.07.020
P. J. Ratcliffe, M. L. Coleman, M. Bix, D. Tantin, H. Park et al., Dynamic regulatory network controlling TH17 cell differentiation, Nature, vol.496, pp.461-469, 2013.
D. R. Green, A. Oberst, C. P. Dillon, R. Weinlich, . Salvesen et al., RIPK-Dependent Necrosis and Its Regulation by Caspases: A Mystery in Five Acts, Molecular Cell, vol.44, issue.1, pp.9-16, 2011.
W. J. Kaiser, J. W. Upton, A. B. Long, D. Livingston-rosanoff, L. P. Daley-bauer et al., RIP3 mediates the embryonic lethality of caspase-8-deficient mice, Nature, vol.181, issue.7338, pp.368-372, 2011.
J. Senft, B. Helfer, and S. M. Frisch, Caspase-8 Interacts with the p85 Subunit of Phosphatidylinositol 3-Kinase to Regulate Cell Adhesion and Motility, Cancer Research, pp.11505-11509, 2007.
D. Finlay, A. Howes, and K. Vuori, Critical Role for Caspase-8 in Epidermal Growth Factor Signaling, Cancer Research, pp.5023-5029, 2009.
C. Scaffidi, F. C. Kischkel, P. H. Krammer, M. E. Peter, T. Fernandes-alnemri et al., Analysis of the CD95 (APO-1/Fas) Death-Inducing Signaling Complex by High-Resolution Two-Dimensional Gel Electrophoresis in Methods in Enzymology pp, vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains Proceedings of the National Academy of Sciences, pp.363-373, 1996.
M. Muzio, A. M. Chinnaiyan, F. C. Kischkel, K. O-'rourke, A. Shevchenko et al., FLICE, A Novel FADD-Homologous ICE/CED-3???like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling Complex, ) FLICE, A Novel FADD-Homologous ICE/CED-3?like Protease, Is Recruited to the CD95 (Fas/APO- 1) Death-Inducing Signaling Complex, pp.817-827, 1996.
D. W. Chang, Z. Xing, V. L. Capacio, M. E. Peter, and X. Yang, Interdimer processing mechanism of procaspase-8 activation, The EMBO Journal, vol.22, issue.16, pp.4132-4174, 2003.
DOI : 10.1093/emboj/cdg414
M. Beneteau, M. Pizon, B. Chaigne-delalande, S. Daburon, P. Moreau et al., Localization of Fas/CD95 into the Lipid Rafts on Down-Modulation of the Phosphatidylinositol 3-Kinase Signaling Pathway, Localization of Fas/CD95 into the Lipid Rafts on Down-Modulation of the Phosphatidylinositol 3- Kinase Signaling Pathway, pp.604-613, 2008.
M. Pizon, H. Rampanarivo, S. Tauzin, B. Chaigne-delalande, S. Daburon et al., Actin-independent exclusion of CD95 by PI3K/AKT signalling: Implications for apoptosis, European Journal of Immunology, vol.9, issue.8, pp.2368-2378, 2011.
C. Feig, V. Tchikov, S. Schutze, and M. E. Peter, Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling, The EMBO Journal, vol.245, issue.1, pp.221-252, 2007.
DOI : 10.1128/MCB.13.10.6385
K. Chakrabandhu, S. Huault, N. Garmy, J. Fantini, E. Stebe et al., The extracellular glycosphingolipid-binding motif of Fas defines its internalization route, mode and outcome of signals upon activation by ligand, Cell Death & Differentiation, vol.269, issue.12, pp.1824-1861, 2008.
DOI : 10.1111/j.1365-2818.2006.01706.x
F. Renault, E. Formstecher, I. Callebaut, M. P. Junier, and H. Chneiweiss, The multifunctional protein PEA-15 is involved in the control of apoptosis and cell cycle in astrocytes, Biochemical Pharmacology, vol.66, issue.8, pp.1581-1589, 2003.
J. Wang, H. J. Chun, W. Wong, D. M. Spencer, and M. J. Lenardo, Caspase-10 is an initiator caspase in death receptor signaling, Proceedings of the National Academy of Sciences, vol.13, issue.19, pp.13884-13892, 2001.
DOI : 10.1101/gad.13.19.2514
M. R. Sprick, E. Rieser, H. Stahl, A. Grosse-wilde, M. A. Weigand et al., Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8, The EMBO Journal, vol.21, issue.17, pp.4520-4550, 2002.
DOI : 10.1093/emboj/cdf441
F. C. Kischkel, D. A. Lawrence, A. Tinel, H. Leblanc, A. Virmani et al., Death Receptor Recruitment of Endogenous Caspase-10 and Apoptosis Initiation in the Absence of Caspase-8, Journal of Biological Chemistry, vol.43, issue.49, pp.46639-46685, 2001.
M. Leverkus, M. Neumann, T. Mengling, C. T. Rauch, E. B. Brocker et al., Regulation of tumor necrosis factor-related apoptosis-inducing ligand sensitivity in primary and transformed human keratinocytes, Cancer Res, vol.60, pp.553-562, 2000.
D. Siegmund, P. Hadwiger, K. Pfizenmaier, H. P. Vornlocher, and H. Wajant, Selective inhibition of FLICE-like inhibitory protein expression with small interfering RNA oligonucleotides is sufficient to sensitize tumor cells for TRAIL-induced apoptosis, pp.725-757, 2002.
U. Fischer, C. Stroh, and K. Schulze-osthoff, Unique and overlapping substrate specificities of caspase-8 and caspase-10, Oncogene, vol.25, issue.1, pp.152-161, 2006.
Y. Tsuchiya, O. Nakabayashi, and H. Nakano, FLIP the Switch: Regulation of Apoptosis and Necroptosis by cFLIP, International Journal of Molecular Sciences, vol.8, issue.12, pp.30321-30362, 2015.
DOI : 10.3390/cancers3021639
A. Golks, D. Brenner, C. Fritsch, P. H. Krammer, and I. N. Lavrik, , a New Regulator of Death Receptor-induced Apoptosis, Journal of Biological Chemistry, vol.60, issue.15, pp.14507-14520, 2005.
DOI : 10.1074/jbc.271.15.8991
K. Schleich, J. H. Buchbinder, S. Pietkiewicz, T. Kahne, U. Warnken et al., Molecular architecture of the DED chains at the DISC: regulation of procaspase-8 activation by short DED proteins c-FLIP and procaspase-8 prodomain, Cell Death & Differentiation, vol.11, issue.4, pp.681-94, 2016.
DOI : 10.1093/nar/gkp889
C. Pop, A. Oberst, M. Drag, B. J. Van-raam, S. J. Riedl et al., induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity, Biochemical Journal, vol.322, issue.3, pp.447-57, 2011.
M. A. Hughes, I. R. Powley, R. Jukes-jones, S. Horn, M. Feoktistova et al., Co-operative and Hierarchical Binding of c-FLIP and Caspase-8: A Unified Model Defines How c-FLIP Isoforms Differentially Control Cell Fate, Molecular Cell, vol.61, issue.6, pp.834-883, 2016.
L. S. Dickens, R. S. Boyd, R. Jukes-jones, M. A. Hughes, G. L. Robinson et al., A Death Effector Domain Chain DISC Model Reveals a Crucial Role for Caspase-8 Chain Assembly in Mediating Apoptotic Cell Death, Death Effector Domain Chain DISC Model Reveals a Crucial Role for Caspase-8 Chain Assembly in Mediating Apoptotic Cell Death, pp.291-305, 2012.
C. Pop, A. Oberst, M. Drag, . Van-raam, J. Bram et al., induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity, Biochemical Journal, vol.322, issue.3, pp.447-457, 2011.
T. Kataoka, R. C. Budd, N. Holler, M. Thome, F. Martinon et al., The caspase-8 inhibitor FLIP promotes activation of NF-??B and Erk signaling pathways, Current Biology, vol.10, issue.11, pp.640-648, 2000.
T. Kataoka and J. Tschopp, N-Terminal Fragment of c-FLIP(L) Processed by Caspase 8 Specifically Interacts with TRAF2 and Induces Activation of the NF-??B Signaling Pathway, Molecular and Cellular Biology, vol.24, issue.7, pp.2627-2663, 2004.
A. Koenig, I. A. Buskiewicz, K. A. Fortner, J. Q. Russell, T. Asaoka et al., Cleavage Product p43FLIP Promotes Activation of Extracellular Signal-regulated Kinase (ERK), Nuclear Factor ??B (NF-??B), and Caspase-8 and T Cell Survival, Journal of Biological Chemistry, vol.54, issue.2, pp.1183-91, 2014.
S. M. Kavuri, P. Geserick, D. Berg, D. P. Dimitrova, M. Feoktistova et al., Cellular FLICE-inhibitory Protein (cFLIP) Isoforms Block CD95- and TRAIL Death Receptor-induced Gene Induction Irrespective of Processing of Caspase-8 or cFLIP in the Death-inducing Signaling Complex, Journal of Biological Chemistry, vol.61, issue.19, pp.16631-16677, 2011.
DOI : 10.1074/jbc.M206882200
D. Siegmund, A. Wicovsky, I. Schmitz, K. Schulze-osthoff, S. Kreuz et al., Death Receptor-Induced Signaling Pathways Are Differentially Regulated by Gamma Interferon Upstream of Caspase 8 Processing, Molecular and Cellular Biology, vol.25, issue.15, pp.6363-79, 2005.
J. Majkut, M. Sgobba, C. Holohan, N. Crawford, A. E. Logan et al., Differential affinity of FLIP and procaspase 8 for FADD???s DED binding surfaces regulates DISC assembly, Nature Communications, vol.26, p.3350, 2014.
DOI : 10.1093/bioinformatics/btq444
O. Micheau and J. Tschopp, Induction of TNF Receptor I-Mediated Apoptosis via Two Sequential Signaling Complexes, Cell, vol.114, issue.2, pp.181-90, 2003.
DOI : 10.1016/S0092-8674(03)00521-X
URL : https://hal.archives-ouvertes.fr/inserm-00527105
E. Varfolomeev, T. Goncharov, A. V. Fedorova, J. N. Dynek, K. Zobel et al., c-IAP1 and c-IAP2 Are Critical Mediators of Tumor Necrosis Factor ?? (TNF??)-induced NF-??B Activation, Journal of Biological Chemistry, vol.7, issue.36, pp.24295-24304, 2008.
J. N. Dynek, T. Goncharov, E. C. Dueber, A. V. Fedorova, A. Izrael-tomasevic et al., c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling, The EMBO Journal, vol.7, issue.24, pp.4198-209, 2010.
DOI : 10.1038/nsmb.1605
