It is a curious irony that you end up needing a holiday after trying to book a holiday online.
I still feel that travel is an area that is lagging behind, when it comes to ecommerce and the user experience (which often leaves a lot to be desired). These sites need to work so much harder than their retail counterparts, for all kinds of reasons.
Booking a holiday is a leap of faith if you're visiting somewhere for the first time, and the pre-customer experience is absolutely vital. Attention to detail is paramount.
But every year it's the same: I brace myself before spending countless hours researching possible destinations, knowing fine well that I'm going to encounter all manner of frustration during the process.
Here are 13 UX issues that I've come across over the weekend, while trying to a) find a hotel / villa, and b) hand over a not inconsiderable sum of money in return for c) a fantastic experience. Many of them are easy to fix. Some may seem trivial, but putting any doubt in the mind of the prospective buyer is a dangerous move.
I guess this is a business decision, but in 2013 I expect to be able to a) see prices, and b) book online. Moreover, the 'Prices and Booking' label in this expandable section suggests that there are prices to show.
There aren't. Why not show a price range, at the very least?
I'd be willing to bet that there isn't a single person in the world who appreciates videos and sound that automatically start to play. I typically open up lots of tabs when researching holiday destinations, and hunting through 30 tabs to find the page that is offending my ears is the opposite of 'magnificent'.
In addition, this page was difficult to read. Small, light grey, unformatted text against a white background is a bad choice for readability.
For reasons I cannot fathom TravelSupermarket makes you manually enter dates as text. Perplexing.
Last year the Four Seasons launched its new website, as part of an $18m investment into its web strategy. It looks stunning, but there remains some room for improvement, as far as the user experience is concerned.
A question: Do you ever go on holiday for 11 nights? I suspect the vast majority of travellers go away for either one or two weeks.
As such it makes sense to allow people to choose the number of nights they want, and automatically calculating the check out date… something I can't do on the Four Seasons site.
Dodgy labelling aside, it's 2013! Again, this may be a business model issue, but we live in a world of APIs, and sites that are plugged in to booking engines are much better for those prepared to buy online.
The reliance on this sort of enquiry system makes for a disjointed, tardy experience.
Those high contrast 'Our review' and 'Book now' buttons are fine, but I instinctively click on images, which are more alluring and which seem to attract my mouse pointer.
A small thing, I know, but very easy to fix.
This is all too common: date drop downs where months do not mix. If I want to check in on Saturday 27 July I need to scroll through to the next month in order to select Saturday 3 August as my check out date.
Why not show the dates in this panel?
This might as well say 'Last updated more than six months ago'. It may be an error, but it instills a lack of trust in the booking process.
The product page on this website leads on images, as many travel sites do. When it comes to holidays, a picture really is worth a thousand words.
But I don't think this is the best implementation. I prefer to see a big image, and at least a little description text without the need to scroll.
In this example, the booking functionality has been demoted by the 'get a quote' form. If I hadn't scrolled down, I would have assumed that I couldn't book online.
I wonder how many people leave this page without realising that you can in fact book online.
It's still whirring away. Does this five-star resort always keep people waiting?
This form appeared immediately after I clicked 'Offers'. Not exactly the best timing!
Yes, we see these forms on all kinds of other websites, but I encountered them a handful of times during my holiday research.


Because it's her. And I can't argue with that!
We have several fun things we plan to add to this site in the next week, but feel free to look around learn a little more about the who, what and why behind #fashionbyMayhem.
What a natural talent!!! Both of you are talented, and mom you don't think you are, but you indeed are. Who needs a sewing machine when you have paper and tape! What a wonderful thing the two of you are doing! No matter what Mayhem does in her life, you are building such a bond, and memories with her. That is a gift far greater than all the electronic toys, and gadgets parents give so freely now. You are giving her time and attention, and she is learning so much! Without realizing she is building math skills, problem solving. She is planning and learning, and having so much fun! It shows in your pictures! I am very impressed! But mainly keep enjoying being together! Wonderful that you are able to spend the time with her, so many moms don't have the time.
This yellow dress is my favorite so far, from the amazing Mayhem design team. And what a team you are. I really really really love this stuff you are creating. I wonder if Tim Gunn has seen these. Hard to imagine that he wouldn't be impressed. Wonderful stuff.


