Cups sporting the "Main bhi chowkidar" (I too am a watchman) slogan popularised by Prime Minister Narendra Modi who has launched a campaign of the same name, and used to serve tea on the Kathgodam Shatabdi train, were withdrawn on Friday because they violate the model code of conduct.
The Indian Railways Catering and Tourism Corporation also suspended the supervisor responsible for the catering and levied a fine of R 1 lakh on him. "We have taken action against the Supervisor and have withdrawn these cups," said MP Mall, managing director of IRCTC. "News reports that tea has been served in cups sporting the slogan "Main bhi chowkidar" have been investigated. This was without any prior approval of IRCTC. The cups have been withdrawn with immediate effect. ~1 lakh fine has been imposed on the service provider. A show-cause notice has also been served for this misconduct," said a spokesperson for Indian Railways. IRCTC does not allow political advertisements as per its contract with service providers. The matter has also been referred to the EC. "How could they allow this to happen? I was travelling in Kathgodam Shatabdi when I noticed the cup with political message. I complained to the on-board staff also," said DN Mohanty, who retired as ADG from All India Radio.
Meanwhile, Air India, on Friday, again issued boarding passes with photographs of Narendra Modi and Gujarat chief minister Vijay Rupani, despite saying it has withdrawn such boarding passes on March 25. "AI issued notice on 25.03.19 to all domestic stations to discontinue usage of boarding cards with a Vibrant Gujarat advertisement on reverse with immediate effect. Today's incident is because of human error. A show-cause notice for this error has been issued to the airport manager of AI at Madurai," said AI Spokesperson Dhananjay Kumar.


As the wind screams through the house, Maeve lifts her head. A voice comes through the air, a voice carried on the wind itself. She tilts her head toward the gales, concentrating on the sound beneath the roar.
Someone calls her name. A name she remembers from long ago. Before the storm.
It is a voice she knows; a voice as familiar to her as her own. A voice she has heard every day for as long as she remembers. The warmth of the voice carries through the bite of the sand pelting her from the blown-out windows. She rises to her knees.
She holds out her hand to the maelstrom around her.


text:
Пражки кръг () е група немскоезични писатели в Прага от края на XIX в. до 1918 г., когато се разпада Австро-Унгарската империя.

Понятието е създадено през 1966 г. от писателя Макс Брод. Той различава по-тесен Пражки кръг, в който участват Франц Кафка, Феликс Велч, Лудвиг Виндер, Оскар Баум и самият Макс Брод. Към по-широкия кръг причислява писатели, които имат връзка с "тесния кръг", като Райнер Мария Рилке, Франц Верфел, Густав Майринк или Хуго Бергман.

По времето на Пражкия кръг Прага е епицентър на "Езиковия конфликт в Бохемия" – борба за надмещие между немския и чешкия език в областта. Важен белег за членовете на Пражкия кръг е липсата у тях на всякаква немско-национална надменност.

Голяма част от членовете са от еврейски произход, мнозина владеят чешкия език и кръгът има живо общуване с чешки писатели, музиканти и художници.

Литература
  Max Brod: Der Prager Kreis. Kohlhammer, Stuttgart / Berlin / Köln / Mainz 1966.
  Margarita Pazi: Fünf Autoren des Prager Kreises, Lang, Frankfurt am Main / Bern / Las Vegas 1978.
  Andreas Kilcher: Kampf um die Deutungshoheit. Der "Prager Kreis" ist Max Brods Erfindung, in: NZZ, 10. August 2016, S. 22.
  Elisabeth Buxbaum: Es kafkat und brodelt und werfelt und kischt: Der Prager Kreis, Armin Berg Verlag, Wien 2012.