M. J. Bertrand, S. Milutinovic, K. M. Dickson, W. C. Ho, A. Boudreault et al., cIAP1 and cIAP2 Facilitate Cancer Cell Survival by Functioning as E3 Ligases that Promote RIP1 Ubiquitination, ) cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination, pp.689-700, 2008.
T. L. Haas, C. H. Emmerich, B. Gerlach, A. C. Schmukle, S. M. Cordier et al., Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and??Is Required for TNF-Mediated Gene Induction, Molecular Cell, vol.36, issue.5, pp.831-875, 2009.
C. K. Ea, L. Deng, Z. P. Xia, G. Pineda, and . Chen, Activation of IKK by TNF?? Requires Site-Specific Ubiquitination of RIP1 and Polyubiquitin Binding by NEMO, Molecular Cell, vol.22, issue.2, pp.245-57, 2006.
F. Ikeda, Y. L. Deribe, S. S. Skanland, B. Stieglitz, C. Grabbe et al., SHARPIN forms a linear ubiquitin ligase complex regulating NF-??B activity and apoptosis, Nature, vol.2, issue.7340, pp.637-678, 2011.
DOI : 10.1038/nprot.2007.261
A. Kanayama, R. B. Seth, L. Sun, C. K. Ea, M. Hong et al., TAB2 and TAB3 Activate the NF-??B Pathway through Binding to Polyubiquitin Chains, Molecular Cell, vol.15, issue.4, pp.535-583, 2004.
S. Rahighi, F. Ikeda, M. Kawasaki, M. Akutsu, N. Suzuki et al., Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-??B Activation, Cell, vol.136, issue.6, pp.1098-109, 2009.
DOI : 10.1016/j.cell.2009.03.007
Y. Dondelinger, M. Darding, M. J. Bertrand, and H. Walczak, Poly-ubiquitination in TNFR1-mediated necroptosis, Cellular and molecular life sciences : CMLS, pp.2165-76, 2016.
I. N. Lavrik, T. Mock, A. Golks, J. C. Hoffmann, S. Baumann et al., CD95 Stimulation Results in the Formation of a Novel Death Effector Domain Protein-containing Complex, Journal of Biological Chemistry, vol.109, issue.39, pp.26401-26409, 2008.
DOI : 10.1182/blood-2006-03-011585
F. Gonzalvez, D. Lawrence, B. Yang, S. Yee, R. Pitti et al., TRAF2 Sets a Threshold for Extrinsic Apoptosis by Tagging Caspase-8 with a Ubiquitin Shutoff Timer, Molecular Cell, vol.48, issue.6, pp.888-99, 2012.
Z. Jin, Y. Li, R. Pitti, D. Lawrence, V. C. Pham et al., Cullin3-Based Polyubiquitination and p62-Dependent Aggregation of Caspase-8 Mediate Extrinsic Apoptosis Signaling, Cell, vol.137, issue.4, pp.721-756, 2009.
E. Lafont, C. Kantari-mimoun, P. Draber, D. De-miguel, T. Hartwig et al., The linear ubiquitin chain assembly complex regulates TRAIL???induced gene activation and cell??death, The EMBO Journal, vol.36, issue.9, pp.1147-1166, 2017.
DOI : 10.15252/embj.201695699
Z. Jin and W. S. El-deiry, Distinct Signaling Pathways in TRAIL- versus Tumor Necrosis Factor-Induced Apoptosis, Molecular and Cellular Biology, vol.26, issue.21, pp.8136-8184, 2006.
S. P. Cullen, . Henry, M. Conor, . Kearney, J. Conor et al., Fas/CD95-Induced Chemokines Can Serve as ???Find-Me??? Signals for Apoptotic Cells, Molecular Cell, vol.49, issue.6, pp.1034-1048
S. Kleber, I. Sancho-martinez, B. Wiestler, A. Beisel, C. Gieffers et al., Yes and PI3K Bind CD95 to Signal Invasion of Glioblastoma, Cancer Cell, vol.13, issue.3, pp.235-283, 2008.
DOI : 10.1016/j.ccr.2008.02.003
M. Malleter, S. Tauzin, A. Bessede, R. Castellano, A. Goubard et al., CD95L Cell Surface Cleavage Triggers a Prometastatic Signaling Pathway in Triple-Negative Breast Cancer, CD95L Cell Surface Cleavage Triggers a Prometastatic Signaling Pathway in Triple-Negative Breast Cancer, pp.6711-6721, 2013.
P. Schneider, N. Holler, J. L. Bodmer, M. Hahne, K. Frei et al., Conversion of Membrane-bound Fas(CD95) Ligand to Its Soluble Form Is Associated with Downregulation of Its Proapoptotic Activity and Loss of Liver Toxicity, The Journal of Experimental Medicine, vol.8, issue.8, pp.1205-1218, 1998.
T. Suda, H. Hashimoto, M. Tanaka, T. Ochi, and S. Nagata, Membrane Fas Ligand Kills Human Peripheral Blood T Lymphocytes, and Soluble Fas Ligand Blocks the Killing, The Journal of Experimental Medicine, vol.54, issue.12, pp.2045-50, 1997.
I. Lang, A. Fick, V. Schafer, T. Giner, D. Siegmund et al., Signaling Active CD95 Receptor Molecules Trigger Co-translocation of Inactive CD95 Molecules into Lipid Rafts, Journal of Biological Chemistry, vol.103, issue.28, pp.24026-24068, 2012.
T. S. Soderstrom, S. D. Nyberg, and J. E. Eriksson, CD95 capping is ROCK-dependent and dispensable for apoptosis, Journal of Cell Science, vol.118, issue.10, pp.2211-2234, 2005.
DOI : 10.1242/jcs.02343
T. Vargo-gogola, H. C. Crawford, B. Fingleton, and L. M. Matrisian, Identification of novel matrix metalloproteinase-7 (matrilysin) cleavage sites in murine and human Fas ligand, Archives of Biochemistry and Biophysics, vol.408, issue.2, pp.155-61, 2002.
R. Herrero, O. Kajikawa, G. Matute-bello, Y. Wang, N. Hagimoto et al., The biological activity of FasL in human and mouse lungs is determined by the structure of its stalk region, The Journal of clinical investigation, pp.1174-90, 2011.
R. Alonso, C. Mazzeo, M. C. Rodriguez, M. Marsh, A. Fraile-ramos et al., Diacylglycerol kinase alpha regulates the formation and polarisation of mature multivesicular bodies involved in the secretion of Fas ligand-containing exosomes in T lymphocytes, Cell death and differentiation, pp.1161-73, 2011.
N. R. Bianco, S. H. Kim, A. E. Morelli, and P. D. Robbins, Modulation of the Immune Response Using Dendritic Cell-Derived Exosomes, Methods Mol Biol, vol.380, pp.443-55, 2007.
DOI : 10.1007/978-1-59745-395-0_28
A. J. Abusamra, Z. Zhong, X. Zheng, M. Li, T. E. Ichim et al., Tumor exosomes expressing Fas ligand mediate CD8+ T-cell apoptosis, Blood Cells, Molecules, and Diseases, vol.35, issue.2, pp.169-73, 2005.
DOI : 10.1016/j.bcmd.2005.07.001
K. Bajou, H. Peng, W. E. Laug, C. Maillard, A. Noel et al., Plasminogen activator inhibitor-1 protects endothelial cells from FasLmediated apoptosis, Cancer Cell, pp.324-358, 2008.
E. J. Steller, I. H. Borel-rinkes, and O. Kranenburg, How CD95 stimulates invasion, Cell Cycle, pp.3857-3862, 2011.
DOI : 10.4161/cc.10.22.18290
URL : http://www.tandfonline.com/doi/pdf/10.4161/cc.10.22.18290?needAccess=true
N. Khadra, L. Bresson-bepoldin, A. Penna, B. Chaigne-delalande, B. Segui et al., CD95 triggers Orai1-mediated localized Ca2+ entry, regulates recruitment of protein kinase C (PKC) ??2, and prevents death-inducing signaling complex formation, Proceedings of the National Academy of Sciences, vol.16, issue.12, pp.19072-19079, 2011.
DOI : 10.1038/cdd.2009.111
B. J. Chang, A. B. Samal, J. Vlach, T. F. Fernandez, D. Brooke et al., Identification of the Calmodulin-Binding Domains of Fas Death Receptor, PLOS ONE, vol.10, issue.1???3, 2016.
DOI : 10.1371/journal.pone.0146493.s011
Y. J. Lai, V. T. Lin, Y. Zheng, E. N. Benveniste, and F. T. Lin, The Adaptor Protein TRIP6 Antagonizes Fas-Induced Apoptosis but Promotes Its Effect on Cell Migration, Molecular and Cellular Biology, vol.30, issue.23, pp.5582-96, 2010.
E. J. Steller, L. Ritsma, D. A. Raats, F. J. Hoogwater, B. L. Emmink et al., The death receptor CD95 activates the cofilin pathway to stimulate tumour cell invasion, EMBO reports, vol.60, issue.9, pp.931-938, 2011.
DOI : 10.1002/ijc.23090
B. C. Barnhart, P. Legembre, E. Pietras, C. Bubici, G. Franzoso et al., CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells, The EMBO Journal, pp.3175-3185, 2004.
T. G. Bivona, H. Hieronymus, J. Parker, K. Chang, M. Taron et al., FAS and NF-??B signalling modulate dependence of lung cancers on mutant EGFR, Nature, vol.28, issue.7339, pp.523-526, 2011.
DOI : 10.1038/onc.2009.135
L. Chen, S. Park, A. V. Tumanov, A. Hau, K. Sawada et al., CD95 promotes tumour growth, Nature, vol.14, issue.7297, pp.492-496, 2010.
DOI : 10.1038/nprot.2008.80
URL : http://www.nature.com/nature/journal/v475/n7355/pdf/nature10221.pdf
G. Bellone, C. Smirne, A. Carbone, K. Mareschi, L. Dughera et al., Production and pro-apoptotic activity of soluble CD95 ligand in pancreatic carcinoma, Clin Cancer Res, vol.6, pp.2448-55, 2000.
M. Tanaka, T. Suda, K. Haze, N. Nakamura, K. Sato et al., Fas ligand in human serum, Nature Medicine, vol.2, issue.3, pp.317-322, 1996.
H. Hashimoto, M. Tanaka, T. Suda, T. Tomita, K. Hayashida et al., Soluble Fas ligand in the joints of patients with rheumatoid arthritis and osteoarthritis, Arthritis & Rheumatism, pp.657-662, 1998.
H. Das, S. Imoto, T. Murayama, K. Kajimoto, T. Sugimoto et al., Levels of soluble FasL and FasL gene expression during the development of graft-versus-host disease in DLT-treated patients, British Journal of Haematology, vol.148, issue.4, pp.795-800, 1999.
Y. Kanda, Y. Tanaka, K. Shirakawa, T. Yatomi, N. Nakamura et al., Increased soluble Fas-ligand in sera of bone marrow transplant recipients with acute graft-versus-host disease, Bone marrow transplantation, pp.751-755, 1998.
. Tomokuni, . Otsuki, . Isozaki, . Kita, . Ueki et al., Serum levels of soluble Fas ligand in patients with silicosis, Clinical and Experimental Immunology, vol.68, issue.3, pp.441-444, 1999.