text:
Uitslag Veloopzwem De Haan top 3
23/03/2019 · 0.50 - 27 - 8.60
1 Heemeryck Sander 00:06:2484.80 00:39:2190.54 00:27:2391.62 01:13:48 92.05
2 Vandenbroucke Sven 00:05:5186.98 00:38:5590.12 00:28:3888.56 01:14:00 90.89
3 Van hamme Tim 00:05:5286.88 00:38:5690.09 00:28:5688.06 01:14:19 90.64
4 Hernaert Antonio 00:06:0385.75 00:38:4890.33 00:29:0887.73 01:14:32 90.47
5 Lemmens Tuur 00:05:1191.08 00:39:3289.01 00:29:5486.47 01:15:18 89.87
6 Wera Joachim 00:05:4887.29 00:38:5590.12 00:30:0586.17 01:15:27 89.75
7 Van Vooren Brecht 00:05:4987.19 00:38:5790.06 00:31:0784.46 01:16:30 88.93
8 Vanden Broucke Giani 00:06:3582.48 00:40:5986.39 00:28:2189.03 01:16:32 88.90
9 Cool Hannes 00:06:3682.37 00:39:5788.25 00:29:2587.27 01:16:46 88.72
10 Dieussaert Dennis 00:06:2883.19 00:39:1089.67 00:30:4984.96 01:17:11 88.39
11 Marclé Xander 00:06:0185.96 00:38:4690.39 00:31:5883.06 01:17:22 88.25
12 Schoonbaert Galliano 00:06:0985.14 00:39:3488.95 00:31:2084.11 01:17:47 87.92
13 Paermentier Michiel 00:06:2883.19 00:39:1589.52 00:31:2284.05 01:17:47 87.92
14 Dewaele Quinten 00:06:3582.48 00:39:1089.67 00:31:2883.89 01:17:53 87.84
15 Scherpereel Andres 00:06:1384.73 00:39:3488.95 00:31:2883.89 01:17:54 87.83
16 Penne Pieterjan 00:06:4981.04 00:39:4388.68 00:31:1784.19 01:18:28 87.38
17 De Smedt Brecht 00:06:3682.37 00:39:1489.55 00:32:0882.79 01:18:34 87.30
18 Verbelen Remco 00:05:3988.21 00:40:5786.45 00:31:2284.05 01:18:40 87.22
19 Vandenbroele Niels 00:06:3982.07 00:39:0389.88 00:32:4181.88 01:19:04 86.91
20 Pieter Luyckx 00:06:1284.83 00:39:3588.92 00:32:5381.55 01:19:20 86.70
21 Patteeuw Brent 00:07:0879.09 00:39:3289.01 00:32:2582.32 01:19:44 86.39
22 Mariën Toon 00:06:5680.32 00:42:1584.10 00:29:5986.33 01:19:51 86.29
23 Verlet Benjamin 00:07:2277.66 00:40:1187.83 00:31:5283.23 01:20:06 86.10
24 De Smedt Volkwin 00:06:2084.01 00:39:3289.01 00:33:4180.23 01:20:09 86.06
25 Steyaert Kris 00:06:5780.22 00:39:3788.86 00:33:0781.17 01:20:29 85.80
26 Claeys Lorenz 00:07:1878.07 00:40:0987.89 00:32:4081.91 01:20:54 85.47
27 Hamerlinck Steven 00:07:2077.87 00:40:1187.83 00:32:4281.85 01:20:56 85.44
28 Lemaître Loïc 00:07:5973.87 00:41:0686.18 00:31:1284.33 01:20:59 85.40
29 De Volder Arthur 00:06:4681.35 00:40:3986.99 00:32:5281.58 01:21:08 85.29
30 Martinsen Niels 00:06:3082.99 00:40:5786.45 00:33:0381.28 01:21:16 85.18
31 Bogaert Mike 00:07:2976.94 00:41:3885.22 00:31:4183.53 01:21:29 85.01
32 Van Haverbeke Emiel 00:06:2084.01 00:39:2589.22 00:35:1577.65 01:21:43 84.83
33 Gouwkens Joeri 00:06:3082.99 00:39:5988.19 00:34:2778.97 01:21:45 84.80
34 Vandevoorde Ruben 00:06:3582.48 00:40:5486.54 00:33:3680.37 01:21:47 84.77
35 Van Hoornick Tim 00:07:0679.30 00:38:5390.18 00:35:0777.87 01:22:02 84.58
36 Hernaert Emilio 00:06:5280.73 00:39:5688.28 00:35:0078.06 01:22:27 84.25
37 Vanoirbeek Bart 00:06:5280.73 00:40:3587.11 00:34:1379.35 01:22:29 84.22
38 Bonamie Davey 00:07:2477.46 00:40:0887.92 00:34:2678.99 01:22:38 84.11
39 De Winter Jeroen 00:07:0379.61 00:39:0289.91 00:35:5676.52 01:22:50 83.95
40 Verschaeve Milan 00:07:1378.58 00:43:1482.33 00:31:4183.53 01:22:52 83.92
41 Van Vooren Niels 00:06:2883.19 00:41:0486.24 00:35:5876.47 01:24:13 82.86
42 vanbelle simon 00:07:5574.28 00:42:2083.95 00:33:1281.03 01:24:22 82.74
43 Latruwe Dimitri 00:07:3376.53 00:41:1885.82 00:34:3578.75 01:24:23 82.73
44 STUBBE Kristof 00:07:2477.46 00:41:3785.25 00:34:3478.78 01:24:25 82.71
45 Van Haecht Pepijn 00:07:2477.46 00:41:3685.28 00:34:4078.61 01:24:30 82.64
46 Labeeuw Tijl 00:06:3282.78 00:40:5186.63 00:36:2475.75 01:24:37 82.55
47 Vansieleghem Jasper 00:08:3969.77 00:41:0786.15 00:34:0979.46 01:24:55 82.31
48 Tanghe Tom 00:08:1072.74 00:41:5784.64 00:34:2379.08 01:25:29 81.87
49 Parein Filiep 00:10:0061.48 00:42:1884.01 00:32:3382.10 01:25:40 81.72
50 De Rous Robin 00:06:4181.86 00:39:4088.77 00:38:2772.37 01:25:44 81.67
51 Debaere Steven 00:07:3476.43 00:42:3683.47 00:34:3978.64 01:25:49 81.60
52 Debaeke Jelmer 00:08:0872.95 00:42:1284.19 00:34:4578.47 01:25:54 81.54
53 Hemelsoen Bram 00:07:3376.53 00:42:3483.53 00:34:5178.31 01:26:04 81.41
54 Naesen Davy 00:08:2671.10 00:43:0582.60 00:34:0879.49 01:26:33 81.03
55 Dewitte Bart 00:07:3676.23 00:43:1482.33 00:35:0278.01 01:26:51 80.79
56 De Wispelaere Allan 00:08:3869.88 00:42:5682.87 00:34:0879.49 01:26:57 80.71
57 Verschuere Jelle 00:09:1965.68 00:43:0582.60 00:33:4680.09 01:26:58 80.70
58 Vyvey Knut 00:07:3376.53 00:41:2485.64 00:37:1674.32 01:27:06 80.60
59 Homblé Peter 00:07:5674.18 00:42:4683.17 00:35:2577.37 01:27:07 80.58
60 Brissinck Johan 00:07:2577.35 00:41:4085.16 00:37:1774.30 01:27:10 80.54
61 Verbruggen Thijs 00:08:1971.82 00:43:0182.72 00:34:4578.47 01:27:15 80.48
62 Vanparrys Mark 00:07:4974.89 00:42:0984.28 00:36:5774.85 01:27:42 80.12
63 Vanderhaeghe Alexander 00:07:4375.51 00:41:2085.76 00:37:5473.28 01:27:47 80.06
64 Desender Dries 00:08:2870.90 00:41:3785.25 00:36:4675.15 01:27:49 80.03
65 Claeys ALexander 00:08:0273.56 00:42:1983.98 00:36:4375.23 01:27:51 80.01
66 Meiresonne Tim 00:07:2577.35 00:44:3579.89 00:34:5778.14 01:28:13 79.72
67 Cattellion Jema 00:08:4669.06 00:43:2182.12 00:35:0677.90 01:28:16 79.68
68 Vanhoutte Jonie 00:07:2678.19 00:44:2581.80 00:35:4583.89 01:28:30 81.67
69 Crabeels Pascal 00:06:3882.17 00:40:5186.63 00:40:3368.91 01:28:51 79.22
71 Vercarre Marc 00:08:0573.26 00:42:0184.52 00:37:5173.36 01:28:59 79.12
72 Timmerman Frauke 00:07:3375.89 00:44:2280.73 00:36:1881.69 01:29:01 80.04
73 Claeys Yves 00:09:1166.49 00:42:2683.77 00:36:2975.61 01:29:13 78.93
74 Ameloot Peter 00:07:5174.69 00:42:1584.10 00:38:1372.76 01:29:15 78.91
75 Ceyssens Wouter 00:08:1572.23 00:43:1982.18 00:36:5175.01 01:29:17 78.88
76 Vanspeybroeck Bart 00:07:5174.69 00:42:1884.01 00:38:1472.73 01:29:21 78.83
77 Debackere Brecht 00:11:1953.38 00:40:4786.75 00:36:0876.19 01:29:21 78.83
78 Spruytte Stefaan 00:08:3969.77 00:42:4983.08 00:36:5474.93 01:29:26 78.76
79 Van Mullem Nicolas 00:07:3576.33 00:46:2376.64 00:34:4578.47 01:29:35 78.64
80 Toebat Andrew 00:08:0373.46 00:41:5484.73 00:38:3972.04 01:29:45 78.51
81 Linskens Gareth 00:08:2471.31 00:43:5781.03 00:36:4575.17 01:30:01 78.30
82 Vermont Lies 00:07:0779.98 00:44:4279.88 00:38:0478.49 01:30:51 78.53
83 Vermont Filip 00:10:4456.97 00:43:1482.33 00:36:0476.30 01:30:51 77.65
84 Laflere Lieven 00:08:2271.51 00:43:1882.21 00:38:2872.34 01:30:56 77.58
85 Vanhee Geoffrey 00:07:3876.02 00:42:2483.83 00:40:0769.62 01:31:11 77.39
86 Jansen Ruben 00:09:1566.08 00:44:0180.91 00:36:3675.42 01:31:15 77.33
87 Janssens Enzo 00:07:4875.00 00:44:4179.71 00:37:5873.17 01:31:18 77.29
88 Pype Bene 00:09:1566.08 00:42:4683.17 00:38:2472.45 01:31:36 77.06
89 Bultot Claude 00:09:5661.88 00:44:0880.70 00:36:0976.16 01:31:38 77.03
90 Verbeke Bert 00:09:0766.90 00:47:1575.08 00:34:2279.10 01:31:46 76.93
91 Fraeyman Bart 00:10:3757.69 00:42:5382.96 00:37:0674.60 01:31:55 76.81
92 Breeur Ben 00:08:1372.44 00:44:0280.88 00:38:4771.82 01:32:01 76.73
93 Nenin Geoffrey 00:09:1366.29 00:42:3983.38 00:38:5171.71 01:32:09 76.63
94 Vanbrabant Bjorn 00:07:1378.58 00:42:5183.02 00:41:0368.08 01:32:11 76.60
95 Bossier Michiel 00:09:2964.65 00:42:4883.11 00:39:0371.38 01:32:17 76.52
96 Denolf Wim 00:11:2053.28 00:40:4686.78 00:39:0371.38 01:32:18 76.51
97 Tackx Koen 00:08:1772.03 00:43:5181.22 00:39:0171.44 01:32:19 76.50
98 Hocedez Steven 00:10:3258.20 00:45:0479.02 00:35:4276.91 01:32:22 76.46
99 Geerardyn Nicolas 00:08:3470.28 00:41:2785.55 00:41:2567.48 01:32:29 76.36
100 Hamers Peter 00:10:1659.84 00:45:0379.05 00:36:1376.05 01:32:37 76.26
101 Houtteman Jelle 00:08:1672.13 00:44:1080.64 00:39:4070.37 01:32:57 76.00
102 Mares Thomas 00:08:4968.75 00:44:5679.26 00:38:3072.29 01:33:23 75.66
103 Reinquin Filip 00:07:5674.18 00:42:0784.34 00:42:2365.89 01:33:26 75.62
104 Feys Bert 00:09:2465.16 00:42:4383.26 00:40:2369.18 01:33:37 75.47
105 Van Tricht Frank 00:10:5156.25 00:43:4081.55 00:38:0572.98 01:33:38 75.46
106 Cleenwerck Dieter 00:08:3869.88 00:45:4077.94 00:38:1372.76 01:33:41 75.42
107 Vandeputte Joost 00:08:4469.26 00:43:2482.03 00:40:3168.96 01:33:42 75.41
108 Van Troyen Ines 00:07:3775.26 00:48:1270.97 00:37:0680.24 01:33:45 76.14
109 Vanoverberghe Dries 00:08:3570.18 00:43:4281.49 00:40:3368.91 01:33:49 75.32
110 Devos Jelle 00:09:1366.29 00:44:2280.28 00:39:0071.46 01:33:49 75.32
111 Weyn Shelsea 00:06:4184.08 00:45:4177.38 00:40:5773.26 01:34:16 75.72
112 Schockaert Gillian 00:06:2583.50 00:45:1578.69 00:41:5266.74 01:34:18 74.94
113 Verbeke Filip 00:08:1072.74 00:43:5081.25 00:41:0967.92 01:34:21 74.90