Източници

Чешка литература
Немскоезична литература
Култура в Прага

redpajama_set_name: RedPajamaWikipedia


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text:
JB Special Collection
JB Classic Spotlights
About JB
Families of Soft-Metal-Ion-Transporting ATPases
Christopher Rensing, Mallika Ghosh, Barry P. Rosen
Christopher Rensing
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan 48201
Mallika Ghosh
Barry P. Rosen
Life undoubtedly first arose in waters rich in metal ions. Since most metal ions are toxic in excess, it is reasonable to speculate that metal resistances probably evolved early, predating antibiotic resistances. This minireview focuses on transport ATPases that produce resistance to ions of the metals zinc, cadmium, lead, copper, silver, arsenic, and antimony in prokaryotes. Other aspects of transport and resistance to those metal ions have been reviewed recently (44, 45, 53, 55, 62) and will not be discussed here.
Soft Lewis acids such as the transition metals Cu(I), Ag(I), Zn(II), and Cd(II) and the heavy metal Pb(II) have high polarizing power (a large ratio of ionic charge to the radius of the ion) and typically form strong bonds with soft Lewis bases (30). These include sulfur and nitrogen ligands such as cysteine and histidine residues in proteins. In contrast are the hard Lewis acids of groups 1a and 2a such as Na+ and Ca2+, which form ionic bonds with hard Lewis bases, for example the oxygen of protein carboxylates. The metalloids As(III) and Sb(III) of group 5a have properties similar to those of soft Lewis acids. For the purposes of this review, alkali and alkaline earth cations are termed hard metals, and transition metals, heavy metals, and metalloids are termed soft metals.
Genes for resistance to inorganic salts of soft metals are found both on plasmids and in chromosomes (44, 53, 55). The physiological role of plasmid-encoded determinants is generally to confer resistance, while the role of chromosomally encoded systems may also include metal ion homeostasis. Copper and zinc ions are required for growth; there must be a fine balance between uptake and efflux to provide metal ion homeostasis. In the case of soft metals that are only toxic, specific uptake systems may not exist. Rather, those ions may be accumulated via other existing transport systems.
ARSENIC AND ANTIMONY
The oxyanions of arsenic and antimony are quite toxic, especially the reduced (trivalent) forms, and enter cells via transporters for other compounds. In Escherichia coli and other bacteria, arsenate [As(V)] is taken up by phosphate transport systems such as the ATP-coupled Pst pump (52), a member of the ABC superfamily of transport ATPases (Fig.1). One route of entry of Sb(III) [and probably As(III)] is via the GlpF polyol transporter (48). Once inside cells, the toxicity of the trivalent metalloids is a double-edged sword. On the one hand, this property made them useful in the development of antimicrobial agents, exemplified by Paul Ehrlich's silver bullet, the organoarsenical Salvarsan. On the other hand, arsenical and antimonial drugs are so toxic to humans that their use was difficult to manage. Paul Ehrlich is not only the father of modern antimicrobial chemotherapy but was also one of the first to comprehend that organisms could become resistant following continued drug use. We now recognize that resistance to arsenicals and antimonials is widespread, occurring in bacteria, fungi, protozoans, and animal cells (44). Bacterial operons encoding resistance to arsenicals and antimonials (ars operons) can be found on transmissible plasmids and in chromosomes. These operons usually have either three (arsRBC) or five (arsRDABC) genes. ArsR is an As(III)/Sb(III)-responsive transcriptional repressor (25, 47,49). ArsB is a secondary transporter that catalyzes efflux of the arsenite anion from cells (14) (Fig. 1). ArsC is a reductase that catalyzes electron transfer from reduced glutathione and glutaredoxin (in E. coli) (18) or thioredoxin (inStaphylococcus aureus) (23, 24) to arsenate, reducing it to arsenite, the substrate of the efflux system. Thus, this enzyme extends the spectrum of resistance to include both oxidized and reduced forms of arsenic. While all ars operons have those three genes, some operons have two additional genes, arsDA. ArsD is a repressor that works independently of ArsR to provide fine tuning of operon expression (9). ArsA is an As(III)/Sb(III)-stimulated ATPase (46) that associates with ArsB to form an extrusion pump that is more efficient than ArsB alone (14) (Fig. 1).
Soft metal transport ATPases. In E. colithere are primary pumps for the uptake and efflux of transition metals, heavy metals, and metalloids. (Left) Arsenate is accumulated by phosphate transporters such the Pst pump (51), a member of the ABC superfamily of transport ATPases. Arsenate is reduced to arsenite via the ArsC arsenate reductase. Arsenite is then extruded from cells by the Ars extrusion system (44). In cells expressing the chromosomal arsRBC operon, ArsB is a secondary arsenite carrier protein coupled to the membrane potential that confers low-level resistance to metalloid salts. In contrast, in cells expressing a plasmid-encoded arsRDABC operon, the ArsAB complex is an As(III)/Sb(III)-translocating ATPase that confers high level resistance. (Middle) The CopA P-type ATPase confers resistance to copper ion and probably transports the monovalent cation. (Right) ZnuABC is an ABC transport ATPase that catalyzes uptake of Zn(II) (37), and ZntA is a Zn(II)-translocating P-type ATPase (2, 42). It is hypothesized that these two pumps are a homeostatic mechanism that controls the intracellular concentration of Zn(II). In addition, ZntA confers resistance to Pb(II), Cd(II), and excess Zn(II).
The best-studied ArsAB pump is that encoded by the arsoperon of E. coli plasmid R773 (7). The ArsA subunit has two repeats, A1 and A2, that are clearly the result of an ancestral gene duplication and fusion. Each half contains a consensus nucleotide binding domain (NBD) for ATP. When purified in the absence of ArsB, ArsA is soluble and exhibits an ATPase activity that is allosterically activated by binding of Sb(III) or As(III). Both NBDs are required for enzymatic activity, and it is likely that the two sites must interact to produce a catalytically competent protein (29).
While many enzymes with vicinal cysteines are inhibited by As(III) and Sb(III), ArsA is allosterically activated by those soft metals and is the only known enzyme that requires metalloids for activity (Fig.2A). The metal binding site is composed of a triad of three cysteine residues, Cys113, Cys172 and Cys422, which form a novel three-coordinate As-S structure (3, 4). This allosteric control ensures that the enzyme will not hydrolyze ATP when the pump is not required. It is unlikely that the As(III) bound at the allosteric site is transported. More likely, the membrane component, ArsB, has a separate binding site for the arsenite oxyanion. Thus, the pump need only be activated by a binding of a single metal ion to allow multiple rounds of transport through the pump.
The ArsA ATPase. (A) Model of ArsA catalysis. In the absence of an allosteric effector, the A1 and A2 halves of ArsA are connected only by a 25-residue flexible linker and have a low basal rate of ATP hydrolysis (46). Binding of either Sb(III) or As(III) to Cys113, Cys172, and Cys422 is proposed to bring together A1 and A2, forming an interface of the two NBDs, promoting hydrolysis of ATP (3, 4). (B) Reaction mechanism of the ArsA ATPase. A minimal multistep kinetic scheme for the reaction catalyzed by ArsA has been proposed (60). In this scheme, ArsA undergoes several conformational changes during binding of substrate (MgATP) and release of products (MgADP and Pi). In the steady state, the ArsA7 conformation of the enzyme builds up, with a slow isomerization back to the ArsA1 form. Since binding of substrate and release of products are all faster than this isomerization, it becomes the rate-limiting step in the reaction in the absence of activator. Binding of As(III) or Sb(III) at the allosteric site increases the rate of ArsA7 conversion to ArsA1, accelerating catalysis.
Recently, ArsA homologues have been identified in eubacteria, archaea, fungi, plants, and animals (44). At this time the physiological functions of these proteins are largely unknown. In addition to the NBDs, there is a highly conserved region termed the DTAP motif (63). In the R773 ArsA the role of the DTAP domain in the A1 half was examined by using the effects of substrates and effectors on intrinsic tryptophan fluorescence. By site-directed mutagenesis two single-tryptophan ArsAs were constructed. One encoded a protein with a single tryptophan residue located at position 141, the N-terminal side of the DTAP domain. The second engineered gene coded for an ArsA with a single tryptophan residue at position 159, the C-terminal side of the DTAP sequence. These two tryptophans served as intrinsic probes of the environment of the DTAP domain. During ATP hydrolysis this domain undergoes significant conformational changes that may be involved in coupling the allosteric site to the catalytic site in the R773 ArsA. Binding of the product, MgADP, but not the substrate, MgATP, produced a decrease and red shift in Trp141 fluorescence, indicative of movement of the N-terminal end of the A1 DTAP domain from a relatively hydrophobic environment into a more hydrophilic one. In contrast, MgATP resulted in a large increase and blue shift in Trp159 fluorescence, which indicates that the C-terminal end of the A1 DTAP domain had moved into a relatively more hydrophobic environment. However, no change in Trp159 fluorescence was observed with MgADP, with nonhydrolyzable ATP analogs, or with MgATP in noncatalytic ArsA enzymes. Thus the N-terminal end of the domain moves in response to ATP hydrolysis, not binding, and the C-terminal end moves as product is formed.
Recently, changes in the intrinsic fluorescence of Trp159 have been used to elucidate a minimum reaction scheme for ArsA catalysis (60) (Fig. 2B). From the results of stopped-flow fluorescence measurements the rates of substrate binding and product release could be determined. In addition, a number of fluorescence changes were observed that suggested that the enzyme underwent several conformational changes during the reaction cycle. Of importance was the fact that a steady-state conformation (ArsA7) builds up following hydrolysis and release of products. The slowest (and hence rate-limiting) step in the overall reaction appears to be the decay of ArsA7 back to the initial state (ArsA1). Although not unique to ArsA, such conformational isomerizations are rarely the rate-limiting step in catalysis. Binding of As(III) or Sb(III) increases the rate of decay of ArsA7; in other words, the acceleration of catalysis produced by the allosteric effector can be accounted for by an increase in the rate of isomerization between two different ArsA conformations. Together, the kinetic, genetic, and biochemical data suggest a model in which ATP hydrolysis at either the A1 or A2 catalytic site in ArsA is slow and limited by a conformational change in each half. Binding of As(III) or Sb(III) to the allosteric site, which is composed of Cys113 and Cys172 in A1 and Cys422 in A2, produces physical movement of the two halves toward each other. At the newly formed interface of A1 and A2, the slow isomerization of the two conformations speeds up, accelerating catalysis (Fig. 2B).
Yet to be answered is the question of how the energy of ATP hydrolysis is coupled to transport through ArsB. As a complex of ArsA and ArsB, the pump can use only chemical energy as an energy source (13). In intact cells electrochemical energy was neither necessary nor sufficient for73AsO2 −1 transport. Only ATP could support transport in everted (inside-out) membrane vesicles. Again, transport in vitro could not be driven by respiratory substrates, and transport was insensitive to uncouplers. Thus, both in vitro and in vivo, electrochemical energy was neither necessary nor sufficient.
As mentioned above, ars operons come in two flavors: those with three genes, arsRBC, and those with five genes,arsRDABC. How do cells expressing a three-gene operon extrude arsenite without ArsA, the catalytic subunit of the pump? Without ArsA, ArsB can function as a secondary carrier, perhaps as an electrophoretic uniporter coupled to the membrane potential, not ATP (27). The arsRBC operons confer lower resistance to metalloids than the five-gene operons, which is consistent with the fact that secondary transporters cannot form concentration gradients of the same magnitude as can primary pumps. It is likely that the form of arsenic recognized by the pump is the arsenite oxyanion. First, there is only a single cysteine residue in ArsB that is not required for activity, so soft metal-thiol chemistry cannot be involved (8). Second, since the membrane potential is the driving force, the most parsimonious interpretation of the data is that an anion is transported from the negative to the positive side of the membrane, that is, out of the cell. This capacity of ArsB to function in a dual mode as a secondary carrier or a subunit of a primary pump is novel. We postulate that ArsB arose first as a low-level mechanism of resistance toward metalloids; under environmental pressure to adapt to higher levels the pump evolved by association with an ATPase ancestor of ArsA (44).
SOFT-METAL-TRANSPORTING P-TYPE ATPASES
The superfamily of P-type ATPases is a ubiquitous group of proteins involved in transport of charged substrates across biological membranes (1). The term "P-type" refers to the formation of a phosphoenzyme intermediate in the reaction cycle. P-type ATPases share common features including a conserved aspartate residue that is phosphorylated during the reaction cycle, a conserved proline residue in a membrane domain that probably forms a portion of the ion translocation pathway, and consensus domains for ATP binding and energy transduction. The superfamily of P-type ATPases has five major branches that are distinguished by substrate specificity rather than the relatedness of the organisms in which they are found (1).
One branch contains the phylogenetically related subgroup of P-type ATPases that catalyze transport of transition or heavy-metal ions. They have previously been described as CPx-type ATPases (55) or soft-metal-transporting P-type ATPases (42). These ATPases have eight transmembrane domains (34), in contrast to the hard-metal P-type ATPases, which have 10 transmembrane segments. Other unique features of soft-metal ATPases include a metal binding domain in the cytosolic N-terminal region, a highly conserved CPC motif in the sixth transmembrane domain, the putative translocation domain, and a conserved histidine-proline sequence 34 to 43 residues C terminal to the CPC motif (55).
Soft-metal-transporting P-type ATPases can be further divided into subgroups that contain Cu(I)/Ag(I)-translocating ATPases and Zn(II)/Cd(II)/Pb(II)-translocating ATPases (Fig.3). The first branch harbors representative members such as CopA from Enterococcus hirae,Helicobacter pylori, and E. coli. The second branch includes ZntA from E. coli and CadA from S. aureus plasmid pI258. As discussed below, members of the first branch most likely transport monovalent soft-metal cations, while members of the second branch are divalent soft-metal-cation pumps. This is similar to the two branches of the hard-metal-ion P-type ATPases, where members of one branch pump monovalent alkali cations such as H+, K+, and Na+ and members of the other branch transport divalent alkaline earth cations such as Ca2+ and Mg2+.