text:
Q: iptables with DNAT and multiple gateways: How to route replies to correct gateway? I have a problem setting up iptables rules and routes on a Linux client for a scenario with DNAT and multiple gateways:
We have two gateways to the Internet. The first has a fixed IP, the second offers a better bandwidth. Both gateways do SNAT for outgoing traffic from our private network.
On the first gateway with the fixed IP I've set up port forwarding for port 22 so that all SSH traffic will be forwarded to my Linux client.
That works fine.
But only if I use this first gateway as default route on the Linux client.
When I switch the Linux client to the second gateway as default route, incoming SSH connections no longer work.
How can I setup the Linux client to send reply packets related to incoming SSH connections to the first gateway, but all other traffic to the second gateway?

A: I found a solution in the accepted answer to the question "Route return traffic to correct gateway depending on service".
I've implemented these rules on my Linux client:
# Default route is second gateway:
ip route add default via 10.0.0.2

# Create a routing table "FIXED" using our fixed IP gateway
echo "200 FIXED" >>/etc/iproute2/rt_tables
ip route add default table FIXED via 10.0.0.1

# Create a rule to route any packets marked "42" through FIXED:
ip rule add fwmark 42 table FIXED

# Finally, the iptables rule:
# Any outgoing traffic from source port 22 of my Linux client
# that has a destination inside our private network (10.0.0.0/24)
# is marked "42" (and therefore goes to FIXED):
iptables -t mangle -A OUTPUT ! -d 10.0.0.0/24 \
                             -p tcp -m tcp --sport 22 \
                             -j MARK --set-mark 42

redpajama_set_name: RedPajamaStackExchange


I'm surprised to learn that the two albums I've released over the last 12 months, "CYCLS" and "Everything is connected", are both nominated for the Norwegian "Spellemann" awards (our version of the Grammy awards). Both are listed in the "Electronica/Dance" category, alongside my old label-mate from the Smalltown Supersound days – Kim Hiorthøy – and his album "Dogs". Strangely enough our biggest national success of the year – the good man Todd Terje and his bestseller "It's album time" – is not included at all in this year's nominations. Spokepersons from the award committee explain this by referring to the fact that it is the labels themselves that have to register their releases in order to be included in the nomination process. Whatever the reasons, I'm sending a big shout-out to Terje and all the other heads on the Norwegian scene who have been releasing great music throughout the year, and hope 2015 will be even better. You can check out my nominated albums through the Bandcamp players above.


The in-flight magazine of Aegean Airlines, BLUE, features an extensive coverage of the SNFCC and photographer Vassilis Makris's photographic project titled "Incarnation." The magazine also hosts an interview with the Greek National Opera's Artistic Director on the GNO's future plans once this moves to its new home.
Newsbeast presents the unique architectural, construction, and operational challenges and opportunities the SNFCC presents, through the eyes of its own people.
Kathimerini's editor, Margarita Pournara, writes an op-ed about the responsibility we all bear to protect the SNFCC and all major public interventions, as a means of safeguarding our future.
On January 15th, the Mobile Medical Units will visit the island of Agathonisi to provide extensive medical services, free of charge, to its permanent residents.
SNF's Co-President Andreas Dracopoulos contributes to Kathimerini's Sunday edition with an op-ed, on the need to rebuild Greece by going back to basics and working on a culture change.
The Royal Institute of International Affairs is awarded a Cornerstone Contribution of £3m by the Stavros Niarchos Foundation towards the Chatham House Second Century Initiative to support the expansion and renovation of the institute's ground floor.
On Monday, December 14th, 2015 the Visitors Center of the Stavros Niarchos Foundation Cultural Center (SNFCC) turned into an open-air concert space for the Christmas celebration of the people working at the SNFCC construction site!
The Board of Directors of the SNF announced today three new grants, totaling $500,000, to support initiatives that assist U.S. veterans.