114 Bertels Ronny 00:08:4669.06 00:45:0479.02 00:39:3370.56 01:34:24 74.86
115 Blondel Michaël 00:09:3763.83 00:46:5775.62 00:37:3173.91 01:34:56 74.44
116 Michiels Johan 00:10:0061.48 00:46:5375.74 00:37:1074.49 01:35:04 74.33
117 Pollentier shana 00:08:0570.85 00:47:4372.20 00:38:2177.98 01:35:07 75.02
118 vermoortele jochen 00:09:4363.22 00:44:4279.68 00:39:4070.37 01:35:09 74.27
119 lebacq kris 00:10:3358.09 00:46:2476.61 00:37:1974.24 01:35:13 74.22
120 Moerenhout Bart 00:09:0966.70 00:47:0675.35 00:37:5573.25 01:35:17 74.16
121 Poppe Alain 00:10:1959.53 00:45:5077.64 00:38:1772.65 01:35:38 73.89
122 Beauprez Ronan 00:09:4762.81 00:44:2380.25 00:40:1369.46 01:35:44 73.81
123 Decubber Kristof 00:10:5555.84 00:45:0079.14 00:38:4571.88 01:36:04 73.55
124 De Maet Jonas 00:07:1378.58 00:47:5773.82 00:39:2870.70 01:36:07 73.51
125 Roels Gregory 00:07:2677.25 00:47:0275.47 00:41:1567.75 01:36:49 72.96
126 Verlinden Jessica 00:07:0680.14 00:44:5579.33 00:44:0667.55 01:36:52 73.57
127 Sigmans Peter 00:08:5568.13 00:43:1182.42 00:44:2262.62 01:37:34 72.37
128 Vanderhaeghe Frederick 00:08:1971.82 00:43:2981.88 00:44:4961.87 01:38:09 71.91
129 Barber Kris 00:08:4369.36 00:47:3374.54 00:40:5468.33 01:38:18 71.79
130 Soenen Björn 00:09:3364.24 00:46:4575.98 00:40:5868.22 01:38:18 71.79
131 Dobbelaere Seppe 00:10:4556.87 00:48:3872.58 00:38:0772.92 01:38:20 71.77
132 De Vos Pieter 00:12:0548.67 00:46:1077.03 00:38:5871.52 01:38:21 71.75
133 De waele Karlien 00:07:1279.20 00:48:3470.03 00:41:4871.72 01:38:28 72.25
134 Deferme Bart 00:09:3963.63 00:48:0673.54 00:39:2170.89 01:38:37 71.54
135 Carlier Anthony 00:11:0554.82 00:47:0175.50 00:39:0071.46 01:38:41 71.49
136 Carton Filip 00:09:0567.11 00:47:0775.32 00:41:3367.26 01:38:57 71.28
137 Van Vooren Jan 00:08:3470.28 00:46:1876.79 00:42:4865.20 01:39:06 71.16
138 Lagae Wim 00:08:4169.57 00:42:5083.05 00:46:2159.34 01:39:08 71.14
139 Vincent Blommaert 00:08:1472.33 00:45:3078.24 00:44:3062.40 01:39:27 70.89
140 Hollevoet Saïda 00:09:1060.61 00:50:5963.88 00:38:0678.43 01:39:35 71.33
141 Ulin Kenny 00:08:2970.80 00:49:5970.15 00:39:3170.61 01:40:11 70.31
143 De Craemer Marieke 00:07:2876.68 00:48:2370.50 00:43:4468.21 01:40:35 70.51
144 Pauwels Michael 00:10:0760.76 00:49:0271.86 00:40:3068.99 01:40:42 69.91
145 Wittevrongel Steve 00:09:2864.75 00:48:3472.70 00:41:3567.20 01:40:52 69.78
146 lievens mathias 00:09:1066.60 00:44:1680.46 00:46:2759.18 01:41:03 69.63
147 Tack Charlotte 00:08:4265.02 00:49:0168.88 00:42:3970.18 01:41:24 69.84
148 Vandenborre Jolien 00:09:1659.66 00:48:2470.46 00:42:4570.00 01:41:28 69.78
149 Pinto Timothy 00:09:5961.58 00:46:1876.79 00:44:1262.89 01:41:32 69.25
150 Van Acker Henk 00:10:0461.07 00:48:5372.13 00:41:2567.48 01:41:41 69.13
151 Van Valckenborgh Jef 00:09:0866.80 00:49:5270.36 00:41:4566.93 01:42:00 68.88
152 Himpe Nicolas 00:11:1054.30 00:47:0175.50 00:42:5565.01 01:42:21 68.61
153 Piepers Stijn 00:09:0067.62 00:44:5879.20 00:47:3157.42 01:42:28 68.52
154 Deley Danielle 00:08:0970.22 00:50:2065.53 00:43:2368.85 01:43:05 68.45
155 Dildick Andre 00:09:2964.65 00:48:3772.61 00:44:0463.11 01:43:18 67.86
157 Vandevelde Liesbeth 00:08:5363.29 00:48:4469.61 00:44:5466.10 01:43:39 67.98
158 Geschier Philip 00:10:4956.46 00:50:2469.39 00:41:0767.97 01:43:55 67.38
159 Van Crombrugghe Steven 00:08:5668.03 00:52:1466.08 00:41:1667.73 01:44:02 67.29
160 Boelens Gilbert 00:10:0560.96 00:48:1873.18 00:44:3362.31 01:44:41 66.78
161 Mestdagh Windy 00:08:2268.17 00:49:1468.33 00:46:0563.95 01:44:48 67.03
162 Nelissen Jo 00:09:3164.45 00:46:4476.01 00:47:1957.75 01:45:12 66.37
163 Vandeleur Mario 00:09:3763.83 00:49:2571.17 00:44:4861.90 01:45:27 66.17
164 Bauters Jens 00:11:0954.41 00:50:3369.12 00:42:4065.42 01:45:29 66.15
165 Smeets Tom 00:09:0067.62 00:50:5368.52 00:44:1462.84 01:45:40 66.00
166 Beys Jan 00:09:3164.45 00:48:3772.61 00:46:4258.77 01:45:54 65.82
167 Mommaerts Jan 00:08:3270.49 00:50:0070.12 00:46:1959.40 01:46:04 65.69
168 Godderis Luc 00:11:5649.59 00:51:5866.57 00:41:2367.53 01:46:19 65.49
169 Deruytter Jari 00:08:2870.90 00:49:5270.36 00:46:3858.88 01:46:22 65.45
170 De Visschere Pieter 00:09:3164.45 00:50:3868.97 00:45:0161.54 01:46:24 65.43
171 Dorlandt Koen 00:10:2259.22 00:49:4870.48 00:45:4860.25 01:47:13 64.78
172 De Meyer Gustaaf 00:11:0155.23 00:47:1075.23 00:47:5756.71 01:47:23 64.65
173 Van Wijk Nico 00:09:5062.50 00:49:1071.62 00:47:0958.03 01:47:27 64.60
174 Ribas Philippe 00:09:1266.39 00:48:3272.76 00:48:1656.18 01:47:28 64.59
175 Ossieur Patrick 00:08:3370.39 00:50:5268.55 00:46:0359.84 01:47:30 64.56
176 Fossaert Kevin 00:10:0361.17 00:50:3269.15 00:45:2660.86 01:47:30 64.56
177 Vankeirsbilck Fien 00:08:4564.55 00:52:1960.48 00:45:4164.68 01:47:49 64.55
178 Jonckheere Patrick 00:12:3745.39 00:50:2069.51 00:43:4163.74 01:48:12 64.01
179 Ferret Sammy 00:11:4850.41 00:49:4270.66 00:45:2560.88 01:48:14 63.98
180 Flameyn Cindy 00:08:4065.33 00:51:5061.71 00:47:1661.81 01:48:44 63.79
181 Gryp Jeroen 00:11:0454.92 00:50:2469.39 00:45:5560.06 01:48:45 63.58
182 Vanmassenhove Katty 00:09:1160.45 00:53:4556.83 00:44:4366.43 01:48:52 63.68
183 Gyselinck Martin 00:12:1847.34 00:50:2969.24 00:44:3062.40 01:48:59 63.40
184 Desmedt Dries 00:09:2365.27 00:53:3063.80 00:45:2360.94 01:49:35 62.92
185 Peerlinck Frank 00:10:5855.53 00:50:2669.33 00:46:5158.52 01:49:45 62.79
186 Schillewaert Cédric 00:08:2471.31 00:53:5463.08 00:45:5859.98 01:50:05 62.53
187 Ostijn Björn 00:10:4157.28 00:47:3974.36 00:50:5151.92 01:50:38 62.10
188 Depoorter Arne 00:12:1247.95 00:49:1071.62 00:47:3257.39 01:50:50 61.94
189 De Loose Francky 00:10:0860.66 00:49:0571.77 00:49:4153.85 01:50:58 61.84
190 Vangilbergen Hilde 00:09:1659.66 00:51:3662.30 00:48:5158.93 01:51:01 61.91
191 Meeus Jeff 00:06:4981.04 00:49:4470.60 00:54:1246.40 01:51:34 61.36
192 Mattheeuws Christoph 00:10:0161.37 00:54:1462.48 00:45:5060.20 01:51:40 61.29
193 Beerens Filip 00:09:0567.11 00:52:2765.69 00:49:0654.81 01:51:54 61.10
194 Dequeecker Alexander 00:10:0760.76 00:53:0764.49 00:47:3257.39 01:51:56 61.08
195 stevens bart 00:11:2253.08 00:52:2065.90 00:47:0358.19 01:52:17 60.80
196 Geerardyn Gino 00:13:2040.99 00:50:0370.03 00:47:5556.76 01:52:24 60.71
197 Devriendt Griet 00:09:0960.77 00:53:4956.66 00:48:3059.57 01:52:51 60.40
198 Devlies Veerle 00:09:4455.25 00:53:1158.27 00:49:4357.36 01:53:59 59.46
199 Bossuyt Daphne 00:10:1959.53 00:52:4865.06 00:49:4453.77 01:54:04 59.40
200 Van Crombrugghe Patrick 00:12:2846.31 00:50:1869.57 00:50:0853.11 01:54:35 58.99
201 Craeynest Maaike 00:11:0143.12 00:55:5651.27 00:46:3762.98 01:54:53 58.72
202 de schrijver jimmy 00:11:4850.41 00:53:2863.86 00:48:1256.29 01:55:01 58.65
203 Crijns Bart 00:11:4151.13 00:55:3759.98 00:47:1957.75 01:55:31 58.26
204 Versluys Tanja 00:10:4945.01 00:52:0960.90 00:52:0153.19 01:56:02 57.77
205 Lienard Anthony 00:09:2065.57 00:45:4277.88 01:00:1936.31 01:56:42 57.33
206 Breye Annemie 00:11:0941.86 00:51:5161.67 00:53:2450.68 01:57:39 56.44
207 Mouton Like 00:12:0433.20 00:56:0251.01 00:48:4559.12 01:58:01 56.14
208 Mat Rene 00:12:1447.75 00:51:4067.11 00:53:2247.77 01:58:54 55.60
209 kurz sofie 00:11:3238.24 00:55:1852.88 00:50:5955.07 01:59:17 55.09
210 Billiet Carine 00:11:3837.30 00:58:5343.75 00:46:5062.59 01:59:18 55.08
211 Mauws Ingrid 00:09:4255.57 00:52:5558.95 00:57:4442.83 02:02:06 52.77
212 Croquet Vincent 00:09:1366.29 00:53:2164.07 00:58:1539.72 02:02:33 52.73
213 De Bruyn Bruno 00:09:5362.19 00:53:5063.20 00:58:4338.95 02:03:49 51.74
214 Coulier Nel 00:10:3247.69 00:52:0361.16 01:00:2637.93 02:04:44 50.60
215 Coopman Jitse 00:10:5344.38 00:55:5651.27 00:59:4539.17 02:08:03 47.86
216 Capitaine Tamara 00:11:4935.56 00:59:3242.10 00:55:1647.30 02:08:03 47.86
217 Daper Claudia 00:10:4645.49 00:55:5651.27 01:00:1438.29 02:08:33 47.45
218 Picard Mireille 00:09:5761.78 00:59:1953.30 00:59:0538.35 02:10:07 46.78
219 Vandemoortele Natalie 00:12:1230.94 01:01:1636.68 00:59:5437.90 02:14:56 41.19
220 Sauwens Filip 00:14:4131.69 01:01:2848.42 01:00:4134.71 02:16:45 40.57
Lemmens Tuur
Verbelen Remco
Wera Joachim
Marclé Xander
Hernaert Antonio
Van Hoornick Tim
Heemeryck Sander
Vanden Broucke Giani
Vandenbroucke Sven
Ready, set, GO! Triatlonseizoen is begonnen :)
Debaeke Jelmer
Zaterdag om 9u50 het zwembad in om 500m te knallen (of toch zoiets te proberen). Na 8min08 kon ik aantikken. Geen supertijd maar toch dik tevreden. Nu wachten tot 15u...
Lees alle blogposts over deze wedstrijd
Uitslag van de Veloopzwem De Haan staat online
Andere uitslagen van de wedstrijd
Veloopzwem De Haan
0.50 - 27.30 - 8.60
0.50 - 28 - 8.60