The family of soft-metal-ion-translocating P-type ATPases. This family is growing rapidly, so only representative ones are shown. GenBank accession numbers are given in parentheses. The dendograms were made using the CLUSTAL4 algorithm (22) with DNASIS software from Hitachi Software Engineering Co., Ltd. The calculated matching percentages are indicated at each branch point. Zn(II)/Pb(II)/Cd(II) pumps: ZntA, E. coli (P37617); ZntA,P. mirabilis (CAA04762); CadA, Bacillus firmus(AAA22858); CadA, pI258 (AAB59154); CadA, Tn5422 (L28104); CadA, H. pylori (AAA93043); ZiaA, Synechocystissp. strain PCC 6803 (Q59998); P. aeruginosa reading frame (unfinished genome); Chlamydia pneumoniae reading frame (AAD19006); A. thaliana reading frame (CAB16773). Cu(I)/Ag(I) pumps: MNK, human Menkes disease-related protein (Q04656); WND, human Wilson disease-related protein (U03464); PacS,Archaeoglobus fulgidus (AE0010711); CopA, E. hirae copper uptake pump (P32113); CopA, E. coli(AAB02268); SilP, S. typhimurium Ag(I) pump (AAD11750); PacS, Synechocystis sp. strain PCC 6803 (P73241); CtaA,Synechococcus sp. strain PCC 7942 (P37385); CopA, H. pylori (AAB05475); CCC2, S. cerevisiae vacuolar copper pump (L363171); CopB E. hirae copper efflux pump (P05425).
COPPER AND SILVER
Copper is an essential metal ion for most organisms, required for enzymes such as cytochrome oxidase and superoxide dismutase. However, cells need to keep the intracellular concentration of free copper ion low, since the free metal ion can facilitate oxidative damage through generation of free radicals. In contrast to copper, silver is not required for growth and is only detrimental to cells. In bacteria, energy-dependent copper uptake by a specific copper transporter has not been directly demonstrated.
The best-studied copper transport systems are the copper ATPases ofE. hirae, CopA and CopB (36). CopB is a Cu(I)/Ag(I) efflux pump, while CopA is thought to be involved in copper uptake. Cells with a disruption of the copA gene are copper requiring and more silver resistant than the wild type, while disruption of copB rendered the cells hypersensitive to copper salts. Structurally, CopB differs from CopA and its homologues primarily in the N-terminal metal binding domain. CopA and homologues have one or more N-terminal CXXC metal binding motifs. In contrast, CopB has a histidine-rich repeat at the N terminus. In vitro, CopB has been shown to catalyze accumulation of either110Ag or 64Cu in membrane vesicles prepared from E. hirae (54). These vesicles are presumably everted (inside-out), so uptake corresponds to extrusion from intact cells.
A close homologue of CopA is CtaA from Synechococcus strain 7942; disruption of the ctaA gene rendered the cells more resistant to copper (38). Other CopA homologues include PacS from Synechococcus strain 7942 and CopA from H. pylori. Disruption of pacS rendered the cells more sensitive to copper and silver salts. PacS is apparently localized in the thylakoid membrane and is specifically induced by copper and silver (26). Disruption of H. pylori copAalso resulted in copper sensitivity (33). Another CopA homologue, SilP, was isolated from a plasmid of a pathogenicSalmonella strain (20). SilP, which has a unique histidine-rich N terminus, is part of a silver resistance determinant and has been suggested to be a specific Ag(I)-translocating ATPase.
E. coli has only two genes for soft-metal P-type ATPases, one of which is zntA (2, 42), which encodes a Zn(II)/Cd(II)/Pb(II)-translocating ATPase and is described in more detail below. The other is a CopA homologue, f834 (GenBank accession no. AE0001541) (Fig. 3). Disruption of E. coli copA renders the cells more sensitive to copper ions, indicating that it is a copper-translocating ATPase that probably catalyzes copper extrusion (42a) (Fig. 1), as opposed to the homologousE. hirae CopA, which is thought to transport copper into the cytosol. Consistent with its role as a copper efflux pump, the copper-sensitive phenotype of a copA-disrupted E. coli strain could be complemented by copB from E. hirae (42a).
Eukaryotes possess similar copper ATPases, examples of which are CCC2 in Saccharomyces cerevisiae (16) and ATP7A (59) and ATP7B (6) in humans. These proteins have been shown to be involved in intracellular copper trafficking in all organisms examined, and putative homologues have been found in most sequenced genomes but are notably absent from some of the smaller ones such as the Mycoplasma genitalium genome.
What is the ionic species transported by copper-translocating ATPases? Although it is difficult to verify physiologically, the substrate of copper efflux P-type ATPases is probably Cu(I). Cells are usually presented with Cu(II) because Cu(I) rapidly oxidizes in air. However, the cytosol of cells is highly reducing, with high concentrations of reduced glutathione or other thiols, indicating that copper should be in the form of Cu(I) intracellularly. The results of in vitro copper or silver transport experiments indicate that the transported species is likely Cu(I) or Ag(I). Both ATP7A and E. hirae CopB were shown to transport copper only in the presence of dithiothreitol, consistent with transport of Cu(I) (58). Additionally, Lutsenko and coworkers cloned and expressed the N-terminal cysteine-rich sequences from ATP7A and ATP7B and demonstrated that the peptides bound 5 to 6 nmol of copper per nmol of protein (32). The copper released from polypeptides reacted with bicinchoninic acid, which reacts with Cu(I) but not Cu(II).
By multidimensional nuclear magnetic resonance the solution structures of a 72-residue polypeptide corresponding to the fourth metal binding domain of ATP7A was recently determined (17). In the absence of metal, the region containing the putative metal binding sequence GMTCXXC was disordered. Binding of Ag(I) induced order to that domain. Ag(I) was bound in a linear bicoordinate manner to the two cysteine residues, again suggesting that both Cu(I) and Ag(I) may be substrates of copper pumps. On the other hand, the N-terminal domain from ATP7B was expressed and purified as a glutathione S-transferase chimera (15). The chimeric protein bound to metal chelate columns charged with various transition metals. The order of binding affinity was Cu(II) >> Zn(II) > Ni(II) > Co(II), with no binding to Fe(II) or Fe(III). Cu(I) binding was also detected by neutron activation. Thus, it is possible that these proteins recognize both oxidized and reduced forms of copper ion. In contrast to the copper efflux ATPases, copper uptake systems such as E. hirae CopA would be exposed primarily to extracellular Cu(II), which is probably reduced extracellularly prior to transport (61).
Since free copper produces oxidative damage, eukaryotes have evolved intracellular chaperones that reduce free intracellular copper to undetectable concentrations (12, 19, 40). These proteins bind copper tightly and deliver the ion to specific target enzymes. Three eukaryotic copper chaperones were identified in S. cerevisiae, but functional homologues have since been identified in many eukaryotic species, including humans. In yeast, Lys7p delivers copper to cytosolic superoxide dismutase 1 (Sod1p) (11); Cox17p directs copper to the mitochondria for activation of cytochrome oxidase (19); and Atx1p specifically carries copper to the secretory pathway for incorporation into surface or extracellular copper enzymes (39). Although homologues of these copper chaperones have not been identified in prokaryotes, they likely possess other metal chaperones. For example, CopZ of E. hiraeappears to function as a copper chaperone, delivering Cu(I) to a copper-responsive repressor, CopY, that controls copexpression (10). CopZ is homologous to MerP, a periplasmic mercury binding protein that is probably an Hg(II) chaperone for the MerT transporter (21). A common motif in all of these chaperones is a CXXC motif reminiscent of the N-terminal repeat of soft-metal-transporting P-type ATPases.
ZINC, CADMIUM, AND LEAD
Zinc is essential for all organisms, in part because it plays a critical role in the catalytic activity and/or structural stability of many enzymes. As an essential but potentially toxic ion, zinc homeostasis is crucial for all organisms. In prokaryotes homeostasis is maintained by regulating the uptake and the efflux of zinc. In E. coli zinc deficiency induces expression of a specific zinc uptake system, ZnuACB, which is an ABC transporter for zinc uptake (37) (Fig. 1). ZnuA is a periplasmic binding protein. ZnuB is the membrane sector or the pump, and ZnuC is the ATPase catalytic subunit. Genes encoding a ZnuABC homologue have also been identified inHaemophilus influenzae (31). Under conditions of zinc sufficiency, expression of the pump is repressed by the Fur homologue Zur, which presumably binds to the bidirectional promoter region of znuA and znuCB. In addition to repressing zinc uptake, growth of E. coli in high concentrations of zinc results in zinc efflux by induction of ZntA, a zinc-transporting P-type ATPase (2, 42) (Fig. 1). ZntA is activated by ZntR, a MerR homologue that is an activator ofzntA (5). Disruption of zntA results in sensitivity to Zn(II), Cd(II), and Pb(II). The strain did not exhibit increased sensitivity to any other metals ions, including copper and silver, suggesting that this P-type ATPase is a specific Zn(II)/Cd(II)/Pb(II) pump. ZntA has been shown to catalyze ATP-coupled accumulation of 65Zn(II) and 109Cd(II) in everted (inside-out) membrane vesicles of E. coli, where accumulation in everted membrane vesicles is equivalent to efflux from intact cells (42). Vesicles prepared from thezntA-disrupted strain did not accumulate65Zn(II), and the transport defect could be complemented by expression of zntA on a plasmid. The unavailability of a Pb(II) radioisotope prevents direct demonstration that ZntA transports Pb(II). However, ATP-dependent Zn(II) transport by ZntA was inhibited to the same degree by either Pb(II) or Cd(II), and the latter is a demonstrated pump substrate (43).
ZntA homologues are widespread in gram-negative bacteria, includingSalmonella typhimurium, Vibrio cholerae,Yersinia pestis, Deinococcus radiodurans, andProteus mirabilis. A mutation in the P. mirabilisgene produces a swarming defect (28). The relationship between zinc and swarming is unclear but suggests a possible role of Zn(II) in pathogenesis. The E. coli and P. mirabilis ZntA proteins exhibit 61% identity and 69% overall similarity. The zntA gene from P. mirabiliscomplemented the Zn(II)/Cd(II)-sensitive phenotype of the E. coli zntA-disrupted strain. Everted membrane vesicles from the complemented strain catalyzed ATP-dependent 65Zn(II) transport (41).
Another homologue of ZntA is CadA from S. aureus plasmid pI258 (35). The cad operon of pI258 has two genes, cadC, which encodes a transcriptional repressor, andcadA, which encodes CadA, a P-type ATPase that is about 30% identical to ZntA. CadA has been shown to catalyze ATP-dependent109Cd(II) uptake in everted membrane vesicles from B. subtilis (57). CadA homologues have been identified in plasmids and chromosomes from a number of gram-positive organisms, inSynechocystis sp. strain PCC 6803 (1), and in the incomplete genome sequences from Arabidopsis thaliana andPseudomonas aeruginosa. Recently, the CadA homologue fromSynechocystis sp. strain PCC 6803 has been named ZiaA and shown to confer Zn(II) and Cd(II) tolerance due to reduced accumulation (56). The pI258 cadA gene also complemented the Zn(II)/Cd(II)/Pb(II)-sensitive phenotypes of an E. coli zntA-disrupted strain (41). While the E. coli zntA gene is positively regulated by ZntR, cadAand ziaA are negatively regulated by the CadC (25) and ZiaR (56) repressors, respectively, both of which are members of the ArsR family of metalloregulatory proteins (50). CadC responds to Zn(II), Cd(II), and Pb(II), the same metal ion specificity as the pumps themselves (43).
SUMMARY AND PERSPECTIVES
Within the last 5 years, much progress has been made in understanding the mechanism of action and evolution of soft-metal ATPases. The evolutionary pressure to flourish despite the geological omnipresence of metals has ensured that gene families for soft-metal resistances are not confined to a single species or even a single kingdom. Many questions remain to be answered, and we look forward to an accelerated acquisition of knowledge in the near future.
One question is the function of ArsA homologues. Clearly in bacteria the arsA gene encodes the catalytic subunit of the ArsAB pump. It is not known whether the eukaryotic and archealarsA homologues are orthologues or encode proteins with unrelated functions. Eukaryotes have resistance mechanisms for arsenicals. In both Leishmania and Chinese hamster cells we have shown that resistance is related to active extrusion of arsenite (44). But at this time the genes or gene products that produce the resistance have not been identified.
A second question is the distribution of chaperones for soft metals in bacteria. While homologues of copper chaperones such as Atx1p and Lys7p are widely distributed in eukaryotes (12), they do not appear to exist in bacteria. CopZ serves a chaperone function inE. hirae (10), but homologues with copper chaperone activity have not been found in other bacteria. Additionally, it is not clear whether cells require chaperones for non-redox-active metals such as Zn(II), Cd(II), and Pb(II).
A third question is the distribution of ZntA homologues in nature. The related Cu(I)-translocating P-type ATPases are found in most organisms. In humans these pumps are required for copper homeostasis, and mutations in either the ATP7A or ATP7B gene produce inborn errors of copper metabolism, resulting in Menkes or Wilson disease, respectively. Even though zinc is not as toxic as copper, in part because it is not a redox-active metal, it is still toxic in excess, and mechanisms to prevent overaccumulation must be present. To date a growing number of zntA and cadA genes for zinc-translocating P-type ATPases have been identified. Genes for putative ATP-dependent zinc pumps are being discovered in other kingdoms, for example in the genome of the archeaonMethanobacterium thermoautotrophicum (GenBank accession no. 2621474) and in the genome of the plant A. thaliana (GenBank accession no. 4210504). Within the next 5 years the sequencing of the human genome—and many others—will be completed. At that point the phylogenic distribution of zinc pumps and their involvement in human health and disease will be better understood.
Research in our laboratory is funded by U.S. Public Health Service grants GM55425 and GM52216 to B.P.R and National Research Service Award GM18973 to C.R.
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42a.↵
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Q: Adding in SQL, adding Income, Expenses, Sorting by Name would like to ask for help if there is a way to do this?
any suggestion please thank you.
I have this table on my database for example