text:
Global Grants and Opportunities for Faculty
A significant part of the mission of the IANR Global Engagement Office is to support faculty in the continuation and generation of international collaborations, field work, fellowships, and more. This aids in their own professional and academic development as well as helps them to internationalize the curriculum to help prepare students to thrive in our globalized world. Please see the current opportunities below and contact us if you have questions about these or other international endeavors.
SPRINT Initiative - São Paulo Researchers in International Collaboration 2021 Call for Proposals
Due January 31, 2022
Nebraska's Institute of Agriculture and Natural Resources (IANR) in partnership with the São Paulo Research Foundation (FAPESP) announce the call for proposals under the SPRINT initiative - São Paulo Researchers in International Collaboration. The call aims to promote the engagement of researchers affiliated with higher education and research institutions in the State of São Paulo in partnership with researchers abroad in order to: further develop qualitatively the ongoing research projects and work cooperatively, with the purpose of elaborating joint research projects for the medium and long term. FAPESP and IANR (Agricultural Research Division and IANR Global Engagement) will each fund the equivalent of US $10,000 per proposal per year (total of US $20,000 per year). Interested in applying? Contact Liana Calegare for more details.
Awards: 1 award of $20,000 for a maximum 24 months
Global Experience Innovation Fund
Due: Check back for possible renewal of this opportunity.
The Education Abroad Office, in partnership with the Office of Global Strategies, has created a Global Experiences Innovation Fund to support faculty and staff in the development and promotion of innovative virtual, on-campus or "glocal," and domestic programs for Summer 2021 and Fall 2021. In addition, the Fund will support faculty and staff efforts to integrate education abroad more seamlessly into the curriculum. Interested faculty/staff are invited to submit 1) a statement of interest describing their vision for the program (suggested 500 word limit), 2) a brief letter of support from the chair of the academic unit and/or staff member's direct supervisor, and 3) a budget request.
Awards: Award amounts will range from $1,000 to $8,000, with consideration given to higher amounts if warranted.
For further opportunities across more disciplines, visit the UNL Office of Global Strategies grants page.

redpajama_set_name: RedPajamaCommonCrawl


Following the Return to Douala special feature (Dec 2014 / Jan 2015), where we went looking for the memorial to those lost in 1962 aboard G-ARUD, I was contacted by Amanda Lane.
Amanda is the daughter of Captain Allen Frost, one of those lost onboard that fateful night in March 1962.
Though never exactly sure where her father was buried, until the web page, Amanda had been passed two photos of the memorial by her family. These look to have been taken a few weeks after the accident when the memorial was completed.
Amanda has kindly shared these photos with us and they show us that those lost on board were respectfully remembered with a very striking memorial.
As we have seen, the memorial has aged, but when it was finished in 1965 it dominated the landscape next to the runway at Douala.
The memorial has plaques to remember both the passengers and crew.
The Crew plaque is shown above.
The plaques for the passengers are on 3 sides of the memorial base, the front being for the memorial dedication as can be seen to the left.
The wreath is being placed by Alan Bartlett at the memorial's dedication to remember those lost.


This article shows you to fit a thermostatic mixer shower with a simple pushfit bracket that can be installed at 1st fix plumbing I.e. Before tiling.
2 x 15mm inlets for the hot & cold water supplies into the valve (this one features pushfit connections) that can face up or down depending on where the supply pipes come from (above or below).
2 x ¾" male threaded outlets at 150mm centres (which you screw the shower valve onto).
Easy push fit connections allow for a quick installation with no compression or solder joints.
Plastic construction of this particular bracket is not as strong as metal alternatives.
Not all plumbers like pushfit connections but in my experience they do not develop a leak over time or suffer from very slow leaks as compression fittings can – if it leaks you will know about it when you 1st test it!
In this instance the hot and cold pipework drops down to the bracket (but it can be rotated if the pipes come up from the floor) and is connected with 2 x standard pushfit connections.
PS Please see here for a compression version of the same valve.
These connections must be thoroughly checked for leaks before the pipework is entombed behind the shower wall.
This is done by putting the valve under pressure by turning the water on and capping the shower end of the bracket – this is done with the stop caps supplied (as in the picture above) or with the shower valve itself.
In the picture above you can see that I have screwed a piece of wood to the wall behind the bracket in order to set it at the correct depth. I have also used plastic packers to make micro-adjustments to ensure the bracket is level & square to the finished wall surface.
Before boarding out the whole wall, I temporarily connect the shower valve to the bracket and use an offcut of plasterboard and a wall tile to check whether the bracket is set at the correct distance back from the wall (you will have to estimate 2-3mm for the depth of the tile adhesive here).
At this stage it is vitally important that the threads protrude far enough out beyond the surface of the tiles so that the chrome cover caps and the shower valve can be screwed on and nipped up tight before bottoming out.If the valve is set too far forward it is not usually the end of the world as the threads may be a bit on show, but if it is set too far back into the wall, then the shower valve may collide with the chrome collars before it has tightened up sufficiently to form a watertight seal. This will make it constantly leak, unless you forego the chrome collars.Please see here for an example (mid way through this article in the box).
The bathroom walls are then boarded and tanked prior to tiling.
The holes around the male threads are filled with silicon sealant to form a waterproof barrier to mitigate against the risks of water penetration behind the tiles.
These chrome collars attach in a slightly different manner than most other concealed shower brackets in that plastic nuts are first screwed onto the threads before the chrome collars are slid over them.
They are held in place by friction, and are therefor more likely to come loose than with collars that screw onto the thread directly, but they are designed in such a way that they obstruct the view of the exposed thread (which is normally left exposed with other concealed shower brackets).
This bracket also has a filter that you can see inside the male thread of the bracket.
The 2 x male ¾" threads which the shower valve attaches onto are plastic on this model, so there is a small chance of the threads stripping if the metal threads of the shower valve nuts are overtightened – When attaching the shower valve just nip up the connections until the rubber washer grips.


What is starting to dawn on many people is that this change is anything but "A fairer treatment for FBT on cars".
Furthermore, the people impacted by the change will not be the "top end of town" as has been maintained.
The Government wants to ensure that the FBT exemption for vehicles is targeted to actual business use, rather than including personal use, by removing the statutory formula method for both salary-sacrificed and employer provided cars. However, this method is also heavily utilised by many small businesses operating through either a trust or company as well as the vast majority of people who salary-sacrifice a vehicle.
The announcement applies to new contracts entered into after 16 July 2013.
Until the election is "run and won", our advice is for NOBODY to enter into any salary-sacrificing arrangements. Furthermore, small businesses looking to purchase a new vehicle for use by the owners should also defer any purchases.
If you need further clarification on these changes, please contact Ellingsen Partners.


Man has a sophisticated manner of examination. His mind draws him to a place of comfort and at the same may draw him to the place of agony. This book helps bring about man's attitude in relation to his environment, people and also, God Almighty. Most of these outward expressions are actually what is nursed within. Attitude is everything. It affects the character in ways we can't really imagine. Following man's behavioral pattern, the elements which give him attitudes is practically everything. What we consider an attitude, is what the Divine considers as "nature". Every attitude you see in this book has to do with nature, that is who we are an in most cases, who we become in the end. Love being the alpha attitude is what we need as a consciousness of our nature to live in accordance with Abba (FATHER).
Unforgiveness can cause cancer in a family, in a union, among brethren in Christ and anywhere in the world. A lot of people claim to be hurt and deliberately decide not to forgive brethren or comrade and they live like that for years with themselves. When they see those who offended them they become furious and sometimes transfer aggression. But we forget we have a Heavenly Father who lives in us and knows all things. We hardly see that we have offended God but worry about those who have offended us. God forgives both you and your offender but u got to let go. We need to be conscious of our attitude of forgiveness to save homes and make the world a better place.
Love is that attitude that always brings peace and makes people stronger than what they were. We have forgotten that God is Love and he who knows not love knows not God. This attitude breaks the ice for all to live in harmony. It births a new you.
-	Can we leave in this Earth realm without being thought and without us studying?
-	Can love actually birth peace in a man's character and Leave in peace with God?
-	Will an unforgiving heart bring genuine unity?
Bantar-Shey is an aspiring young man living in the city of Douala, Cameroon. He is inspired by the works of God and led by the Holy Spirit, to write this piece of revelation for you.
He holds a Bachelor's degree in Technology in Marketing and a Higher National Diploma in Marketing.
He is also a Minister of the Gospel, an Evangelist of our Lord and Savior Jesus Christ, the son of God.


Sunday 25th March – mothers Day saw the start of the new Piles Sunday market. In an effort to promote local businesses and make the playa an area for permanent living – the town hall organised this first Sunday market. At 7 o'clock the stall holders set up in eager anticipation of the day ahead.
For those of you who don't know Piles it is a typically Spanish town outside of Oliva with a population of 2000. The playa population is around 150 of which I am one. The town is very popular with Spanish and French holidaymakers due to the history during the civil war.
The organisers could not have asked for as better day – the weather was perfect and one of the hottest days of the year. By 10Am the market had started to get busy and by 12 (I realised the clocks had gone forward so missed the hour between) the market was teaming.
The stalls sell everything from fruit and veg to jeans and t-shirts, with electrical goods, fabrics, paintings and pots and pans thrown in for good measure. Looking around all the bars were full – so you could say the market has had its desired result. If you want to come down the market starts at 9AM every Sunday, but you'd better come early to get the best seats.
While you are there why not drop into bar Spinach at the entrance to the playa – Next Sunday Francois will be serving Bacons sandwiches and a coffee for 3€ , so come on down and enjoy your Sundays with a new alternative to Pedreguer or Potries Sunday markets – with a much more friendly atmosphere.