redpajama_set_name: RedPajamaCommonCrawl


text:
slickr
======

A collection of python and bash scripts to collect and analyze frame rendering performance in Android apps.

## requirements

* [python](https://www.python.org/)
* [matplotlib](http://matplotlib.org/) - only needed for `plot.py`

## setup

### on device

**Make sure to enable the "In adb shell dumpsys gfxinfo" option for "Profile GPU rendering" inside _"Developer options"_ in your settings app!**

_You may need to kill and restart your app for the logging to work!_

### on computer

If you can't execute the scripts, you may need to mark them as executable.

```bash
$ chmod +x *.sh *.py
```

should do the trick on Unix-like operating systems, or cygwin.

## examples

Scroll for 8 seconds and save the GPU profiling information for the current screen into a file.

```bash
$ ./slickr.sh > profile.txt
```

Scroll for 8 seconds and display the average frame delay (in milliseconds).

```bash
$ ./slickr.sh | ./avg.py
```

Scroll for 8 seconds and plot the recorded data and other metrics.

```bash
$ ./slickr.sh | ./plot.py
```

Compare the frame delay histograms and demand curves of two (or more) saved profiles.

```bash
$ ./compare.py profile1.txt profile2.txt
```

## api

```bash
$ slickr.sh <package> <iterations> <distance>
```

* `package` is the Java package name for the Android application. For example, for the [Tumblr app](https://play.google.com/store/apps/details?id=com.tumblr), it is `com.tumblr`. It can be gleaned from the play store url for an application.

    If an app has multiple activities open, `profile.py` will choose the activity with `visibility=0` (the currently visibile activity). On devices below [Lollipop](https://developer.android.com/about/versions/lollipop.html), all profile data is exported.

* `iterations` is the number of 2 second iterations to run (since 128 frames, the default buffer size, is a duration of about 2 seconds at 60 frames per second). Default is `4`.

* `distance` is the scroll distance in pixels. It defaults to 3x the display density (at the bucket the device belongs to).

[`framestats` in Android Marshmallow (6.0)](http://developer.android.com/preview/testing/performance.html#timing-info) is automatically enabled as long as a package name is provided. It provides detailed information about the draw stage of the rendering pipeline.

## understanding the plots

![tumblr app profile](/../example/com.tumblr.png?raw=true)

The Android M `framestats` data [is a series of raw timestamps](http://developer.android.com/preview/testing/performance.html#fs-data-format). These are then converted into time deltas according to the Android Developer guidelines. The [`gfxinfo` data](https://io2015codelabs.appspot.com/codelabs/android-performance-profile-gpu-rendering#5) is also plotted if available, though there is some overlap.

| component  | `gfxinfo` | `framestats` timestamps                              | notes                              |
| ---------- | --------- | ---------------------------------------------------- | ---------------------------------- |
| start      | ↓    | `INTENDED_VSYNC` → `HANDLE_INPUT_START`         | time spent by system               |
| input      | ↓    | `HANDLE_INPUT_START` → `ANIMATION_START`        | time spent handling input events   |
| animations | ↓    | `ANIMATION_START` → `PERFORM_TRAVERSALS_START` | time spent evaluating animators    |
| traversals | ↓    | `PERFORM_TRAVERSALS_START` → `DRAW_START`       | time spent on layout and measure   |
| draw       | draw      | `DRAW_START` → `SYNC_START`                     | time spent on `View.draw()`        |
| sync       | prepare   | `SYNC_START` → `ISSUE_DRAW_COMMANDS_START`      | time spent transfering data to gpu |
| ↓     | execute   |                                                      | time spent executing display lists |
| gpu        | process   | `ISSUE_DRAW_COMMANDS_START` → `FRAME_COMPLETED` | time spent waiting on gpu          |

The green line represents the 16.67 ms threshold needed to achieve a [smooth 60 frames per second](https://www.youtube.com/watch?v=CaMTIgxCSqU).

### duration curve

The duration curve rearranges the profiling data by sorting it from slowest to fastest frame. This is based off [load duration curves](https://en.wikipedia.org/wiki/Load_duration_curve) in power engineering and illustrates how many frames went over the 16 ms threshold needed for 60 FPS and how many milliseconds they went over.

redpajama_set_name: RedPajamaGithub


text:
ROLLING THROUGH THE VALLEY
NOVA Jeepers is a car club that scales off-road trails
Story by Paul Murphy
Photos by James Allen and Sean O'Brien
Most people would be enraged if it took them seven hours to cover 8 miles in their car. However, one group of people enjoy doing exactly that as a weekend activity. The Nova Jeepers are a club of off-road enthusiasts who spend many weekends a year battling rocks, mud and steep gradients in an effort to optimize their smiles-per-gallon. Their Jeeps sit high off the ground and resemble four-wheel drive gladiators, kitted out to do battle against all that Virginia's trails, including the Flagpole Knob trail in Rockingham county, can throw at them. "I don't have any kids, so she's almost my baby," said Nova Jeepers' vice president Jeremy Long in regard to his Jeep.
Long and 16 other Jeepers hit the Potts Mountain Jeep Trail trail just outside of Covington, Virginia, for a full day of off-roading on what many of them called the most difficult public trail in Virginia. The 8-mile trail took about seven hours to negotiate. In those seven hours, the Jeepers had to crawl over sofa-sized rocks, drive trails pitched so heavily to the side that it felt as though the Jeep was going to tip over, and climb slopes so steep that the only thing visible in the windshield was the cloudless, blue sky above. "You've got obstacles that you can't go around," said Long. "I love the problem-solving aspect of it."
Even in purpose-built Jeeps, maneuvering through the obstacles on the trail requires precision, specifically in the line the driver uses. "The line is just the path you want your tires to go on," said Alec Schreiber. When drivers navigating obstacles, other Jeepers will stand in front and spot for the driver because it's impossible for drivers to see what's under their front wheels. "What makes you good at spotting is knowing where to put your wheels and stay off the gas," said Richard "Turkey Man" Graham, one of the ride's leaders. "I've put a lot of Jeeps in places they thought they'd never go." Along with spotting and driving technique, the Jeeps themselves play an important role in overcoming the obstacles. Tires from 32 to 40 inches, upgraded suspension, skid plates and winches, which are cables that pull the jeep when the tires can't get traction, are required on a difficult trail like Potts Mountain. One of the Jeeper's Jeeps had about $70,000 in aftermarket parts installed.
However, less difficult trails like Flagpole, just a few miles from Reddish Knob, can be done with fewer upgrades. "Even a stock Jeep is quite capable," said Long. The Nova Jeepers use Flagpole as a way to introduce people to off-roading. "We use it for our new members," said Long. "We kind of show them some things and at least give them a taste of going off-road." "I think it's really cool to see new people experience the things that I've experienced," said Graham. "Just the expressions on their face and the fun that they have, that's what Jeepin' means to me."
Previous Previous post: STILL SERVING
Next Next post: A CHANCE FOR CHANGE


My Mum recommended I read The Woman Who Breathed Two Worlds by Selina Siak Chin Yoke, as she knows how much I enjoy reading historical fiction or non-fiction about women in the twentieth century through the interwar and world war two period (see my blogs on Reading Vietnam, Trilogies, Quartets and Quintets). I was also about to go to Malaysia on holiday for the second time, so this was the perfect book to enjoy the build-up. It is brilliant and I was hooked from page one.
It follows the life of Chye Hoon, born into the Nyonya community of Chinese in Malaysia in 1878 in the small village of Songkhla in a family who choose to try their luck by moving to the island of Penang when Chye Hoon is small. It is here in Georgetown (which I was lucky enough to visit on holiday a few years ago) that she grows up, frustrated at being denied going to school despite her clear appetite for learning and for business. Her fiery temper and bargaining skills in the local market soon get her noticed, but don't prevent her from marrying Wong Pen Choon who is happy to let her run their new household, in the Nyonya tradition. This arranged marriage turns out extremely well and her married life in Ipoh back on the mainland of Malaysia is a happy one, as her husband's business grows and she makes new friends and brings up ten children. When her husband prematurely dies she is left with the challenge of financially providing for her family and turns to her childhood skill of cooking, successfully setting up a business selling sweet and savoury Kueh – a Nyonya speciality.
As the novel moves through the early part of the twentieth century and the first world war and beyond, the changes in the town of Ipoh and the way of life of Malaysians, as well as the growing influence of the British, are laid out as the life of Chye unfolds. Ipoh sees its first motor car, bicycle and school for girls, and eventually Chye sees her son going to study in London. This book is a fascinating social history of Malaysia, seen through the eyes of what becomes one of Ipoh's main families. It tantalisingly takes us up to 1938 and the outbreak of world war two, as Japanese drop bombs on Ipoh, and I am already looking forward to reading the sequel to see what happens to Chye's children in wartime.
I absolutely loved being immersed in the world Selina Siak Chin York so beautifully creates and I can't recommend this book enough.