And want to have a result like this one

A: You can do conditional aggregation:
select
    sum(case when money_type = 'Income' then amount else 0 end) total_income,
    sum(case when money_type = 'Expenses' then amount else 0 end) total_expenses,
    ...
from mytable

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text:
Q: Automate running files in R I need to automate a process in R. Basically I have a an R script (I will call it R1) that needs three separate files to run. These three files are the results output of one trial in my study.
For each run of R1 on these three files, I obtain the summary results for one trial, in a csv file, plus 32 graphs for each decision point in the trial.
One subject goes through nine trials.
I was thinking about putting all the files originally generated by one subject in one big folder, so I will have 27 files (three files times nine trials). This way I won't have to change working directory multiple times (I wonder if there is a way to have R open a folder with a certain name as directory, run a scripts, move the directory to the next folder, run the script again...)
The nine trials are specified by the labels: AA AB AM BA BB BM MA MB MM.
So for subject 1, trial 1, I will have three files with the ending …mov1_AA
After a run of the three files corresponding to one trial, R should save the csv summary output in a separate folder called "summary_mov1" and name the file summary_mov1_AA, and so on. R should save the 32 graphs in a different folder, named mov1_graphs, graph1_mov1_AA, graph1_mov1_AB and so on.
Ideally, after the script has gone through the nine trials, another R script called R2 should take the nine CSV files and build some graphs out of them.
Once R has run the R1 script nine times, I would proceed to a new subject.
So basically:

*

*use R1 with three mov1 files, get a summary csv file in a summary folder (plus 32 graphs in a different folder).

*do this nine times. Once one gets the nine CSV summary files in the same folder, use R2 to average them and build a graph.

*Then do this for each subject (right now I have 7).
I have never done this type of automation so I am a bit lost. Any suggestions? Any examples you can point me to? Which would be the best workflow? At which level should I automate and which things should I rather do by hand?

A: The following does not answer your question in terms of all the names you use, since I did not quite get all the combinations you need. However, the following code demonstrates how you could basically create directories, read/wite csv files, write plots into files, etc. and loop over various files. I have only used some nonsense data, plots, etc. for the purpose of demonstration (in future questions please try to provide some exemplary data.). You will have to adapt the calculations and plotting to your needs. Please also note that you might use different data structures for storing objects, I just used lists here for the simple example.
# make sure you are in a safe directory!
# define dirs
dir_project = "test"
dirs = list(
dir_project = dir_project
,dir_data = paste0(dir_project, "/data")
,dir_summary = paste0(dir_project, "/summary")
,dir_plots= paste0(dir_project, "/plots")
)
# create dirs
lapply(dirs, dir.create)
# create some exemplary data and write it in dir
m = matrix(1:4, nrow = 2)
data = list(m1 = m, m2 = m, m3 = m
            ,n1 = m, n2 = m, n3 = m)
for (i in 1:length(data)) {
  write.csv(data[[i]], file = paste0(dirs[["dir_data"]], "/", names(data[i]), ".csv"))
}

# read data as if it were your files
# assuming that the desired patterns of the filenames are known
# you can loop over them
patterns = c("m", "n")
for (p in patterns) {
files = list.files(dirs[["dir_data"]], pattern = paste0(p, "\\d.csv"), full.names = T)
data = lapply(files, read.csv)
names(data) = gsub(".csv", "", basename(files), fixed = T)
for (i in 1:length(data)) {
  png(file = paste0(dirs[["dir_plots"]], "/", names(data)[i],  "_plot.png"))
  plot(data[[i]])
  #turn off the graphics device
  dev.off()
}
# do some summary thing - of course, this depends on what you want as summary
# here I just bind all matrices together and call the standard summary()
data_summary = do.call(rbind, data)
#      X V1 V2
# m1.1 1  1  3
# m1.2 2  2  4
# m2.1 1  1  3
# m2.2 2  2  4
# m3.1 1  1  3
# m3.2 2  2  4
write.csv(as.data.frame(summary(data_summary))
          , file = paste0(dirs[["dir_summary"]], "/", paste0(names(data), collapse = "_"), "_summary.csv"))
}

# check output
list.files(dirs[["dir_plots"]])
# [1] "m1_plot.png" "m2_plot.png" "m3_plot.png"
# [4] "n1_plot.png" "n2_plot.png" "n3_plot.png"
list.files(dirs[["dir_summary"]])
# [1] "m1_m2_m3_summary.csv" "n1_n2_n3_summary.csv"
read.csv("test/summary/m1_m2_m3_summary.csv")
# X Var1     Var2          Freq
# 1   1   NA        X Min.   :1.0
# 2   2   NA        X 1st Qu.:1.0
# 3   3   NA        X Median :1.5
# 4   4   NA        X Mean   :1.5
# 5   5   NA        X 3rd Qu.:2.0
# 6   6   NA        X Max.   :2.0
# 7   7   NA       V1 Min.   :1.0
# 8   8   NA       V1 1st Qu.:1.0
# 9   9   NA       V1 Median :1.5
# 10 10   NA       V1 Mean   :1.5
# 11 11   NA       V1 3rd Qu.:2.0
# 12 12   NA       V1 Max.   :2.0
# 13 13   NA       V2 Min.   :3.0
# 14 14   NA       V2 1st Qu.:3.0
# 15 15   NA       V2 Median :3.5
# 16 16   NA       V2 Mean   :3.5
# 17 17   NA       V2 3rd Qu.:4.0
# 18 18   NA       V2 Max.   :4.0