Send us an email with the product/s and quantities you're interested in, and we'll get back to you quickly with pricing and order details.
Email your artwork to hello@engravegoods.com We'll create a free mockup and send it to you for approval.
We'll get to work making your custom leather goods. We take pride in delivering on time straight to your doorstep!


The series consists of six separate international races. All races are financial, legal and sporting independent. The General Regulations and the UCI Rules apply to all races.
The total result consists of five Qualifying Run results and five Final Run results. The results will be published on www.ixsdownhillcup.com.
Every rider has to use the registration form on www.ixsdownhillcup.com. For registration please include the UCI ID.
The transfer/delivery of a starting slot to other riders is always precluded.
Registration and payment deadline is always on Tuesday 24h00 before the races. If the registered starter cannot attend the race, they have no right to reclaim the registration fee. If the registration quota is reached the organisers reserve the right to close registration in advance. There is no claim for a late registration on site.
The registration will be valid when the registration process is completed and the payment was made. If the fee is received on the account a confirmation e-mail will be sent.
The fee to attend the race is Euro 60, if received before the registration is closed. This fee includes transportation from the finish area to the start via lift/gondola.
After the registration deadline the fee increases to Euro 80.
Every rider gets a new number board at every race. Riders must display their handlebar number while training as well as their back number during the qualifying round and the final. Number plates must be fixed in front of the handlebar and should readable throughout the competition. It is strictly prohibited to alter the number boards in any manner.
Start numbers may be reserved for registered riders and allocated according to UCI rankings and iXS European Downhill Cup rankings.
The race is open to all UCI-licenced riders.
The Qualifying Run takes the form of a timed run over the course by each rider. Riders who are DSQ or DNS in the qualifying round can not enter the main event. All other riders will be able to enter the Final Run.
The Final Run of the Elite Men category is divided in Small Final and Super Final.
The Super Final of the Elite Men category is disputed by 30 riders. That means 30 fastest riders will be qualified for the Super Final run. All other riders will enter the Small Final.
Riders ranked in the top 10 Elite Men on the current UCI standings (attendant riders) and the top 3 Elite Men on the current European Cup standings are "protected" for the Super Final. They must start in the qualifying round but qualify automatically for the Super Final in any case. If the times of the protected riders are not among the 30 best times Elite Men, they will race the Super Final in addition to the 30 Elite Men already qualified.
Riders in the Qualifying Run and Final Run start at intervals of 30 seconds, except the last ten riders of Elite Women and Elite Men categories will start at intervals of 1 minute. The intervals for the Super Final run will be determined separate.
All starting times are binding. In case of delays/interruptions the starting order is to be maintained.
For the Final Run, the starting order will be in accordance with the results of the Qualifying Run. The start order for the Elite Men Super Final is determined on the basis of the reverse result of the final round, the fastest rider starting last. The order in the Qualifying Run complies with the current UCI-ranking and the current total results of the series.
All competitors must ride two practice runs during the obligatory training session. The training runs will be registered and the riders can start at the Qualifying Run only with the registration. Each obligatory training run must begin from the official starting point and must end in the finish area.
On Saturday a training period will be provided for best 80 ranked men, best 10 ranked women, best 5 Masters and best 5 U19 male riders of the current UCI ranking resp. European Cup standings.
On Sunday the Top Training period will be provided for best 80 ranked men, best 10 women, best 5 Masters and best 5 U19 male riders of the result of the Qualifying Run. Thereby all Super Final riders, the 3 best ranked women, the 3 best ranked Masters and the 3 best ranked U19 male rider of the top training list from Saturday are "protected".
In addition to this agreement the organization refers to the safety rules and racing agreement defined by national cycling federations and the UCI.
The result of the Elite Men category will compose of the Super Final of top 30 (plus "protected" riders) and the Small Final result. The ranking is determined by the places of the riders. That means, the sheet of the Small Final will be inserted behind the riders of the Super Final. Therefore the best ranked rider of the Small Final will be placed as the rank number of participants of the Super Final plus one.
The first five riders will be honoured with a ceremony, 30 min after the race. Riders not present for the awards ceremony will forfeit trophies and/or prizes.
Prize money for the Elite Men and Elite Women classes are paid according to the UCI provisions.
The series prize money will be paid directly after the ceremony on presentation of a valid licence at the finish area. The organization is not responsible for paying the prize money at a later date. The prizes listed above are gross prizes. Due to legal requirements the series´ organization is bounded to transfer the tax, therefore only net amounts will be paid.
The overall result consists of the results of five Qualifying Runs and five Final Runs. That means one Qualifying Run result and one Final Run result will be deleted. The discounted Qualifying Run and Final Run can stem from different events.
The UCI functionaries are responsible for submit the results for points of UCI.


A heavily pregnant Victoria is frustrated by both Albert and her mother's attempts to confine her to the Palace. Cumberland arrives in London, hoping that Victoria may die in childbirth, as he is still the heir Presumptive. Determined to show herself in public, Victoria goes for a drive and is accosted by an unhinged admirer, desperate to free her from her 'German tyrant'. Whilst Victoria is taken aback, she is resolute that it will not frighten her and despite Albert's misgiving, goes out again.
After a series of assassination attempts, the queen is forced to seek sanctuary far from the palace. She and Albert travel to the Scottish Highlands, an area that has always fascinated her, but proves to be far from the romantic retreat she had fantasised about. However, travelling incognito gives both the royal couple and their servants a freedom they do not often experience.
Albert resents Lehzen's influence over the queen, and fears she is putting the health of their child at risk. The prince also unwittingly creates problems for Peel, who is facing the most important battle of his political career as he takes a stand against the corn laws, only to find that Albert has played into their enemies' hands. When tragedy strikes, personal and political sacrifices must be made. Last in the series.
As news of the horrific famine in Ireland reaches the Queen, Victoria is adamant that her government should be doing more to help. However, Prime Minister Peel is trapped, knowing that to send food to the Irish would destabilise his party and jeopardise his career. With Albert blinded by his trust in Peel, Victoria begins to question her own convictions.
Prince Albert arrives in England for the first time, and he and Victoria take an instant dislike to each other in an awkward first encounter. Below stairs, Albert's valet clashes with the royal servants, while Skerrett is visited by a girl in need of money.
The queen becomes pregnant, and declares that Albert will become head of state in the event of her death. The developments outrage members of the Tory party, who fear a German prince holding sway over the nation and make arrangements to disrupt his visit to the industrial north. The consort finds an unlikely ally in Sir Robert Peel, who seeks royal approval for the rapidly developing railway. At first, Victoria does not approve, but soon changes her mind when she experiences Peel's creation for herself.
Albert feels he needs a greater role in public affairs, and becomes involved in the anti-slavery movement. Victoria matches wills with the Duke of Sussex to see that her husband is granted more respect, while Skerrett faces a dilemma when she realises that the only person who can save her cousin and child from certain death is the man she trusts the least.
Discontent is growing in the country, and upon hearing the pleas of a silk weaver of Spitalfields, Victoria decides she must help. Against Peel and Albert's advice, she hatches a plan: a fantastic medieval ball at the Palace, where the attendees have to wear costumes made from Spitalfields silk.
Concerned that the pending marriage of King Louis Philippe of France's son to the Spanish Queen will form a dangerous alliance, Victoria sets sail on her first voyage to the continent in an attempt to deter the wily French King.
Picking up a month after the birth of her first child, the new series sees Queen Victoria surprise the court when she insists on returning to her duties as soon as possible.Having taken charge in her absence, adoring new father Albert decides not to trouble his wife with worrying news regarding the British soldiers in Afghanistan. However, as the reports worsen, Victoria grows increasingly suspicious that he and Prime Minister Robert Peel are hiding something from her.Determined to reclaim her place with characteristic impulsiveness, Victoria brings in the formidable Duchess of Buccleuch as her new Mistress of the Robes and demands that former chef, Francatelli, return to the palace kitchens.Meanwhile, Albert's family descend on the palace for the Christening of baby Vicky and their dynastic plotting only intensifies Victoria's sense of frustration. Convinced that the truth is being kept from her, Victoria seeks answers from the Duke of Wellington.
Lord Melbourne's resignation as Prime Minister leaves Victoria devastated. As Lord Melbourne's popularity in the house wanes, the Tories eagerly await their imminent triumph, while the Duke of Cumberland views it as a chance to prey on his niece's vulnerability.
The royal court celebrates the birth of the Queen's second child, but Victoria alone is unhappy as she struggles to bond with her newborn son. A crisis compels Albert to return to Coburg, separating the couple for the first time since their wedding. Skerrett makes a disastrous mistake, while Drummond's relationship with Lord Alfred comes under threat.
The queen suspects that her husband is attracted to another woman, and discovers that she is pregnant with a second child - leaving her concerned that motherhood will dominate her life and reign, at the expense of any other possibilities. Below stairs, new dresser Cleary thinks that the palace is haunted, but Brodie believes there is a natural explanation for the events that have frightened her.