658 beneficiaries of Tulong Panghanapbuhay sa Ating Disadvantaged/ Displaced Workers (TUPAD) Program received their respective salaries on March 12, 2018 during the Cash Pay-out held at the Villasis Public Auditorium. Mayor Nato together with Mr. Arnel Arimas, PESO Manager and Ms. Mary Jane Hufano, DOLE-ROI Representative, distributed the salary to the benefiaciaries.
Each beneficiary received P2,800.00 for working for ten days at their respective barangays.
TUPAD is a program of DOLE in coordination with the Abono Partylist through Cong. Conrado M. Estrella, III and local government unit which aims to provide emergency employment for displaced workers and unemployed residents of Villasis.
Meanwhile, Villasinians should expect for more upcoming projects and programs of LGU in DOLE such as Special Program for Employment of Students (SPES) and Livelihood Assistance.


02:30 - How did you come on to this project?
13:00 - Who is this book intended for?
15:30 - What was the most difficult part of this project?
19:30 - How did you select the music for the Rarities CD?
25:30 - How are you feeling as this book is finally about to release?
29:04 - What's happening with Howard Shore and THE HOBBIT?


text:
Binoculars and Scopes
Discover Wildlife Weekends
Guided Wildlife and Birding Walks
Custom Wildlife and Birding Tours
Irish Wildlife News
International Wildlife News
Wildlife Events
Wildlife Press Releases
Whales and Dolphins
Wildlife Podcasts
The Calendar Road
Wildlife Calendar
Birding for Beginners
How to watch whales and dolphins
How to watch Basking Sharks
Wildlife Portfolio
Wild Wide Web
Wildlife Optics
Binocular Reviews
Spotting Scope Reviews
Wildlife Clothing
Wildlife Accessories
Wildlife Marketing Services
Ireland's Wildlife
Irish wildlife, nature and biodiversity
You are here: Home / Wildlife Reviews / Wildlife Gear / Wildlife Optics / Binocular Reviews / Nikon EDG 8×42 Binocular Review
Nikon EDG 8×42 Binocular Review
April 30, 2013 by Calvin Jones 3 Comments
Pros: Stunning optics, high quality materials (including eco-friendly lead- and arsenic-free glass) and contemporary design combine to put this Japanese binocular up there with the best of the European competition. Bright, clear, razor sharp image practically to the edge of the field of view, coupled with excellent balance and handling makes the EDG a superb binocular in the field. A real pleasure to use.
Cons: It's hard to find any functional flaws in a binocular of this calibre… but there are a few niggles. While many reviewers cite Nikon's super smooth focus mechanism as a plus point (and there's no question that it IS silky smooth), to be honest I found it a bit "spongy". The close focus isn't as close as it might be either, at around 2.5 metres. It's adequate, some competitors easily focus to under 2m. Although the EDGs perform very well in low light, they are perhaps a shade darker at twilight than I was expecting, given their optical pedigree and high-end prisms and coatings.
Price: c. €1,900 (GB£1,600)
Value: Good
Rating: Highly Recommended
With the EDG Nikon has created a pair of premium binoculars that are up there with the very best in the dizzying heights of the optics stratosphere. The price, of course, reflects that, but if you're looking to invest in the very best, then the EDG from Nikon should certainly be on your premium binocular short list.
View the Nikon EDG on the Nikon UK & Ireland website.
Nikon EDG 8×42 Full Review
When I knew Nikon was sending the EDG in for review I was genuinely excited. I'd heard great things about this flagship model from the Japanese optics heavyweight, and couldn't wait to put them through their paces.
The binoculars arrived in a classy black box with the EDG branding emblazoned on it in gold lettering. Nestled in the matt black cardboard of the box interior was a swanky-looking case containing the binocular itself, and the usual assortment of accessories including a rain guard, padded neck strap, cleaning cloth tethered objective covers… and an added extra you don't normally see: some flared rubber eye-cup attachments to block out stray light.
It's always a nice touch when you find something unexpected in the box.
When you pick up the EDGs they feel like a premium binocular. They are solid, and a comfortable weight: not so light that you'd question the quality of the materials or build, but not too heavy to carry and hold comfortably for long periods either. They are covered in a tactile black rubber armour that is tough, but yielding and textured enough to offer a secure and comfortable grip. It also feels substantial enough to protect the binoculars from knocks.
Ergonomics and build quality
The Nikon's are a great fit in the hand thanks to the single hinge design and exposed barrels.
The Nikon EDG handles beautifully. At 785g they're around average weight for binoculars in their category… but they are superbly balanced, so that you hardly notice the weight at all when you're using them. You need a bit of weight in a binocular anyway: binoculars that are too light are, curiously, more difficult to hold steady than well balanced binoculars with optimal "ballast". Light weight can also equate to cheap, sub-standard components in the optical system — so be wary of "lightweight" binoculars.
The rubber armouring works well — it is tactile and yields just enough under your grip to be comfortable and secure. It also provides protection from knocks — although to be honest the EDGs feel solid enough to take a few knocks and come out unscathed — and help protect from unwanted noise (few things will send wary wildlife diving for cover more quickly than the chink of a wedding ring off bare metal).
In common with several contemporary designs (the Swarovski SLC HD and the Vortex Razor HD, for example), the Nikon EDG employs a single hinge high on the barrels, giving the binoculars a "H" profile. To my mind this is the optimal binocular design — it facilitates a superb wrap around grip on the barrels with no lower hinge to get in the way. It's simple, elegant and effective… and it looks good. Hats off to Nikon… the EDGs certainly looks the part.
The twist up rubber-coated eyecups provide a maximum quoted eye relief of 19.3 mm — making them a long-eye-relief binocular, which means they should work very well for people who wear eye glasses. The Nikons also offer more capacity for eye relief adjustement than you generally see, with three "click stops" between the fully up and fully down position, so setting the optimum eye relief for you should be straightforward. Typically if you're using the binoculars without glasses you'd use the eyecups in the fully-up position. I did have an issue a couple of times with the eye cups moving when I was traversing difficult terrain — but generally it wasn't a problem.
The body itself is made from magnesium alloy, which is light, but very strong. Naturally the Nikons are sealed and purged with nitrogen, so the optical system is completely waterproof, dust proof and immune to internal fogging.
Optical Performance
The Nikon EDG is, quite simply, optically superb.
It renders a pin sharp image with excellent colour fidelity, contrast and sublime detail from the centre of the wide 7.7° field of view right out to the edge — with very minimal softening only apparent right at the edge. It offers a "walk in and look around view" that is consistently impressive across every type of viewing condition I managed to test it in… from early morning directional sunlight, to squally April showers, to hazy overcast days. The EDG took it all in its stride and continued to deliver stunning views.
The coatings and glass used in the Nikon EDG are, as you would expect, the best available on the market today. Compared to most, if not all premium sports optics companies, Nikon is a monster. It's a huge company, and has the benefit of it's long optical heritage to draw on, not just in sports optics, but in photography, medical devices and other high-grade optical fields. It's scale means it has all of the resources it needs to manage every aspect of optics production in house, from R&D through design, right through to production of the finished product at its own state-of-the-art manufacturing facilities. The quality and attention to detail evident in the EDG reflects that.
ED (Extra-low Dispersion) glass in the objective lenses compensate for chromatic aberrations, and provide images with better contrast and resolution, while a field flattener system works to minimise field curvature giving sharp, clear images all the way to the edge of the field. The use of advanced dielectric multi-layer coatings on the prisms provide consistently high light transmission across the visible spectrum, resulting in bright, vibrant images with remarkably natural colour. The prisms are also phase corrected to prevent phase shift and improve resolution.
It all adds up to an impressive package… not just on paper, but out in the field too.
There was no sign of chromatic aberration (colour fringing) during normal use. A fly-by raven sillhouetted against a backlit cloud was perhaps the ultimate test — the black bird was clearly defined with no sign of colour fringing: the EDGs even managed to reveal some feather detail at distance in this extremely high contrast situation. Impressive stuff.
The detail rendered is "count the feathers" sharp. I handed the EDGs to a few people who weren't used to using high-end binoculars and the results were consistent: a sharp intake of breath followed by a "Wow!". Suffice it to say that to my eyes at least, the Nikon EDG is at least on a par in terms of resolution and detail with the best of the best.
The one area optically where I felt that the EDGs should deliver more… given their spec and their price point… was low light performance. They perform superbly in mediocre light, but in fading twilight, when things get really murky, the image through the EDGs seemed darker to my eyes than the view through the similarly specced Vortex Razor HD and Swarovski SLC HD I had around to compare them with.
The strange thing about that is that both of the other binoculars sported a 10×42 configuration, with a correspondingly smaller exit pupil, so on paper you'd expect the 8×42 EDG to blow them away in terms of low light performance. They didn't!
Size comparison (from left to right): Vortex Razor HD, Nikon EDG, Swarovski SLC HD and the Vanguard Endeavour ED.
The focus wheel on the EDG is large, wide and in the ideal place for your focusing finger of choice. It's also consistently smooth as it turns through its 1 1/4 turns from close focus to infinity. Nikon has earned a reputation for its buttery focusing mechanism, but to be honest I wasn't so taken with it. To me it felt a little spongy and imprecise. I never had an issue achieving pin-sharp focus with the Nikons… but there was a slight feeling of disconnect between rotating the focus wheel and the focusing of the image. It's hard to explain properly — but if you try a pair you'll know what I mean (or perhaps it won't be an issue for you).
You get used to it, of course… but it was a little disconcerting.
The quoted close focus of the EDG is a relatively pedestrian 3m. In practice I managed to focus the binocular a little closer than that… but it was still a fair way short of the best of the competition. For most wildlife viewing and birding situations it's not going to be an issue, but it could leave you struggling if you're watching insects (dragonflies and butterflies, for example) or want a close up view of a delicate wildflower just the other side of the fence. Many of the EDG's contemporaries comfortably focus to within 2m, and I was expecting better from the Nikon's here.
The EDGs come in a fancy case that has obviously been custom designed exclusively for the EDG range. It looks good, and is functional as far as cases go — but I suspect most people who buy the EDG won't really use the case much. Binoculars of this calibre are built to be used… and cases tend to get in the way. So, if you're anything like me the case will probably live in the back of a cupboard or drawer somewhere until you need to put your venerable binoculars into storage — at which point you're unlikely to be worried about the case.
Much more important are the accessories you'll actually use. The padded neck strap is perhaps the most important of these… it is wide, with sufficient padding to comfortably carry the binoculars for long periods. There are handy quick-adjust buckles that let you easily shorten or lengthen the strap to suit, and the strap in general is unobtrusive and functional. The EDG branded rain guard is pretty standard fare, and attaches to one side of the strap to protect the eyepieces from rain and dust when you're not viewing. The tethered objective lens covers also work as expected, attaching to the barrels. They are removable, so you can put them away with the case if you find they get in the way (they are good for protecting the objective lenses, but anything dangling around the front of the binoculars can be a real pain in windy conditions — flapping into the field of view, and worse… introducing "shake").
An interesting touch is the inclusion of "winged" eyecup attachments to block stray light from the side. It's always great to get something unexpected… but while I enjoyed testing them, they soon went back in the box. They do cut out light from the side, which in some conditions can be a bit distracting, but I preferred using the binoculars without them, and they stop you using the rain guard… which in Ireland is a really useful tool.
The Nikon EDG comes with Nikon's 10 Year Warranty covering defects in material and workmanship.
Taken from the Nikon UK website
Magnification (x) 8
Objective diameter (mm) 42
Angular field of view (Real/degree) 7.7
Angular field of view (Apparent/degree) 56.6
Field of view at 1000m (m) 135
Exit pupil (mm) 5.3
Relative brightness 28.1
Eye relief (mm) 19.3
Close focusing distance (m) 3
Weight (g) 785
Length (mm) 148
Width (mm) 137
Interpupillary distance adjustment (mm) 55-76
Waterproof 5m
Nikon has done an outstanding job with the EDG — it is a superb binocular. There really is very little to fault — optically its as good as anything out there, it's exceptionally well made and is comfortable to carry and use. Bar a few personal foibles there's not much more to add.
Yes, they are expensive… but the best binoculars always are. Unlike, say, consumer electronics, which become dated practically overnight, binoculars age gracefully. You measure the useful life of a good pair of binoculars in decades, not a few years. If you use them every day — or even just a few times a week — then, measured over the lifetime of the product, even the most expensive binoculars work out costing just pennies per week.
If you're shopping for the best birding and wildlife optics money can buy, then you'll need to make room on your shortlist for the Nikon EDG — it's a real contender.
I'd like to thank the PR Office at Nikon UK and Ireland for submitting the EDG 8×42 for review on the Ireland's Wildlife website.
NB. Ireland's Wildlife has no specific affiliation to any optics or gear manufacturer and all reviews on the site are completely independent and objective. Reviews are carried out by a select team of experienced birders and wildlife watchers, and all gear is tested in Ireland under field conditions.
If you're an optics or gear manufacturer and would like to submit your wildlife related product for review on the site please get in touch using the contact form and we can take things from there.
Filed Under: Binocular Reviews, Featured Tagged With: binoculars, birding, full size binoculars, nikon, optics, review
About Calvin Jones
Calvin Jones is a freelance writer, author, birder and lifelong wildlife enthusiast. He is founder and editor of IrelandsWildlife.com and founder and wildlife guide of Ireland's Wildlife Tours offering wildlife and birding holidays on Ireland's south coast.
Supporting Ireland's Wildlife
Experience Ireland's Wildlife for yourself
Join us on a wildlife adventure on Ireland's Wild South Coast… and find out first hand why we call this Europe's Undiscovered Wildlife Frontier.
Ireland's Wildlife runs on the Genesis Framework from StudioPress · Hosted with InterServer
2023 Discover Wildlife Weekend Dates
Review: Hawke Frontier APO 10×42 Binocular
Book Review: Crossbill Guides, Ireland
Avian Influenza hits Irish seabird colonies
German Precision Optics (GPO) Passion HD 10×42 Binocular Review
Beneficial Garden Insects and How to Attract Them to Your Garden
Cuckoo spit/spittlebug foam on plants is harmless. Please leave it alone.
Purple Heron: an epic end to our spring Discover Wildlife Weekend
audio binoculars biodiversity birding birds Birdwatch Ireland books cetaceans citizen science CJ Wildlife competition conservation Cork fin whale full size binoculars garden birds garden wildlife Golden Eagle Trust Hawke Highly Recommended humpback whale Ireland IWDG Kerry mammals national biodiversity data centre npws optics raptors review reviews spring stranding surveys Vanguard west cork whales whales and dolphins whale watching whalewatching white tailed eagle Wildlife wildlife crime wildlife photography wildlife podcasts
Take it from the top....
Copyright © 2023 Ireland's Wildlife · Site Design by West Cork Websites · Content by CJ Writing
Like most sites, Ireland's Wildlife uses cookies to improve functionality, enhance your user experience and to gauge the popularity of our content.