# delete the test directory and all data (just to have a clean example here)
unlink("test", recursive = TRUE)


text:
Global PokédeX Plus Forums -> -> Profiles -> Accepted Profiles
Olivia Prewitt
Sad Girl In the City
Name: Olivia Anne Prewitt
Hometown: Olivia was born in Lilycove and traveled to Noverus when she was in Highschool. To her, it was simply a matter of learning a new route to school.
Appearance: Olivia keeps her raven-black hair short, grazing her jaw at its longest. She combs it meticulously, leaving it shiny and straight, but does not seem to be bothered if it gets mussed; she will not immediately seek to set it right, only doing so when and if time permits. She usually wears either a long white-grey overcoat over her clothing, or a white cape with a capelet (smaller cape) around her shoulders, like a shawl. Her clothes usually consist of long sleeve white shirts and a dark grey or black skirt, with a sweater if the weather is prohibitively cold. She keeps her pokéballs in a pocket in her jacket or cape, hidden. The jacket and cape both serve to hide her figure, which is on the average side of attractive. A pair of knee high black stockings and black flats round out her usual attire. Her skin is pale and without mark, and if she wears make up, it is so subtle as to be invisible. There is hardly ever anything more than a blank expression on her face, and the variations are in the mild negative strata of facial emotions: annoyance, confusion, and a hint of pervading sadness, mostly in her eyes. The one exception to her grayscale clothing scheme is a boater hat that belonged to her mother. It is white, but with a red band around it. When she wears it, there is a nearly undetectable spring in her step. She does not wear it often.
Personality: Olivia is very terse and stoic. She will not react to even the most grievous provocation, at the most giving the perpetraitor a raised brow as if to say, "you are confusing, go away". Her speech is terse and clipped, not because she is annoyed by the speaker, simply because there is no reason to her to put energy into conversation. The same goes for pokémon battles, and this is also where most of the emotional changes to her features come. She cares for her pokémon, but it is hard to see it because she seems incapable of grand emotions.
This is not to say that she will not step in and battle if she feels it is necessary, however she is more apt to stay out of battles that do not directly affect her unless asked or ordered to do so.
In situations where human interaction is required, she will stay as far in the background as circumstances allow. If it is a party or raid situation, some people, both with her group and opposing it, may never know she is there, despite the fact that her outer garments are always white. If forced to take the lead in any situation, she shows no fear. She is not afraid to be around people or to speak, she simply has no desire to seek those positions out.
Biography: Olivia was born to Thomas and Allison Prewitt in Lilycove City. Her father was a sailor, and her mother had a business raising and training pokémon for people who could not, or would not, do it themselves. This usually saddled her with hard-to-control pokémon, which Allison accepted gleefully, as she loved to tame them. She was not cruel in her ways, and the pokémon under her care learned to trust humans well, but there were the occasional injury from a frantic and violent pokémon.
When she was five, Olivia had been brought to work with her mother. This is how it was that she watched an abused and uncontrollable drapion, a then unknown species from a far off and mysterious land called Sinnoh, go on a rampage that ended with her mother's bloody death. Allison had had a panic button installed after she had gotten pregnant, and managed to get Olivia to safety, but was sliced nearly in half when the drapion went berserk. Help arrived too late: Olivia was found in a pool of her mother's blood, stroking her hair calmly. Though there were tear tracks down her face, she did not sob or call out, and was quiet as she was taken away.
Her father did not handle it well and ended up trapped at the bottom of a bottle. While she was still young, Thomas made an lame attempt at taking care of her, but by the time she had entered junior high school, Olivia was taking care of his basic needs; food, shelter, clothing when he would change. Despite all of this, Olivia excelled in school, partially because she did not participate in any extra curricular activities, and did not go on a traditional pokémon journey. When Olivia entered high school, her father disappeared. She was put in a government run foster care system when this was discovered (ironically, by her grades increasing), which elected to send her to a private school in Noverus. She did not seem to mind that, slowly, Noverus had become a police state, so long as no one bothered her directly.
Recently, she was approached by a pair of pokémon who had been traveling together, a purple feline with large white marks on her body, and a small black fox-like creature with bright red fur on her head and feet. Seeming to find kindred spirits, the purrloin being aloof and the zorua being able to avoid detection, Olivia felt a kinship with them that she had felt for no living creature before. She found herself seeking them out, giving them food, even talking to them, until, one day, they followed her back where she was staying, and she allowed them to come in. Since then, they never left her side. She bought her first pokeballs and captured them.
Olivia had been emancipated soon after leaving Lilycove city, and lived in an apartment provided by the foster care system, which was a Magma front. When she discovered some of the research that Magma was doing, she ran from the apartment and found hiding in the poor district. This is where, in a seedy diner that she found work for food, she was introduced to the concept of a returning rebellion. Curious, she followed one of the patrons who had mentioned it to his home and confronted him. Despite his fervent denials, she insisted, until finally, believing himself trapped, he arranged a meeting with his superiors. The plan had been to capture her and hold her, to see if anyone came for her, or if she was a spy for one of the two organizations in Noverus. Instead, she was quiet, unassuming, and unasked for.
A perfect operative. She was recruited on the spot.
Preferred Faction: The Rebellion
Isra, Purrloin
Ability: Prankster
Mother: purrloin - Father: meowth
Moves: Scratch, Growl, Assist, Sand Attack, Payday(egg)
Isra had been one of a pokémon kennel that had been shipped to Hoenn for study. Unlike the daycare, the kennel bred pokémon in bulk and in unhealthy conditions. Her mother and father, a liepard and a persian, had been taken from the streets, but unlike the other "breeders", had been competition pokémon before that, leading to strong bond and litters of strong pokémon. In Isra's youth, she bonded with a female zorua, and managed to get into the same crate. The crate ended up in Noverus, but a botched interception mission caused the crate to be lost and broken. The pokémon scattered, and the two made their way in the new city.
As Olivia's pokémon, Isra is the more outgoing of the two. She will be the one that warns Olivia of danger, and is the first to jump into the fray, unless Olivia gives her the command to stand down.
Nyx, Zorua
Ability: Illusion
Mother: Zoruark - Father: Ninetails
Moves: Scratch, Leer, Pursuit, Fake Tears, Extrasensory (egg)
Nyx had been one of a pokémon kennel that had been shipped to Hoenn for study. Unlike the daycare, the kennel bred pokémon in bulk and in unhealthy conditions. Nyx had been caught from the street to be a breeder, but she was deemed too young and left with the kits to grow. The shoddy keeping of the kennel meant that she was forgotten, and she ended up bonding with a purrloin in that kennel. When packed in a crate to be shipped to Hoenn, the purrloin snuck in and joined Nyx, staying with her out of loyalty. The crate ended up in Noverus, but a botched interception mission caused the crate to be lost and broken. The pokémon scattered, and the two made their way in the new city.
Nyx is as quiet as Olivia herself, and will use her illusion powers to hide, either changing into an unobtrusive pokémon, simply not allowing people to see her. Though both are quiet by nature, Nyx is oddly able to get Olivia to talk. She does this in the privacy of their chambers, turning into a young version of Olivia of the approximate age of 5.
Various potions
Pokeball x4
PokeNav (White)
Additional Notes: It seems that Olivia has several pockets lining her cape and her coat, which, both being a bit larger than she is, can hide most of her gear.
Olivia HAS emotions, but her reactions are subdued. A Rebellion doctor worries what might happen if something happens to illicit a much stronger reaction from her.
Approved! You know what to do.
« Next Oldest · Accepted Profiles · Next Newest »


If you need an inspirational and funny story, this one is for you. The story revolves around the life of Lanie – a graphic designer trying to get life back in order after her cheating husband's death. Will Lanie's cold, broken heart ever heal? The book has all the answers for you.
Could the life of your dreams be the stuff of nightmares? Steadman's debut novel protagonists are a couple – Erin and Mark, who board on a dream honeymoon to the island of Bora Bora. Read the book to find out what happens next!
The author narrates a story of a British couple, returning from vacation. On their way back, Finn pulls over his car at the gas station to use the loo and returns to find no trace of his dear wife Layla. What happens next is enclosed in this absolutely convincing thriller.
This debut novel by Drews is about Beck, a passionate, aspiring musician living under his mom's shadow. Thrilling and powerfully written, this is an explosive debut for YA readers that tackles the dark subject of domestic abuse in an ultimately uplifting tale.
This is a hilarious tale of female friendship, bookshops and fighting for a cause, where Bennett's Bookshop has always been a haven for Paige Turner, where she can escape from her sleepy hometown, hang out with her best friend, Holly and also earn some money.