Rodney Williams is showing the world that what you don't hear can be just as important as what you do. Williams, who happens to have been born partially deaf, is the founder of Lisnr, the world leader in data-over-audio technology that allows businesses to use inaudible tones to securely transmit data.
Ticketmaster is already in the process of implementing Lisnr technology so concert-goers can use inaudible tones to enter venues with little more than their smartphones — No QR codes or paper ticket barcodes required. Williams envisions a future where Lisnr's inaudible tones replace your wallet, your work badge, and your house and car keys, a future they're in the process of bringing to life at their new Cincinnati headquarters.
But Williams doesn't just see data delivered over sound in an interesting way — he also has a different take on how to process information that's communicated person-to-person.
At Cincinnati Startup Week 2017, Williams was featured on a panel with Lisnr investor and CincyTech CEO Mike Venerable about the CincyTech-Lisnr funding story. Venerable referred to a time he gave Williams some business advice that Williams was initially resistant to. During the panel, Williams said, as a founder, he had to learn how to accept feedback. But he clarifies that accepting feedback wasn't about overcoming his own stubbornness — it's about learning to work backwards from the advice to identify the problem at the root, then find the best solution.
"You can't get emotional when someone tells you to do something. You really have to be able to strategize around why they're asking what they're asking," Williams explains.
Williams points out it's unfortunate that we're not taught in school how to dismantle the information we take in so we can see the true problem at hand and search for the right solution. He encourages people to push past seeing themselves as a finance person or a marketing person and to take a broader view of their position within a company.
Minda Honey once lived in Cincinnati for nine months where she made weekly visits to grocery store mecca, Jungle Jim's. She still dreams about their international food aisles.


text:
Q: Problem with import matplotlib.pyplot as plt in python (Anaconda - Spyder) i'm newbie in python but i don't know how to solve this problem
I need an histogram in my code. I use this:
import matplotlib.pyplot as plt
plt.hist(datos["Ozone"], bins=10)

Note: datos is a dataframe.
I tested with other more basic examples, but never show the graph of the histogram.
I think is a problem with the Console, but i don't know how solve the problem.

A: You have to write:
plt.show()

at the end to see your plot.
EDIT:
In case you are using jupyter notebooks, there is no need for plt.show(). You can just add two lines of code as follows:
import matplotlib.pyplot as plt
%matplotlib qt
%matplotlib inline
plt.hist(datos["Ozone"], bins=10)


text:
package com.thoughtworks.go.apiv3.rolesconfig;

import com.thoughtworks.go.api.ApiController;
import com.thoughtworks.go.api.ApiVersion;
import com.thoughtworks.go.api.CrudController;
import com.thoughtworks.go.api.base.OutputWriter;
import com.thoughtworks.go.api.representers.JsonReader;
import com.thoughtworks.go.api.spring.ApiAuthenticationHelper;
import com.thoughtworks.go.api.util.GsonTransformer;
import com.thoughtworks.go.apiv3.rolesconfig.representers.GoCDRolesBulkUpdateRequestRepresenter;
import com.thoughtworks.go.apiv3.rolesconfig.representers.RoleRepresenter;
import com.thoughtworks.go.apiv3.rolesconfig.representers.RolesRepresenter;
import com.thoughtworks.go.config.Role;
import com.thoughtworks.go.config.RolesConfig;
import com.thoughtworks.go.config.exceptions.EntityType;
import com.thoughtworks.go.config.update.GoCDRolesBulkUpdateRequest;
import com.thoughtworks.go.server.newsecurity.utils.SessionUtils;
import com.thoughtworks.go.server.service.EntityHashingService;
import com.thoughtworks.go.server.service.RoleConfigService;
import com.thoughtworks.go.server.service.result.HttpLocalizedOperationResult;
import com.thoughtworks.go.spark.Routes;
import com.thoughtworks.go.spark.spring.SparkSpringController;
import org.springframework.beans.factory.annotation.Autowired;
import org.springframework.stereotype.Component;
import spark.Request;
import spark.Response;

import java.io.IOException;
import java.util.function.Consumer;

import static com.thoughtworks.go.api.util.HaltApiResponses.*;
import static spark.Spark.*;

@Component
public class RolesControllerV3 extends ApiController implements SparkSpringController, CrudController<Role> {
    private final RoleConfigService roleConfigService;
    private final ApiAuthenticationHelper apiAuthenticationHelper;
    private final EntityHashingService entityHashingService;

    @Autowired
    public RolesControllerV3(RoleConfigService roleConfigService, ApiAuthenticationHelper apiAuthenticationHelper,
                             EntityHashingService entityHashingService) {
        super(ApiVersion.v3);
        this.roleConfigService = roleConfigService;
        this.apiAuthenticationHelper = apiAuthenticationHelper;
        this.entityHashingService = entityHashingService;
    }

    @Override
    public void setupRoutes() {
        path(controllerPath(), () -> {
            before("", mimeType, this::setContentType);
            before("/*", mimeType, this::setContentType);
            before("", mimeType, this::verifyContentType);
            before("/*", mimeType, this::verifyContentType);
            before("", mimeType, apiAuthenticationHelper::checkAdminUserAnd403);
            before("/*", mimeType, apiAuthenticationHelper::checkAdminUserAnd403);

            get("", mimeType, this::index);
            post("", mimeType, this::create);
            patch("", mimeType, this::bulkUpdate);

            get(Routes.Roles.NAME_PATH, mimeType, this::show);
            put(Routes.Roles.NAME_PATH, mimeType, this::update);
            delete(Routes.Roles.NAME_PATH, mimeType, this::destroy);
        });
    }

    @Override
    public String controllerBasePath() {
        return Routes.Roles.BASE;
    }

    public String index(Request req, Response res) throws IOException {
        String pluginType = req.queryParams("type");
        RolesConfig roles = roleConfigService.getRoles().ofType(pluginType);
        String etag = entityHashingService.md5ForEntity(roles);

        if (fresh(req, etag)) {
            return notModified(res);
        } else {
            setEtagHeader(res, etag);
            return writerForTopLevelObject(req, res, writer -> RolesRepresenter.toJSON(writer, roles));
        }
    }

    public String show(Request req, Response res) throws IOException {
        Role role = fetchEntityFromConfig(req.params("role_name"));

        if (isGetOrHeadRequestFresh(req, role)) {
            return notModified(res);
        } else {
            setEtagHeader(role, res);
            return writerForTopLevelObject(req, res, writer -> RoleRepresenter.toJSON(writer, role));
        }
    }

    public String create(Request req, Response res) {
        Role role = buildEntityFromRequestBody(req);

        haltIfEntityBySameNameInRequestExists(req, role);

        HttpLocalizedOperationResult result = new HttpLocalizedOperationResult();
        roleConfigService.create(SessionUtils.currentUsername(), role, result);

        return handleCreateOrUpdateResponse(req, res, role, result);
    }

    public String update(Request req, Response res) {
        Role roleFromServer = roleConfigService.findRole(req.params(":role_name"));
        Role roleFromRequest = buildEntityFromRequestBody(req);

        if (isRenameAttempt(roleFromServer, roleFromRequest)) {
            throw haltBecauseRenameOfEntityIsNotSupported("roles");
        }

        if (isPutRequestStale(req, roleFromServer)) {
            throw haltBecauseEtagDoesNotMatch("role", roleFromServer.getName());
        }

        HttpLocalizedOperationResult result = new HttpLocalizedOperationResult();
        roleConfigService.update(SessionUtils.currentUsername(), etagFor(roleFromServer), roleFromRequest, result);
        return handleCreateOrUpdateResponse(req, res, roleFromRequest, result);
    }

    public String destroy(Request req, Response res) throws IOException {
        Role role = fetchEntityFromConfig(req.params("role_name"));
        HttpLocalizedOperationResult result = new HttpLocalizedOperationResult();
        roleConfigService.delete(SessionUtils.currentUsername(), role, result);

        return renderHTTPOperationResult(result, req, res);
    }

    public String bulkUpdate(Request req, Response res) throws IOException {
        JsonReader jsonReader = GsonTransformer.getInstance().jsonReaderFrom(req.body());
        GoCDRolesBulkUpdateRequest bulkUpdateRequest = GoCDRolesBulkUpdateRequestRepresenter.fromJSON(jsonReader);
        HttpLocalizedOperationResult result = new HttpLocalizedOperationResult();
        roleConfigService.bulkUpdate(bulkUpdateRequest, SessionUtils.currentUsername(), result);
        if (result.isSuccessful()) {
            RolesConfig goCDRoles = roleConfigService.getRoles().ofType("gocd");
            return writerForTopLevelObject(req, res, writer -> RolesRepresenter.toJSON(writer, goCDRoles));
        } else {
            return renderHTTPOperationResult(result, req, res);
        }
    }