WASHINGTON -- The Democrats were lying in wait for John Boehner when the Republican leader of the House announced that he would address the subject of congressional reform in a speech on Thursday at the American Enterprise Institute.
Before Boehner opened his mouth, Speaker Nancy Pelosi blasted him in a statement charging that "Congressional Republicans and Mr. Boehner have stood in the way of Democratic reform efforts in Congress for the last four years, and now they want to take America back to the exact same failed policies of the past that put the corporate special interests ahead of the middle class."
That is par for the course in this campaign season, and it represents the sort of reflexive partisanship that voters are understandably sick of.
Unless the forecasts for next month's House elections are wildly off course, the House will operate in 2011-12 with a small majority under nominal control of Pelosi or Boehner, but probably at the mercy of shifting coalitions. In such a setting, it might well behoove people to assume that Boehner should be taken seriously when he acknowledges that the reputation of this Congress is so bad that it cries out for reform.
Many of the Republican leader's proposals are standard, and some that are not are questionable. But few who serve in the House, or observe it closely, would challenge Boehner's analysis of the dynamic that has made Congress a dysfunctional legislative body and Capitol Hill a hostile workplace.
"One of the reasons why we do not have a functioning civil society in the House," he said, "is that our efforts are geared toward catering to the individual member instead of focusing on our collective responsibility to govern."
Boehner argued that on the House side, "the rules are too often manipulated to shut down debate and protect individual members from tough votes." He was too polite to say so, but the Senate is even worse when it comes to accommodating or indulging its members, at the cost of collective responsibility.
What Boehner called "a cycle of gridlock" afflicts both sides of the Capitol, and has been enabled by both parties, depending on who had the majority. As he was honest enough to admit, the abuses did not start when Pelosi took the gavel, and both sides have been guilty of twisting the rules. If the margins of control shrink next January, as I think they will, it might well be time to negotiate a truce.
I'd like to see Pelosi and the rest of the Democratic leaders take Boehner up on the challenge he has raised, not try to demean it. He said, for example, that rather than stifling debate through the manipulation of rules, "we should open things up and let the battle of ideas help break down the scar tissue between the parties. ... Let's let legislators legislate again."
It would be great if the leaders could engage each other seriously at the start of the next Congress on rules and procedures for doing the nation's business. There's no excuse for the House failing to pass a budget resolution, as happened for the first time this year.
When large majorities of the nation's voters voice disdain and distrust for a Congress that is supposed to represent them in writing the laws, it is not just a problem for one party or the other. It is a threat to our system of government.
Boehner was a serious legislator for five years at the start of this decade as chairman of the House Committee on Education and the Workforce, before he became a floor leader for his party. His diagnosis of the problems in Congress offers a starting point for a cure. Let's hope the Democrats respond. David Broder is a columnist for The Washington Post. His e-mail address is davidbroder@washpost.com.


Hello and thank you for passing by! My name is Ricky and I've been piesmithing since 2012. In the fall of 2017 I decided to share my pie crafting passion with everyone for Thanksgiving, but it didn't end there as Thanksgiving soon became Christmas, Christmas became New Year and New Year has brought me to today! My goal is to craft imaginative sweet and savory pies that captivate and satisfy!


This morning the kids spotted Tootsie hanging out waaaaay up high! Good thing he can fly or he might have needed some help getting up there. Pretty good vantage point to see all the goings-on around here, too!
While I snapped this pics was the only time this light got turned on today. We don't need a toasted Elf to send back to the North Pole. What's your Elf bee up to lately?!