Learn how-to create and collaborate with Google Docs for professional and classroom use.
When I was a classroom teacher, I remember the nights that I carried home heavy tote bags full of student notebooks to correct work and leave feedback. The next day I'd often get to work and realize I left the pile of notebooks at home, or that I was missing papers which were on my ktichen table!
How did I solve this frustrating problem? My school started using Google Apps, so I had to learn.
At first I was resistant, but once I realized the power of having access to your documents anytime from any device, I was sold. I immediately saw applications for my classroom, professional, and personal life.
Confer on value of Google Apps versus Microsoft Word, Corel Word, etc.
Google Docs for the Connected Classroom will address the relationship between content, pedagogy, and technology while covering the nuts and bolts of Google Docs and how to use this app within the context of your classroom.
My hope is that you can take what you learn in this course and put it in the context of your classroom or your role as an educator. Google Docs for the Connected Classroom will make your life easier and help you use your time more efficiently.
What is Google Docs and what makes it different from other word processing tools?
Learn how-to create and collaborate with Google Docs. You'll discover how-to create private & public documents, adjust the layout, use add-ons, organize with folders, invite others to edit, comment and more!
Find out how-to enhance your curriculum with Google Docs and see how easy it is to use with your colleagues and parents for professional use.
Jennifer is very responsive to student needs – I am amazed at the sheer amount of work it must take for her to respond so thoughtfully to each participant's posts. She always responds with a follow up question or idea that supports a continuing dialogue around the learning. In addition to her direct support of learning, she also organizes a very thorough library of support tutorials that one can return to at anytime, even after the course has ended.
I have recently taken a blended course at another university that met asynchronously, but PLP is always such a wonderful experience. Somehow PLP has really sought to create "connections" and shows their value towards the coaching model of instruction. I can come in not knowing much about a tool and be in an Elluminate space with others with varied experiences and feel that the learning ecosystem is positive but really works to meet the objectives. I highly recommend PLP. When I feel like I am getting "dusty and old" engaging in a PLP course gives me a wonderful boost of the possibilities. I reallly think that using Elluminate helps us connect as it allows us to use the chat as well as use the mic to hear one another respond. It really was excited about how we can share our doc for other in our sharing session using the Elluminate "share" feature.
This course was a terrific learning experience. It's 21st century adult learning that can powerfully impact and improve your skills. The best aspect of the course was the instructor – Jennifer. She is in the real world as a current practicing professional who understands what educators need for their professional development. Self-paced and exciting, this is the way to learn.
The instructors were great facilitators in the course. The webinars provided great opportunities for collaboration. The grouping activities in the webinars kept participants engaged in the learning activities. I also enjoyed all of the additional reading materials and links in the PLP Community.
In just 2 weeks, learn to use the collaborative power of Google Docs in your classroom.
Google Apps 101 has given me confidence and a general understanding of Google Docs. I feel comfortable using Google Docs and have already had success!
I got my specific questions answered and ideas from others on how they are using Google docs!
What I will remember and utilize most from this eCourse is Google drive, templates and groups!
Learn to use Google Docs for your teaching practice. Get expert help from a Google For Education Certified Trainer.


This is a video overview to accompany written instructions for Practice Exercise 1.
we're going to be uploading the file C05-W1-PE-01.
This file contains four quadcopter arms.
the upper and lower sides of these arms to hold them together in flight.


text:
States101.com
State Populations
Gender Ratios
Random State
State Adjectives
State Postal Codes
U.S. Census Bureau | Census.Gov
Crawford County, Illinois Gender Ratios
Gender Ratio:
Total Population:
There are more men than women in Crawford County, Illinois. Total population of Crawford County, Illinois is estimated at 19,393 people with 10,008 male and 9,385 female. There are 623 more men than women in the county, which is 3.21% of the total population.
The Crawford County, Illinois Gender Ratio is 107 men to 100 women (107:100) or 1.07. Crawford County, Illinois's gender ratio is higher than the Illinois State average of 96 men to 100 women (96:100) or 0.96. The gender ratio is also higher than the national average of 97 men to 100 women (97:100) or 0.97.
Note: All ratios are written as Male to Female
Back to Illinois Page
Crawford County, Illinois Gender Ratios By Age
Gender Ratios vary by age group as well as location. The table below shows the gender ratios breakdown in Crawford County, Illinois by age.
Crawford County Ratio
Illinois State Ratio
Nationwide Ratio
0 to 4 92 to 100 104 to 100 104 to 100
10 to 14 100 to 100 104 to 100 104 to 100
40 to 44 128 to 100 99 to 100 100 to 100
55 to 59 106 to 100 95 to 100 93 to 100
65 to 69 89 to 100 89 to 100 79 to 100
80 to 84 68 to 100 † 67 to 100 79 to 100
85 and over 42 to 100 49 to 100 79 to 100
† Due to very low population in this demographic, the ratio shown is not statistically significant.
Cities in Crawford County, Illinois
Gender Ratios on this page are an aggregate of the gender ratios in the following cities within the region:
Annapolis, Flat Rock, Hutsonville, Oblong, Palestine, Robinson, and Stoy.
Other acceptable city names that fall in this region include:
Birds.
Gender Ratios in Washington D.C.
Factors Affecting Gender Ratios
Gender Ratios in Asia
List Countries with the Highest and Lowest Gender Ratios
U.S. Cities with the Best Gender Ratios for Men and Women
© 2022 States101.com. All rights reserved. View Sitemap. Usage is subject to our Terms and Privacy Policy.
States101.com is a free public resource site, and is not affiliated with the United States government or any Government agency
We have detected that your current location is Virginia.
You may also be interested in our sister-site romannumerals.guide — a great resource for teaching roman numerals in the classroom.
** This Document Provided By States101.com **
Source: https://www.states101.com/gender-ratios/illinois/crawford-county


Vilnius, Lithuania - The Pixelmator Team today released Pixelmator Pro 1.2 Quicksilver, a major update to the fast and powerful image editor for Mac. The update adds support for macOS Mojave, including an all-new light appearance, Core ML-powered automatic photo enhancement, batch image processing via the Automator app, and much more.
"Users love Pixelmator Pro for making such powerful image editing tools so incredibly easy to use," said Saulius Dailide, one of the founders of the Pixelmator Team. "And the new ML Enhance is our most powerful feature yet - it lets you dramatically improve the look of any photo with a single click, thanks to a machine learning algorithm trained on millions of professional photos."
The new ML Enhance feature in Pixelmator Pro automatically enhances photos - balancing the colors, evening out exposure, and making changes to individual color ranges - to give you the best starting point for making your own creative edits to a photo. Powered by Core ML and developed using a carefully refined set of millions of professional photos, the machine learning algorithm analyzes photos to detect the objects they contain, then enhances their colors and brings out missing details, leaving the final creative touches to the user.
Founded in 2007 by two brothers, Saulius Dailide and Aidas Dailide, the Pixelmator Team develops Pixelmator - the world's most innovative image editing app for Mac and iOS. Pixelmator has been honored with numerous awards, such as the Mac App of the Year award in 2011, the iPad App of the Year award in 2014, and many more. Pixelmator for iPad was featured at the Apple Special Event in October 2014. All Material and Software (C) Copyright 2007-2018 Pixelmator. All Rights Reserved. Apple, the Apple logo, Macintosh, iPhone, iPad and macOS are registered trademarks of Apple Inc. in the U.S. and/or other countries. Other trademarks and registered trademarks may be the property of their respective owners.


text:
Covid: North Macedonia hospital fire kills at least 10
image sourceEPAimage captionThe clinic in Tetovo was constructed last year to care for people suffering serious effects of Covid-19
At least 10 people have been killed in a fire at a hospital treating Covid-19 patients in North Macedonia.
Footage shared on social media showed a building in flames and a thick cloud of black smoke billowing into the air near a main road in the city of Tetovo.
Firefighters reportedly extinguished the blaze less than an hour after it broke out at about 21:00 local time (19:00 GMT) on Wednesday.
Health Minister Venko Filipce warned the number of casualties could rise.
"This is a very sad day," he wrote on Twitter, adding that several patients had been "urgently transported" to a hospital in the capital Skopje.
"Doctors are fighting for the lives of the injured," Mr Filipce said. He described the fire as a "terrible accident", but provided no further details.
image sourceEPAimage captionSome injured patients were transported to receive care in the capital Skopje
It is unclear how many patients were being treated at the hospital in Tetovo when the incident occurred.
Covid map: Where are cases being reported?
Coronavirus vaccine progress around the world
The facility was reportedly constructed last year to care for people made seriously ill from the coronavirus.
North Macedonia has a population of about two million people.
The country has reported more than 180,000 cases of Covid-19 and 6,153 coronavirus-related deaths since the start of the pandemic, according to Johns Hopkins University data.
Climate change: Fossil fuels must stay underground, scientists say
Theranos founder hit with criminal charges


The council has sacked chief prosecutor Omar Ahmed Mohamed Abdelsalam and deputy public prosecutor Hesham Othman Ibrahim Saleh, as well as head of public prosecutions Amer Ibrahim Majid.
KHARTOUM - The head of Sudan's ruling transitional military council (TMC) has fired the three highest-ranking public prosecutors, the TMC said on Tuesday, after protesters demanded an overhaul of the judiciary as part of steps toward civilian government.
The Sudanese Professionals' Association (SPA) spearheading the revolt has issued a long list of demands for wholesale change to end repression and ease an economic crisis after the military deposed veteran autocrat Omar al-Bashir last week.
In its first news conference on Monday, the SPA - which led weeks of protests that led to Al-Bashir's overthrow after 30 years in power - called for the TMC to be dissolved in favor of an interim civilian ruling council with military representatives.