    @Override
    public String etagFor(Role entityFromServer) {
        return entityHashingService.md5ForEntity(entityFromServer);
    }

    @Override
    public EntityType getEntityType() {
        return EntityType.Role;
    }

    public boolean isRenameAttempt(Role fromServer, Role fromRequest) {
        return !fromServer.getName().equals(fromRequest.getName());
    }

    @Override
    public Role doFetchEntityFromConfig(String name) {
        return roleConfigService.findRole(name);
    }

    @Override
    public Role buildEntityFromRequestBody(Request req) {
        JsonReader jsonReader = GsonTransformer.getInstance().jsonReaderFrom(req.body());
        return RoleRepresenter.fromJSON(jsonReader);
    }

    @Override
    public Consumer<OutputWriter> jsonWriter(Role role) {
        return writer -> RoleRepresenter.toJSON(writer, role);
    }

    private void haltIfEntityBySameNameInRequestExists(Request req, Role role) {
        if (roleConfigService.findRole(role.getName().toString()) == null) {
            return;
        }
        role.addError("name", "Role names should be unique. Role with the same name exists.");
        throw haltBecauseEntityAlreadyExists(jsonWriter(role), "role", role.getName());
    }
}

redpajama_set_name: RedPajamaGithub


text:
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DCF funded student makes headway in Agapanthus pest project
By Leah on	 September 2, 2019 Protected Crops News
The David Colegrave Foundation (DCF) is delighted to be funding Julie Lin, a Biological Sciences student at Imperial College London, as part of a Plant Health Undergraduate Studentship.
DCF worked with the Royal Society of Biology (RSB) to select a plant health project for its Plant Health Undergraduate Summer Studentship Programme for 2019. The selected project is The Life cycle and biology of an emergent pest, the agapanthus gall midge, hosted by RHS, Wisley and supervised by Dr. Hayley Jones.
Julie Lin is thrilled to be working at the forefront of research alongside the plant health team. She says: "I applied to this project after I was enticed by the idea of uncovering information completely new to science…Last summer I undertook a placement which involved the rearing of small insects and annelids efficiently within a lab. To do this, I delved into the literature describing the life cycles of these little critters and during this time became increasingly impressed by the fascinating and diverse life cycles of insects. The summer studentship project to elucidate the life stages of the newly discovered agapanthus gall midge, brought these ideas together and so piqued my interest…I am already very thankful for this opportunity and I am looking forward to carrying out the experiments which will likely reveal critical information towards the development of control against the agapanthus gall midge."
The project has got off to a great start tells Dr. Hayley Jones: "We selected Julie for this project because of her enthusiastic and well written application and performance in a telephone interview, where she outlined her biological research skills and experience with entomology. So far, she has proved an excellent student, working very hard and efficiently and making good progress with the project…She has already successfully photographed the pupal stage and deduced that they do not form a cocoon, a key gap in our knowledge that her project was tasked with…We are only a third of the way into the project and Julie has already achieved so much, I look forward to the rest of the project."
The agapanthus gall midge, Enigmadiplosis agapanthi, causes damage to the popular ornamental plant Agapanthus. The midge larvae form galls in the flower buds, deforming them and stopping their flowering. This project will gather essential life cycle information. The knowledge gained will inform the development and targeting of control options, with the aim of improving the economic stability of Agapanthus breeders and nurseries, and empowering gardeners to protect their garden plants from this pest.
Read more at http://davidcolegravefoundation.org.uk/dcf-funded-student-tackles-agapanthus-pest/
Coventry University awarded €7 million EU research grant
British Group at IPM Essen 2020
Specialist Charlotte Penn to help food processors and producers in new role at CambridgeHOK
Copyright © HortNews


text:
Nasib al-Bakri (; 1888–1966) was a Syrian politician and nationalist leader in the first half of the 20th century. He played a major role in establishing al-Fatat, an underground organization which sought the independence and unity of the Ottoman Empire's Arab territories. As the chief envoy between al-Fatat and the Hejaz-based Hashemites, al-Bakri became a close aide to Emir Faisal when the latter became King of Syria following the success of the 1916 Arab Revolt. Al-Bakri opposed the establishment of the French Mandate of Syria and became one of the chief commanders of the Great Syrian Revolt, leading the rebels' brief capture of Damascus. He escaped a death warrant in Syria in 1927, but returned the following year after being amnestied.

Al-Bakri served as a representative of Damascus in the Syrian Parliament between 1932 and 1946. He was one of the main coordinators of the 1936 general strike and became Vice President of the National Bloc. He defected to join Abd al-Rahman Shahbandar's party in 1938. During the post-independence period, al-Bakri was appointed Syria's ambassador to Jordan but resigned in 1953 in protest against Adib al-Shishakli's seizure of power. The following year, he became President of the People's Party, but retired in 1957.

Early life

Nasib was born in Damascus in 1888 to father 'Ata al-Bakri. Nasib was the second oldest of five sons. 'Ata was an influential official in the city and district councils of Damascus between the 1890s and 1914, and was one of the most prominent Arabs to serve in the imperial Ottoman court of Sultan Abdul Hamid II in Constantinople. The al-Bakri family were Sunni Muslims and claimed descent from the Islamic prophet Muhammad. They were landowners, possessing lands, homes and commercial venues in their native al-Shaghour quarter and in Qaboun, a village in the Ghouta countryside of Damascus. They also owned land in Jaramana, a Druze village outside of Damascus and maintained good relations with the local Druze chiefs.

When Abdul Hamid II was overthrown during the Young Turk Revolution in 1908, 'Ata lost his favor from the central authorities because of his closeness with the deposed sultan and criticized the revolutionary officers. Consequently, the al-Bakri family realigned itself with Arab nationalists in Syria who opposed the increased Turkish nationalist efforts in the Arabic-speaking territories of the empire. 'Ata had also developed close ties with the Hashemites of the Hejaz. In 1909 he hosted the Sharif of Mecca, Hussein bin Ali, his brother Nasir, and Abdullah, Sharif Hussein's son, in his Damascus home.

Nasib attended Maktab Anbar, a preparatory school in Damascus that attracted the children of the elite and produced several future Arab nationalists. In 1912, Nasib graduated from the al-Sultaniya School of Beirut. When Sharif Hussein's son, Faisal, visited Syria in early 1916, he lodged in the al-Bakris' summer house in Qaboun, outside of Damascus. Prior to this, Nasib and his brothers Fawzi and Sami had joined the budding al-Fatat movement, an underground society advocating Arab independence from the Ottomans. Nasib had become the movement's secretary.

Leader in Syrian independence movement

Ally of the Hashemites

In 1915, Nasib hosted Faisal at his Ghouta country house and invited him join al-Fatat, which he reportedly agreed to. At the same time, al-Bakri organized a meeting between him, some members of al-Fatat, and the Druze chiefs of the Hauran, Hussein and Sultan al-Atrash with the intention of gaining Druze support for the planned Arab rebellion against the Ottomans (the Druze had launched several uprisings against the Ottomans prior). The meeting concluded with the Druze offering Faisal and the nationalists their backing, though short of any military support. The meeting was the first of its kind between the Hashemites and the Druze, and afterward Faisal appointed al-Bakri to be his personal secretary and his envoy to the Druze, a post he would serve until 1920.

In the summer of 1916, amid World War I, Sharif Hussein launched the Great Arab Revolt against the Ottomans from Mecca with the backing of the British military. Al-Bakri joined the revolt and moved to the Hejaz where he served as a channel between al-Fatat based in Damascus and the Hashemite forces leading the uprising. When the Ottomans were defeated in 1918 and Arab and British forces reached Damascus, Faisal would soon become the King of Syria and al-Bakri served as one of his advisers. The next year al-Bakri co-founded the first legal political party in Faisal's Syria, the pan-Arabist al-Istiqlal ("Independence") which sought to unify all the former Ottoman-held Arab territories under the leadership of the Hashemites. During this period until 1920, al-Bakri was a member of the Syrian National Congress as a representative of Damascus.

France invaded and began occupying Syria in 1919 and following the Battle of Maysalun in July 1920, Faisal was exiled and the kingdom annulled. Al-Bakri left for Amman in Transjordan, which was under the authority of Faisal's brother King Abdullah. Al-Bakri would later serve as Abdullah's aide in 1921, a position he held for about two years before returning to Syria after the French issued amnesty for political exiles. On his return, he became a member of al-Shahbandar's People's Party and actively sought to topple the French authorities in Syria and align the country with the ruling Hashemites in Iraq, Transjordan and the Hejaz. The Hashemites were driven out of the latter in 1925 by the Saudis.