text:
分子與細胞生物學研究所
Please use this identifier to cite or link to this item: http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/62739
???org.dspace.app.webui.jsptag.ItemTag.dcfield???
dc.contributor.advisor 陳俊宏(Chun-Hong Chen)
dc.contributor.author Po-Lin Chen en
dc.contributor.author 陳柏霖 zh_TW
dc.date.copyright 2020-07-15
dc.identifier.citation Abuaita, B.H., Schultz, T.L., and O'Riordan, M.X. (2018). Mitochondria-Derived Vesicles Deliver Antimicrobial Reactive Oxygen Species to Control Phagosome-Localized Staphylococcus aureus. Cell Host Microbe 24, 625-636 e625.
Altanbyek, V., Cha, S.J., Kang, G.U., Im, D.S., Lee, S., Kim, H.J., and Kim, K. (2016). Imbalance of mitochondrial dynamics in Drosophila models of amyotrophic lateral sclerosis. Biochem Biophys Res Commun 481, 259-264.
Alto, N.M., Soderling, J., and Scott, J.D. (2002). Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics. The Journal of cell biology 158, 659-668.
Amaya, C., Fader, C.M., and Colombo, M.I. (2015). Autophagy and proteins involved in vesicular trafficking. FEBS letters 589, 3343-3353.
Amr, S., Heisey, C., Zhang, M., Xia, X.J., Shows, K.H., Ajlouni, K., Pandya, A., Satin, L.S., El-Shanti, H., and Shiang, R. (2007). A homozygous mutation in a novel zinc-finger protein, ERIS, is responsible for Wolfram syndrome 2. American journal of human genetics 81, 673-683.
Bakeeva, L.E., Chentsov Yu, S., and Skulachev, V.P. (1978). Mitochondrial framework (reticulum mitochondriale) in rat diaphragm muscle. Biochim Biophys Acta 501, 349-369.
Barrett, T.G., Bundey, S.E., and Macleod, A.F. (1995). Neurodegeneration and diabetes: UK nationwide study of Wolfram (DIDMOAD) syndrome. Lancet 346, 1458-1463.
Bauer, M.F., Hofmann, S., Neupert, W., and Brunner, M. (2000). Protein translocation into mitochondria: the role of TIM complexes. Trends in cell biology 10, 25-31.
Beregi, E., Regius, O., Huttl, T., and Gobl, Z. (1988). Age-related changes in the skeletal muscle cells. Z Gerontol 21, 83-86.
Bezawork-Geleta, A., Brodie, E.J., Dougan, D.A., and Truscott, K.N. (2015). LON is the master protease that protects against protein aggregation in human mitochondria through direct degradation of misfolded proteins. Sci Rep 5, 17397.
Bhuin, T., and Roy, J.K. (2014). Rab proteins: the key regulators of intracellular vesicle transport. Experimental cell research 328, 1-19.
Bonifacino, J.S., and Glick, B.S. (2004). The mechanisms of vesicle budding and fusion. Cell 116, 153-166.
Bonifacino, J.S., and Lippincott-Schwartz, J. (2003). Coat proteins: shaping membrane transport. Nature reviews Molecular cell biology 4, 409-414.
Bossy-Wetzel, E., Barsoum, M.J., Godzik, A., Schwarzenbacher, R., and Lipton, S.A. (2003). Mitochondrial fission in apoptosis, neurodegeneration and aging. Current opinion in cell biology 15, 706-716.
Brandt, T., Mourier, A., Tain, L.S., Partridge, L., Larsson, N.G., and Kuhlbrandt, W. (2017). Changes of mitochondrial ultrastructure and function during ageing in mice and Drosophila. Elife 6.
Bueno, M., Lai, Y.C., Romero, Y., Brands, J., St Croix, C.M., Kamga, C., Corey, C., Herazo-Maya, J.D., Sembrat, J., Lee, J.S., et al. (2015). PINK1 deficiency impairs mitochondrial homeostasis and promotes lung fibrosis. J Clin Invest 125, 521-538.
Bui, M., Gilady, S.Y., Fitzsimmons, R.E., Benson, M.D., Lynes, E.M., Gesson, K., Alto, N.M., Strack, S., Scott, J.D., and Simmen, T. (2010). Rab32 modulates apoptosis onset and mitochondria-associated membrane (MAM) properties. The Journal of biological chemistry 285, 31590-31602.
Cai, H., Reinisch, K., and Ferro-Novick, S. (2007). Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell 12, 671-682.
Chang, N.C., Nguyen, M., Germain, M., and Shore, G.C. (2010). Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1. The EMBO journal 29, 606-618.
Chen, B., Shen, S., Wu, J., Hua, Y., Kuang, M., Li, S., and Peng, B. (2015). CISD2 associated with proliferation indicates negative prognosis in patients with hepatocellular carcinoma. Int J Clin Exp Pathol 8, 13725-13738.
Chen, C.H., Huang, H., Ward, C.M., Su, J.T., Schaeffer, L.V., Guo, M., and Hay, B.A. (2007). A synthetic maternal-effect selfish genetic element drives population replacement in Drosophila. Science 316, 597-600.
Chen, H., and Chan, D.C. (2009). Mitochondrial dynamics--fusion, fission, movement, and mitophagy--in neurodegenerative diseases. Human molecular genetics 18, R169-176.
Chen, Y.F., Kao, C.H., Chen, Y.T., Wang, C.H., Wu, C.Y., Tsai, C.Y., Liu, F.C., Yang, C.W., Wei, Y.H., Hsu, M.T., et al. (2009). Cisd2 deficiency drives premature aging and causes mitochondria-mediated defects in mice. Genes & development 23, 1183-1194.
Cipolat, S., Martins de Brito, O., Dal Zilio, B., and Scorrano, L. (2004). OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proceedings of the National Academy of Sciences of the United States of America 101, 15927-15932.
Clark, I.E., Dodson, M.W., Jiang, C., Cao, J.H., Huh, J.R., Seol, J.H., Yoo, S.J., Hay, B.A., and Guo, M. (2006). Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441, 1162-1166.
Colca, J.R., McDonald, W.G., Waldon, D.J., Leone, J.W., Lull, J.M., Bannow, C.A., Lund, E.T., and Mathews, W.R. (2004). Identification of a novel mitochondrial protein ('mitoNEET') cross-linked specifically by a thiazolidinedione photoprobe. American journal of physiology Endocrinology and metabolism 286, E252-260.
Coleman, R., Silbermann, M., Gershon, D., and Reznick, A.Z. (1987). Giant mitochondria in the myocardium of aging and endurance-trained mice. Gerontology 33, 34-39.
Del Campo, A., Jaimovich, E., and Tevy, M.F. (2016). Mitochondria in the Aging Muscles of Flies and Mice: New Perspectives for Old Characters. Oxid Med Cell Longev 2016, 9057593.
Demontis, F., and Perrimon, N. (2010). FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging. Cell 143, 813-825.
Deng, H., Dodson, M.W., Huang, H., and Guo, M. (2008). The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proceedings of the National Academy of Sciences of the United States of America 105, 14503-14508.
Dudek, J., Rehling, P., and van der Laan, M. (2013). Mitochondrial protein import: common principles and physiological networks. Biochim Biophys Acta 1833, 274-285.
Frank, M., Duvezin-Caubet, S., Koob, S., Occhipinti, A., Jagasia, R., Petcherski, A., Ruonala, M.O., Priault, M., Salin, B., and Reichert, A.S. (2012). Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner. Biochim Biophys Acta 1823, 2297-2310.
Geldenhuys, W.J., Benkovic, S.A., Lin, L., Yonutas, H.M., Crish, S.D., Sullivan, P.G., Darvesh, A.S., Brown, C.M., and Richardson, J.R. (2017). MitoNEET (CISD1) Knockout Mice Show Signs of Striatal Mitochondrial Dysfunction and a Parkinson's Disease Phenotype. ACS Chem Neurosci 8, 2759-2765.
Gomes, L.C., Di Benedetto, G., and Scorrano, L. (2011). During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nature cell biology 13, 589-598.
Greene, J.C., Whitworth, A.J., Kuo, I., Andrews, L.A., Feany, M.B., and Pallanck, L.J. (2003). Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proceedings of the National Academy of Sciences of the United States of America 100, 4078-4083.
Griparic, L., Kanazawa, T., and van der Bliek, A.M. (2007). Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage. The Journal of cell biology 178, 757-764.
Grosshans, B.L., Ortiz, D., and Novick, P. (2006). Rabs and their effectors: achieving specificity in membrane traffic. Proceedings of the National Academy of Sciences of the United States of America 103, 11821-11827.
Guarani, V., McNeill, E.M., Paulo, J.A., Huttlin, E.L., Frohlich, F., Gygi, S.P., Van Vactor, D., and Harper, J.W. (2015). QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology. Elife 4.
Gurkan, C., Koulov, A.V., and Balch, W.E. (2007). An evolutionary perspective on eukaryotic membrane trafficking. Adv Exp Med Biol 607, 73-83.
Haas, R.H. (2019). Mitochondrial Dysfunction in Aging and Diseases of Aging. Biology (Basel) 8.
Hachiya, N., Mihara, K., Suda, K., Horst, M., Schatz, G., and Lithgow, T. (1995). Reconstitution of the initial steps of mitochondrial protein import. Nature 376, 705-709.
Haile, Y., Deng, X., Ortiz-Sandoval, C., Tahbaz, N., Janowicz, A., Lu, J.Q., Kerr, B.J., Gutowski, N.J., Holley, J.E., Eggleton, P., et al. (2017). Rab32 connects ER stress to mitochondrial defects in multiple sclerosis. J Neuroinflammation 14, 19.
Hara, Y., Yuk, F., Puri, R., Janssen, W.G., Rapp, P.R., and Morrison, J.H. (2014). Presynaptic mitochondrial morphology in monkey prefrontal cortex correlates with working memory and is improved with estrogen treatment. Proceedings of the National Academy of Sciences of the United States of America 111, 486-491.
He, Q.Q., Xiong, L.L., Liu, F., He, X., Feng, G.Y., Shang, F.F., Xia, Q.J., Wang, Y.C., Qiu, D.L., Luo, C.Z., et al. (2016). MicroRNA-127 targeting of mitoNEET inhibits neurite outgrowth, induces cell apoptosis and contributes to physiological dysfunction after spinal cord transection. Sci Rep 6, 35205.
Hoppins, S., Lackner, L., and Nunnari, J. (2007). The machines that divide and fuse mitochondria. Annual review of biochemistry 76, 751-780.
Hughes, A.L., Hughes, C.E., Henderson, K.A., Yazvenko, N., and Gottschling, D.E. (2016). Selective sorting and destruction of mitochondrial membrane proteins in aged yeast. Elife 5.
Inupakutika, M.A., Sengupta, S., Nechushtai, R., Jennings, P.A., Onuchic, J.N., Azad, R.K., Padilla, P., and Mittler, R. (2017). Phylogenetic analysis of eukaryotic NEET proteins uncovers a link between a key gene duplication event and the evolution of vertebrates. Sci Rep 7, 42571.