text:
39 LISTSThe Wonderful World of Disney
Lists about the $92 billion multi mass media entertainment conglomerate and its many, many properties.
The Best Disney Sports Movies
Ranker Film
Updated July 29, 2020 2.4k votes 126 voters 4.0k views59 items
List RulesVote up the best Disney Sports movies.
It's time to determine the best Walt Disney sports movies. Whatever the sport, Disney's probably made a movie about it, from bobsledding to horse racing. Disney has a pretty sizable backlog of often inspirational and comedic sports films, which you can stream across platforms when you bundle your Disney+ subscription. A lot of these movies are classics such as The Mighty Ducks, Cool Runnings and Angels in the Outfield. But are they the top sports films that Disney has to offer? You'll also find famous actors like Denzel Washington in the Disney football movie Remember the Titans. Dennis Quaid and Jon Hamm have both starred in Disney baseball movies. All of which were inspired by true stories. Rest assured, there are Disney movies for every type of sports fan out there.
Which of these Disney sports films do you love? Vote up all your favorites and vote down the movies that didn't have you cheering in the stands. Also, be sure to check back for new Disney sports films as they are released.
Hayden Panettiere, Ryan Gosling
Directed by: Boaz Yakin
Remember the Titans is a 2000 American sports drama film produced by Jerry Bruckheimer and... more on Wikipedia
More Remember the Titans
#340 of 553 The Greatest Epic Movies Ever Made#977 of 1,540 The Most Rewatchable Movies
Kurt Russell, Patricia Clarkson
Directed by: Gavin O'Connor
Miracle is a 2004 American sports docudrama about the United States men's hockey team, led by... more on Wikipedia
Dennis Quaid, Brian Cox
Directed by: John Lee Hancock
The Rookie is a 2002 sports drama film directed by John Lee Hancock and produced by Walt... more on Wikipedia
The Mighty Ducks
Emilio Estevez, Joss Ackland
Directed by: Stephen Herek
The Mighty Ducks is a 1992 American sports comedy film directed by Stephen Herek, starring... more on Wikipedia
John Candy, Malik Yoba
Directed by: Jon Turteltaub
Cool Runnings is a 1993 American sports film directed by Jon Turteltaub, and starring Leon,... more on Wikipedia
More Cool Runnings
#187 of 277 The Top Tearjerker Movies That Make Men Cry#148 of 629 The Best Black Movies Ever Made, Ranked
Elizabeth Banks, Mark Wahlberg
Directed by: Ericson Core
Invincible is a 2006 sports film directed by Ericson Core set in 1976. It is based on the true... more on Wikipedia
Diane Lane, John Malkovich
Directed by: Randall Wallace
Secretariat is a 2010 biographical sports drama film produced and released by Walt Disney... more on Wikipedia
D2: The Mighty Ducks
Kareem Abdul-Jabbar, Wayne Gretzky
Directed by: Sam Weisman
D2: The Mighty Ducks is a 1994 American sports comedy film directed by Sam Weisman. It is a... more on Wikipedia
McFarland, USA
Kevin Costner, Maria Bello
Directed by: Niki Caro
McFarland, USA is an American 2015 sports drama film directed by Niki Caro and produced by... more on Wikipedia
More McFarland, USA
#97 of 172 The Best Sports Movies Ever Made#24 of 55 The 30+ Greatest Sports Drama Movies of All Time
Emily Deschanel, Jon Voight
Directed by: James Gartner
Glory Road is a 2006 American drama sports film directed by James Gartner, based on a true... more on Wikipedia
Shia LaBeouf, Peyton List
Directed by: Bill Paxton
The Greatest Game Ever Played is a 2005 biographical sports film based on the early life of... more on Wikipedia
More The Greatest Game Ever Played
#59 of 82 The Best Movies Based on Non-Fiction Books#34 of 101 The Best Movies About Underdogs
Angels in the Outfield
Matthew McConaughey, Joseph Gordon-Levitt
Directed by: William Dear
Angels in the Outfield is a 1994 remake of the 1951 film of the same name. The film stars... more on Wikipedia
Tom Hanks, Billy Crystal
Directed by: John Lasseter, Joe Ranft
Cars is a 2006 American computer-animated comedy-adventure sports film produced by Pixar... more on Wikipedia
Joshua Jackson, Emilio Estevez
Directed by: Ron Lieberman
D3: The Mighty Ducks is 1996 American sports comedy film directed by Robert Lieberman. It is... more on Wikipedia
Air Bud
Mark Jackson, Kevin Zegers
Directed by: Charles Martin Smith
Air Bud is a 1997 American family comedy film that sparked the franchise centered on the... more on Wikipedia
More Air Bud
#123 of 145 The Most Inspirational Sports Movies#79 of 190 The Greatest Animal Movies Ever Made
Johnny Tsunami
Lee Thompson Young, Kirsten Storms
Directed by: Steve Boyum
Johnny Tsunami is a 1999 Disney Channel Original Movie. It was nominated in 2000 for the... more on Wikipedia
Brink!
Erik von Detten, Geoffrey Blake
Directed by: Greg Beeman
Brink! is a 1998 Disney Channel Original Movie set in the backdrop of aggressive inline... more on Wikipedia
The Strongest Man in the World
Kurt Russell, Cesar Romero
Directed by: Vincent McEveety
The Strongest Man in the World is a 1975 Disney film starring Kurt Russell, still a student in... more on Wikipedia
Helen Hayes, Stefanie Powers
Herbie Rides Again is a 1974 comedy film. It is the sequel to The Love Bug, released six years... more on Wikipedia
The Love Bug
Buddy Hackett, Dean Jones
The Love Bug, sometimes referred to as Herbie the Love Bug, is the first in a series of comedy... more on Wikipedia
More The Love Bug
#50 of 97 The Best Disney Live-Action Movies#201 of 925 The All-Time Greatest Comedy Films
Henry Gibson, Ryan Merriman
Directed by: Paul Hoen
The Luck of the Irish is a 2001 Disney Channel Original Movie. It has been shown in reruns... more on Wikipedia
Double Teamed
Mackenzie Phillips, Joey Miyashima
Directed by: Duwayne Dunham
Double Teamed! is a 2002 Disney Channel Original Movie based on the life stories of... more on Wikipedia
Motocrossed
Riley Smith, Mary-Margaret Humes
Motocrossed! is a 2001 Disney Channel Original Movie about a girl named Andrea Carson who... more on Wikipedia
More Motocrossed
#2 of 14 Disney Channel Original Movies You Somehow Forgot About#3 of 20 The 20 Best Motocross Movies Of All Time
Herbie Goes to Monte Carlo
Don Knotts, Dean Jones
Herbie Goes to Monte Carlo is a 1977 film, the third of a series of films by Walt Disney... more on Wikipedia
More Herbie Goes to Monte Carlo
#63 of 130 The Greatest Car Movies Ever Made#41 of 106 The Best Kids Movies Of The 1970s
Owen Wilson, Michael Caine
Directed by: Brad Lewis, John Lasseter
Cars 2 is a 2011 American computer-animated action comedy spy film produced by Pixar Animation... more on Wikipedia
More Cars 2
#358 of 575 The Best Animated Films Ever#141 of 306 The Best Movies For Kids
EntertainmentDisney
Top 10 Current Queries in Films: best teenage love story movies on netflixfunny female fightspg 13 romantic moviesjane march moviesmovies from 1900milo and otis deathsantm secretsoscar winning true story moviesdennis hopper funnymunich movie cast


I woke up with the beginning of a cold so I rested in the morning and then felt better by the afternoon. If I had a regular 9-5 job, I would not have been able to take the morning off. This led me to think of the joy of working at home.
3. Being able to work in pajamas if you feel like it.
4. Having an office kitty.
5. Commuting from the downstairs to upstairs.
6. Being able to concentrate without people talking/answering phones.
7. Less germs during cold/flu season.
8. Ability to create anytime you feel inspired.
10. No office politics or drama.
Now some of these benefits might seem like drawbacks to others, especially those who like the social aspects of working with other people. I personally love the solitude.
But when I feel like I'm lonely, then I go out and meet friends and colleagues for lunch dates or go see a movie matinee in the afternoon. I used to perform plays and would get a lot of social interaction in the evenings during rehearsals and performances.
As a radio producer, I meet with people to interview them as well as volunteer producing and hosting a weekly arts show. As a writer and consultant, I also get asked to speak at colleges, universities and college groups so there are plenty of opportunities for to meet and talk with people.
Mostly though, I love working at home. What are your experiences? Please share your thoughts on the benefits or drawbacks about working at home and post your comments!


For almost 30 years, Kitchen Village has been recognized as one of the leading full-service providers of kitchen and bath renovations throughout the northwest suburbs of Chicago.
At Kitchen Village, we help you create the perfect kitchen or bathroom from concept to completion. Our team of award-winning designers have extensive experience in creating stunning designer kitchens and baths that will enhance your home's appearance while increasing its overall value.
the kitchen or bath of your dreams….
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text:
Q: Comparing fields of object store in arraylist using iterator I am passing an integer value address to this function. This integer value is contained by one of the object stored in Arraylist "instrHolder". Now I want to first find out which object contains this value and return the entire object of type "Instruction". Here is what I am trying -
private static Instruction getInstruction( int address) {
    Iterator<Instruction> iterator = instrHolder.iterator();
    while(iterator.hasNext()){
        if(/*condition need to know*/)
        return /*need to know*/;
    }
}

How should I write the if condition and what should be my return statement? Please help me out?

A: iterator.next() will give you the current instance of the List. You should check your condition on that instance and return it if the condition is satisfied :
private static Instruction getInstruction(int address) {
    Iterator<Instruction> iterator = instrHolder.iterator();
    while (iterator.hasNext()) {
        Instruction current = iterator.next();
        if (current.getSomeProperty().equals(someValue))
            return current;
    }
    return null;
}

As hinted by Spotted, you should decide what to return if no element of your list matches the condition. I chose to return null in this case.

A: You can use iterator.next() and because you wanted to compare integer address, you can refer below code:
while (iterator.hasNext()) {
            Instruction instruction = iterator.next();//Get single instruction
            //Get getAddress() from instruction object
            if (instruction.getAddressValue() == address) {
                return instruction;
            }
        }

A: Since instrHolder is an ArrayList, don't bother with an Iterator. Rather use Stream and Optional. Also, in your code the behavior is not specified in case no element matches the address. In the code below it throws an exception, but it can also return a default value (with orElse()).
private static Instruction getInstruction( int address) {
    return instrHolder.stream()
                      .filter(i -> i.getAddress() == address)
                      .findFirst()
                      .orElseThrow(NoSuchElementException::new);
}


A limited number of meeting facilities were found in Deyang, China. Your search was widened to include meeting facilities within 300 miles of Deyang, China. To find more area meeting facilities, click the Zoom link shown above.