Role in Great Syrian Revolt

The summer of 1925 also saw the beginning of the Great Syrian Revolt, launched by Sultan Pasha al-Atrash in the Jabal al-Arab region in southern Syria. After Atrash's men destroyed a French column at al-Kafr, al-Bakri received a letter from al-Atrash on 23 July calling on the nationalists in Damascus to join the revolt; al-Bakri subsequently joined. Following the French defeat at the Battle of Mazraa on 3 August, al-Bakri began working with Abd al-Ghaffar al-Atrash, the Druze chief of al-Suwayda, to advance the revolt to other parts of the country outside of Hauran. Al-Bakri set up a meeting between the Damascus-based nationalists and Sultan al-Atrash at his home in Qaboun, after which the two sides agreed to work together to uproot the French from Syria.

Following the meeting, al-Bakri conferred with al-Shahbandar, who agreed to bring Damascus into the revolt, although this initial attempt did not materialize. As al-Atrash's men headed towards Damascus to launch their attack against French forces there, al-Bakri assembled some 260 armed volunteers from various neighborhoods and villages in and around Damascus, including al-Shaghour, Bab Musalla, al-Midan, and Jaramana. Al-Bakri maintained particularly close ties to Hasan al-Kharrat, the local boss (qabaday) of al-Shaghur and a friend of the al-Bakri family. In early August, upon al-Bakri's urging, al-Kharrat formed a militia, which would become one of the most effective rebel bands in the country. When the French authorities were informed of nationalist rebel plans, they began a wide-scale arrest campaign in the city on 27 August, detaining nearly all of Damascus's nationalist leaders and spokesmen, although al-Bakri, his brothers, and al-Shahbandar managed to evade arrest.

He participated in attacks alongside Druze warriors against French positions and offices in the Hauran, and of all the rebel commanders from Damascus, al-Bakri was the most respected among the Druze. As fighting between rebels and French forces in the Ghouta escalated, al-Bakri devised an operation to wrest control of Damascus from the French by capturing the citadel and the Azm Palace. The former housed the city's French garrison, while the latter housed the French Mandate High Commissioner Maurice Sarrail. Al-Bakri requested reinforcements from al-Atrash and his men, but they were occupied by fighting in the Hauran and notified al-Bakri that any help would be delayed. Al-Bakri decided to move ahead nonetheless. On 17 October, he assembled al-Kharrat's group and another group of rebels from al-Midan and Jaramana inside Damascus. The next day al-Kharrat launched the operation.

While al-Kharrat's men managed to capture the Azm Palace and the police station in Bab Saghir, al-Bakri led a band of 200 fighters from their base in al-Midan to raid an Armenian refugee camp in al-Qadam, killing several Armenian refugees. The rebels accused the Armenians—who along with the Circassians were typically allied with the French authorities—of participating in the French military assaults against several Ghouta villages in the preceding weeks. After attacking al-Qadam, al-Bakri's forces swept through the city, capturing the police stations at Bab al-Jabiyah, Bab Musalla and Qanawat. With each captured neighborhood, their forces increased in size as enthusiastic bystanders joined in the attacks.

Sarrail, who was not in Damascus at the time of the rebel assault, ordered aerial bombardment of the city, leading to the destruction of whole neighborhoods and the deaths of hundreds of Damascus residents. By 24 October, the rebels were routed, and al-Bakri escaped. He became the target of criticism among other rebel leaders, namely Said al-'As. Al-'As stated that al-Bakri sought personal glory when he decided to prematurely launch a mostly uncoordinated attack with small numbers of armed volunteers, instead of waiting for the arrival of al-Atrash's reinforcements, who numbered around 1,000. Al-Bakri was the only member of the Damascus nationalist elite to directly participate in the fighting on the ground.

In early December, al-Bakri chaired a meeting of rebel leaders in the Ghouta village of Saqba. During the meeting, he launched scathing criticism of Ramadan al-Shallash, the rebel commander from Deir ez-Zor, condemning him for levying heavy fines and other fees against the residents of the villages of Douma, al-Qisa, Harran al-Awamid and al-Midaa which had been captured by the rebels. However, these taxes were almost entirely directed at the major landowners and city elites, rather than the commoners or peasants. 'As defended al-Shallash as a skilled commander, criticized al-Bakri's leadership and accused him of holding "secret hatreds and ambitions". Nonetheless, al-Bakri and his ally al-Kharrat managed to have al-Shallash "expelled from the rebellion" during the meeting, and stripped of his arms and insignia. However, subsequent French bombardment of Saqba allowed al-Shallash to escape punishment. Al-Kharrat was killed in a French raid two weeks later, while al-Shallash defected to the French following his expulsion. Al-Bakri's younger brother As'ad was killed in action in 1926.

Politician during French Mandatory rule

The revolt dissipated by June 1927. Al-Bakri was sentenced to death in absentia by French military tribunal. Consequently, he fled to Amman in Transjordan. In March 1928, al-Bakri, his brother Fawzi, and Fares al-Khoury were amnestied by the French authorities and the al-Bakri family's properties, which had been bombed by the French during the revolt, were restored to them. According to historian Peter A. Shambrook, al-Bakri's inclusion on the amnesty list was surprising for two reasons: he maintained a strong relationship with France's chief rivals in the region, the Hashemites and their British patrons, and he held "unrivaled" influence among the bosses of "the popular quarters of Damascus". The French sought to divide the ranks of the rebels and the nationalist politicians by pardoning some leaders and blacklisting others like al-Atrash, al-Shahbandar, and Shukri al-Quwatli. Al-Bakri's relations with the latter two subsequently grew tense as he accused them of diverting funds for the revolt to their personal ventures.

He and Hashim al-Atassi founded the National Bloc political party. It sought to use diplomatic means to end French rule. He was a part of the 1928 Constitutional Assembly, helping draft a constitution for the Syrian Republic. Al-Atassi appointed him Vice President of the National Bloc in 1930. Al-Bakri successfully ran for parliament as a representative of Damascus on the National Bloc's ticket in 1932, after winning a run-off vote by a large margin.

In January 1936, Syrian nationalist sentiments became incensed as the French authorities suspended parliament and appointed the pro-French president Taj al-Din al-Hasani. Following the arrest of some nationalist leaders, a general strike was declared against the French Mandate and President al-Hasani. Speeches denouncing the arrests and colonialism were made at the Umayyad Mosque, after which demonstrators, including students and local youths, gathered at al-Bakri's home where they coordinated a march to the Serail (French government headquarters). The protests were led by al-Bakri, al-Quwatli and Jamil Mardam Bey, but they were confronted by the security forces before leaving al-Bakri's street.

On 24 January, al-Bakri led a sermon at the mosque calling for calm among the 3,000 demonstrators in attendance. Nonetheless, some 300 left to attack French roadblocks and the police station at Souq al-Hamidiyya, before withdrawing back into the mosque. One protester was killed and the following day, al-Bakri led the funeral procession, which was attended by thousands of mourners. By mid-February, unrest spread throughout Syria and the authorities clashed with Syrian protesters in several cities. The commander of the French Army of the Levant declared martial law and forbade public assemblies. Al-Bakri was arrested and deported on 11 February.

He went on to win the election for his seat in 1936, 1943 and 1947. When al-Atassi became president in 1936, al-Bakri became the chief leader of the National Bloc. The following year, he was appointed by al-Atassi to serve as Governor of Jabal al-Arab. In 1938, he defected from the National Bloc to join the rival People's Party led by his former colleague al-Shahbandar. In the short-lived 1939 cabinet of Prime Minister Lutfi al-Haffar, Bakri was made justice minister, while in Prime Minister Khalid al-Azm's cabinet he served as national economy and agriculture minister.

Post-independence career
After Syria became independent in 1946, al-Bakri joined the pro-Western and Arab nationalist People's Party. President al-Atassi assigned him ambassador to Jordan, ruled by the Hashemites, after al-Bakri refused the ambassadorial post to Saudi Arabia, a government that he opposed ideologically. Following Adib al-Shishakli's seizure of the presidency in 1953, al-Bakri resigned. After al-Shishakli stepped down in 1954, al-Bakri became president of the People's Party. He was unsuccessful in establishing a significant support base in Damascus and resigned from political life in April 1957. He died in 1966.

References

Bibliography

1888 births
1966 deaths
Agriculture ministers of Syria
Ambassadors of Syria to Jordan
National Bloc (Syria) politicians
People from Damascus
People of the Great Syrian Revolt
People's Party (Syria) politicians
Place of death missing
Syrian Arab nationalists
Syrian nationalists
Syrian ministers of economy
Syrian ministers of justice

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