Where do you get the ephatch.com stickers with your region of the country?
there was a guy in nashville that had southeast EPhatch stickers, but I've not seen him since the crash. if you want a regular EPhatch sticker, pm oogy-boogy.


Gigaba instead criticised the local tourism sector for not doing enough to sell South Africa as a destination for visitors, adding that other factors, including a constrained global economy, had also contributed to the decline of tourism numbers. The outspoken Minister, who had stuck by his guns on the country's controversial visa reforms, stopped short of outright criticism of the South African Reserve Bank – the latest organisation to raise concerns about the effects the regulations were having on tourism figures.
"That the number of travellers dropped because of the new visa regulations is always an opinion. And the Reserve Bank is entitled to its opinion and also entitled to be wrong," scorned the minister.
He was answering questions on Sunday during a media briefing by the state's governance and administration cluster.
The new visa regulations, among a number of changes made to immigration regulation, require children traveling to and from South Africa to carry an unabridged birth certificate. They also require foreign travellers seeking to obtain visas to South Africa to apply in person and provide biometric data.
But in its latest quarterly bulletin – a publication that the bank releases four times a year and that provides critical and highly trusted data on the country's economy – the Reserve Bank said large reductions in dividend and travel receipts, probably related to stricter South African visa regulations, had implications for South Africa's balance of payments reports the Mail & Guardian.
The bank report claims that the number of children younger than 18 years constitutes a sizeable portion of tourists in South Africa and in this sector there had been a marked drop in tourists, "Relative to the total number of tourists, the number of children dropped from 7.3% in 2014 to 6.4% in the first five months of 2015.
Yet once again Gigaba said that the department was not averse to the issues and concerns that have been raised adding that constructive proposals to mitigate the potential unintended consequences of the new regulations had been made in the inter-ministerial committee on migration, chaired by Deputy President Cyril Ramaphosa.
The process was "at an advanced stage" Gigaba said during the meeting, but he would not elaborate on the status thereof.


text:
- Russian film director Sergei Eisenstein in 1898
- actor Dan Duryea in 1907
- comedian Ernie Kovacs in 1919
- actor Jeanne Moreau in 1928
- actor/singer Chita Rivera in 1933 (age 90)
- actor Gil Gerard in 1943 (age 80)
- actor Rutger Hauer in 1944
- actor Richard Dean Anderson in 1950 (age 73)
- airline pilot Chesley Sullenberger in 1951 (age 72)
- Princess Caroline of Monaco in 1957 (age 66)
- actor Gail O'Grady in 1963 (age 60)
- actor Mariska Hargitay in 1964 (age 59)
- actor Tiffani Thiessen in 1974 (age 49)
- actor Julia Jones in 1981 (age 42).
Today is Sunday, Jan. 22, the 22nd day of 2023 with 343 to follow.


Sarah Heath asks Are You Ok?
Bozell Blasts CNN, NBC, ABC and CBS Reporting of Planned Parenthood Videos; Calls on Networks To Show THEIR Edited Footage.
Move over Netflix, Dove Channel is here.
Interview: Pat 'Nobody' Taylor on His Escape From Infamous OC Punk Rock Scene.
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text:
Institution: Glasgow
A. AASLAND. 1994. Russians in Latvia: Ethnic identity and ethnopolitical change. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 79.25%
A.Z. ANDRZEJEWSKA. 2009. M. E. Saltykov-Shchedrin's plays in the context of nineteenth-century Russian drama. M.Litt. thesis. Glasgow. Added by: gerard Pop. 78.98%
B.L. APPLEBY. 1975. The relations between the Slovaks and the central government of the First Czechoslovak Republic, 1918-1938. M.Litt. thesis. Glasgow. Last edited by: gerard Pop. 80.86%
R.J. ARNOT. 1985. The Shchekino experiment: The question of control over the Soviet industrial workforce. Ph.D. thesis. Glasgow. Added by: gerard Pop. 76.83%
A. ARTUN. 2007. Polish foreign policy between East and West, 1989-2004. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 75.94%
J. BACONOVÁ. 2005. Russian drama at the turn of the 19th and 20th centuries. M.Litt. thesis. Glasgow. Last edited by: gerard Pop. 74.96%
M.J. BAIN. 2001. Soviet / Cuban relations 1985-1991. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 69.86%
C. BAIN. 2007. Entrepreneurship in Russia: Patterns and problems of its development in the post-Soviet period. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 71.38%
GAVIN BAPTIE. 2011. Issues in Rusyn language and standardisation. MPhil thesis. Glasgow. Added by: gerard Pop. 59.3%
Z. BARBU. 1954. The psychology of democracy, Nazism and Communism. Ph.D. thesis. Glasgow. Added by: gerard Pop. 72.36%
VLAD-VICTOR BARNAURE. 2014. Essays on open-economy macroeconomics in emerging Europe [with special reference to the Czech Republic]. PhD thesis. Glasgow. Last edited by: Gregory Walker Pop. 41.95%
V. BARNETT. 1992. At the margins of the market: Conceptions of the market and market economics in Soviet economic theory during the New Economic Policy, 1921-1929. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 68.25%
J.M. BATES. 1997. The PUWP's preferences in the contemporary Polish novel, 1959-1985. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 64.13%
ANNA BATORI. 2017. Enclosed spatial formations: Space and place in the socialist and post-socialist Romanian and Hungarian cinema. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 20.84%
R. BECHER. 1955. A comparative study of primary spatial prepositions in modern literary Russian and Polish. B.Litt. thesis. Glasgow. Last edited by: gerard Pop. 73.7%
R. BELL. 2007. Twentieth-century reception and representation of Czech modernist art within the UK and Anglo-American writings. M.Phil. thesis. Glasgow. Last edited by: gerard Pop. 73.52%
D.J. BETZ. 2002. Politics of mimicry - politics of exclusion: Comparing post-communist civil-military relations in Poland and Hungary, Russia and Ukraine, 1991-1999. Ph.D. thesis. Glasgow. Last edited by: Gregory Walker Pop. 72.54%
J. BIGGART. 1969. The career of B. M. V´yunov: A case-study in the sovietization of Lithuania and in Soviet agricultural administration, 1945-1960. B.Litt. thesis. Glasgow. Added by: gerard Pop. 67.26%
ELEANOR F. BINDMAN. 2013. Economic and social rights within EU-Russian relations: A missed opportunity? PhD thesis. Glasgow. Last edited by: Gregory Walker Pop. 38.73%
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text:
package model;

import java.util.Arrays;

@SuppressWarnings("serial")
public class TDArc extends Arc{

	public int[] costs;

	public TDArc(int maxTime) {
		super();

		this.costs = new int[maxTime];
	}

	public TDArc(Arc arc, int maxTime) {
		super(arc);

		this.costs = new int[maxTime];
		for (int i = 0; i < maxTime; i++)
			this.costs[i] = arc.getCost();
	}

	public TDArc(int targetId, int[] costs) {
		super(targetId, costs[0]);

		this.costs = costs;
	}

	public TDArc(long targetId, int[] costs, boolean arcFlag, long shortcutNode) {
		super(targetId,costs[0],arcFlag,shortcutNode);
		this.costs = costs;
	}

	@Override
	public TDArc copy() {
		return new TDArc(this.headNode, this.costs, this.arcFlag, this.shortcutNode);
	}

	@Override
	public Arc reverseEdge(long v) {
		return new TDArc(v, costs, arcFlag, shortcutNode);
	}

	/**
	 * Get cost at specific time point
	 * @param time
	 * @return
	 */
	public int getCostForTime(int time) {
		return costs[time];
	}

	/**
	 * Sets the cost for a specific time
	 * @param cost
	 * @param time
	 */
	public void setCostForTime(int cost, int time) {
		costs[time] = cost;
	}

	public int[] getCosts() {
		return costs;
	}

	public void setCosts(int[] costs) {
		this.costs = costs;
	}

	@Override
	public String toString() {
		return "("+headNode+", "+cost+", "+arcFlag+", "+shortcutNode+","+Arrays.toString(costs)+")";
	}
}

redpajama_set_name: RedPajamaGithub


text:
San Francisco Bulls Put $2 Million In Renovations Into Cow Palace
By Ernie Pomin Aug 30, 2012, 10:59am PDT
Share All sharing options for: San Francisco Bulls Put $2 Million In Renovations Into Cow Palace
The San Francisco Cow Palace once more has a permanent resident, and the ECHL's San Francisco Bulls are cleaning the place up a bit.
According to CSN Bay Area, the Bulls will be putting up $2 million for renovations into the arena as they get set for the October 12 start of their inaugural season in the Bay as San Jose Sharks affiliates.
Bulls president and coach Pat Curcio noted on his blog that the main expenditure will come in the form of a state-of-the-art scoreboard known as "The Cube." It will provide 360-degree views along with a updated sound system. To go along with the new scoreboard, the concession areas will be getting a facelift as well.
The Bulls are obviously looking to stay in San Francisco for the long haul with these additions. The renovations should help the Bulls survive longer than the San Francisco Spiders, who played their one and only season back in 1995 at the Cow Palace, the last time it was home to a professional hockey team.
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