Johnson, D.C., Dean, D.R., Smith, A.D., and Johnson, M.K. (2005). Structure, function, and formation of biological iron-sulfur clusters. Annual review of biochemistry 74, 247-281.
Kiral, F.R., Kohrs, F.E., Jin, E.J., and Hiesinger, P.R. (2018). Rab GTPases and Membrane Trafficking in Neurodegeneration. Current biology : CB 28, R471-R486.
Koopman, W.J., Visch, H.J., Verkaart, S., van den Heuvel, L.W., Smeitink, J.A., and Willems, P.H. (2005). Mitochondrial network complexity and pathological decrease in complex I activity are tightly correlated in isolated human complex I deficiency. Am J Physiol Cell Physiol 289, C881-890.
Kusminski, C.M., Holland, W.L., Sun, K., Park, J., Spurgin, S.B., Lin, Y., Askew, G.R., Simcox, J.A., McClain, D.A., Li, C., et al. (2012). MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity. Nature medicine 18, 1539-1549.
Leduc-Gaudet, J.P., Picard, M., St-Jean Pelletier, F., Sgarioto, N., Auger, M.J., Vallee, J., Robitaille, R., St-Pierre, D.H., and Gouspillou, G. (2015). Mitochondrial morphology is altered in atrophied skeletal muscle of aged mice. Oncotarget 6, 17923-17937.
Lonhienne, T.G., Sagulenko, E., Webb, R.I., Lee, K.C., Franke, J., Devos, D.P., Nouwens, A., Carroll, B.J., and Fuerst, J.A. (2010). Endocytosis-like protein uptake in the bacterium Gemmata obscuriglobus. Proceedings of the National Academy of Sciences of the United States of America 107, 12883-12888.
MacVicar, T., and Langer, T. (2016). OPA1 processing in cell death and disease - the long and short of it. Journal of cell science 129, 2297-2306.
Matheoud, D., Sugiura, A., Bellemare-Pelletier, A., Laplante, A., Rondeau, C., Chemali, M., Fazel, A., Bergeron, J.J., Trudeau, L.E., Burelle, Y., et al. (2016). Parkinson's Disease-Related Proteins PINK1 and Parkin Repress Mitochondrial Antigen Presentation. Cell 166, 314-327.
Mattson, M.P. (1998). Modification of ion homeostasis by lipid peroxidation: roles in neuronal degeneration and adaptive plasticity. Trends Neurosci 21, 53-57.
Mattson, M.P. (2000). Apoptosis in neurodegenerative disorders. Nature reviews Molecular cell biology 1, 120-129.
Miyamoto, Y., Kitamura, N., Nakamura, Y., Futamura, M., Miyamoto, T., Yoshida, M., Ono, M., Ichinose, S., and Arakawa, H. (2011). Possible existence of lysosome-like organella within mitochondria and its role in mitochondrial quality control. PLoS One 6, e16054.
Moehle, E.A., Shen, K., and Dillin, A. (2019). Mitochondrial proteostasis in the context of cellular and organismal health and aging. The Journal of biological chemistry 294, 5396-5407.
Murgia, M., Toniolo, L., Nagaraj, N., Ciciliot, S., Vindigni, V., Schiaffino, S., Reggiani, C., and Mann, M. (2017). Single Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging. Cell Rep 19, 2396-2409.
Neuspiel, M., Schauss, A.C., Braschi, E., Zunino, R., Rippstein, P., Rachubinski, R.A., Andrade-Navarro, M.A., and McBride, H.M. (2008). Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers. Current biology : CB 18, 102-108.
Noda, S., Sato, S., Fukuda, T., Tada, N., Uchiyama, Y., Tanaka, K., and Hattori, N. (2020). Loss of Parkin contributes to mitochondrial turnover and dopaminergic neuronal loss in aged mice. Neurobiol Dis 136, 104717.
Ogata, T., and Yamasaki, Y. (1997). Ultra-high-resolution scanning electron microscopy of mitochondria and sarcoplasmic reticulum arrangement in human red, white, and intermediate muscle fibers. Anat Rec 248, 214-223.
Ohbayashi, N., Fukuda, M., and Kanaho, Y. (2017). Rab32 subfamily small GTPases: pleiotropic Rabs in endosomal trafficking. J Biochem 162, 65-71.
Ortiz-Sandoval, C.G., Hughes, S.C., Dacks, J.B., and Simmen, T. (2014). Interaction with the effector dynamin-related protein 1 (Drp1) is an ancient function of Rab32 subfamily proteins. Cell Logist 4, e986399.
Osborne, B.A., and Minter, L.M. (2007). Notch signalling during peripheral T-cell activation and differentiation. Nature reviews Immunology 7, 64-75.
Park, J., Lee, S.B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.M., et al. (2006). Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441, 1157-1161.
Payne, B.A., and Chinnery, P.F. (2015). Mitochondrial dysfunction in aging: Much progress but many unresolved questions. Biochim Biophys Acta 1847, 1347-1353.
Perumalsamy, L.R., Nagala, M., and Sarin, A. (2010). Notch-activated signaling cascade interacts with mitochondrial remodeling proteins to regulate cell survival. Proceedings of the National Academy of Sciences of the United States of America 107, 6882-6887.
Pesah, Y., Pham, T., Burgess, H., Middlebrooks, B., Verstreken, P., Zhou, Y., Harding, M., Bellen, H., and Mardon, G. (2004). Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 131, 2183-2194.
Picard, M., White, K., and Turnbull, D.M. (2013). Mitochondrial morphology, topology, and membrane interactions in skeletal muscle: a quantitative three-dimensional electron microscopy study. J Appl Physiol (1985) 114, 161-171.
Picard, M., Zhang, J., Hancock, S., Derbeneva, O., Golhar, R., Golik, P., O'Hearn, S., Levy, S., Potluri, P., Lvova, M., et al. (2014). Progressive increase in mtDNA 3243A>G heteroplasmy causes abrupt transcriptional reprogramming. Proceedings of the National Academy of Sciences of the United States of America 111, E4033-4042.
Pickrell, A.M., and Youle, R.J. (2015). The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease. Neuron 85, 257-273.
Rajendran, L., Knolker, H.J., and Simons, K. (2010). Subcellular targeting strategies for drug design and delivery. Nature reviews Drug discovery 9, 29-42.
Ramirez, S., Gomez-Valades, A.G., Schneeberger, M., Varela, L., Haddad-Tovolli, R., Altirriba, J., Noguera, E., Drougard, A., Flores-Martinez, A., Imbernon, M., et al. (2017). Mitochondrial Dynamics Mediated by Mitofusin 1 Is Required for POMC Neuron Glucose-Sensing and Insulin Release Control. Cell Metab 25, 1390-1399 e1396.
Rana, A., Oliveira, M.P., Khamoui, A.V., Aparicio, R., Rera, M., Rossiter, H.B., and Walker, D.W. (2017). Promoting Drp1-mediated mitochondrial fission in midlife prolongs healthy lifespan of Drosophila melanogaster. Nat Commun 8, 448.
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010). Mitochondrial fission and remodelling contributes to muscle atrophy. The EMBO journal 29, 1774-1785.
Ruan, L., Zhou, C., Jin, E., Kucharavy, A., Zhang, Y., Wen, Z., Florens, L., and Li, R. (2017). Cytosolic proteostasis through importing of misfolded proteins into mitochondria. Nature 543, 443-446.
Schneeberger, M., Dietrich, M.O., Sebastian, D., Imbernon, M., Castano, C., Garcia, A., Esteban, Y., Gonzalez-Franquesa, A., Rodriguez, I.C., Bortolozzi, A., et al. (2013). Mitofusin 2 in POMC neurons connects ER stress with leptin resistance and energy imbalance. Cell 155, 172-187.
Shen, Q., Yamano, K., Head, B.P., Kawajiri, S., Cheung, J.T., Wang, C., Cho, J.H., Hattori, N., Youle, R.J., and van der Bliek, A.M. (2014). Mutations in Fis1 disrupt orderly disposal of defective mitochondria. Molecular biology of the cell 25, 145-159.
Shen, Z.Q., Chen, Y.F., Chen, J.R., Jou, Y.S., Wu, P.C., Kao, C.H., Wang, C.H., Huang, Y.L., Chen, C.F., Huang, T.S., et al. (2017). CISD2 Haploinsufficiency Disrupts Calcium Homeostasis, Causes Nonalcoholic Fatty Liver Disease, and Promotes Hepatocellular Carcinoma. Cell Rep 21, 2198-2211.
Shenouda, S.M., Widlansky, M.E., Chen, K., Xu, G., Holbrook, M., Tabit, C.E., Hamburg, N.M., Frame, A.A., Caiano, T.L., Kluge, M.A., et al. (2011). Altered mitochondrial dynamics contributes to endothelial dysfunction in diabetes mellitus. Circulation 124, 444-453.
Shirihai, O.S., Song, M., and Dorn, G.W., 2nd (2015). How mitochondrial dynamism orchestrates mitophagy. Circulation research 116, 1835-1849.
Sing, A., Tsatskis, Y., Fabian, L., Hester, I., Rosenfeld, R., Serricchio, M., Yau, N., Bietenhader, M., Shanbhag, R., Jurisicova, A., et al. (2014). The atypical cadherin fat directly regulates mitochondrial function and metabolic state. Cell 158, 1293-1308.
Sohn, Y.S., Tamir, S., Song, L., Michaeli, D., Matouk, I., Conlan, A.R., Harir, Y., Holt, S.H., Shulaev, V., Paddock, M.L., et al. (2013). NAF-1 and mitoNEET are central to human breast cancer proliferation by maintaining mitochondrial homeostasis and promoting tumor growth. Proceedings of the National Academy of Sciences of the United States of America 110, 14676-14681.
Song, Z., Chen, H., Fiket, M., Alexander, C., and Chan, D.C. (2007). OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. The Journal of cell biology 178, 749-755.
Tagaya, M., and Arasaki, K. (2017). Regulation of Mitochondrial Dynamics and Autophagy by the Mitochondria-Associated Membrane. Adv Exp Med Biol 997, 33-47.
Tarasenko, D., Barbot, M., Jans, D.C., Kroppen, B., Sadowski, B., Heim, G., Mobius, W., Jakobs, S., and Meinecke, M. (2017). The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology. The Journal of cell biology 216, 889-899.
Trushina, E., Nemutlu, E., Zhang, S., Christensen, T., Camp, J., Mesa, J., Siddiqui, A., Tamura, Y., Sesaki, H., Wengenack, T.M., et al. (2012). Defects in mitochondrial dynamics and metabolomic signatures of evolving energetic stress in mouse models of familial Alzheimer's disease. PLoS One 7, e32737.
van der Bliek, A.M., Shen, Q., and Kawajiri, S. (2013). Mechanisms of mitochondrial fission and fusion. Cold Spring Harbor perspectives in biology 5.
Vanlandingham, P.A., and Ceresa, B.P. (2009). Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration. The Journal of biological chemistry 284, 12110-12124.
Vincent, A.E., White, K., Davey, T., Philips, J., Ogden, R.T., Lawess, C., Warren, C., Hall, M.G., Ng, Y.S., Falkous, G., et al. (2019). Quantitative 3D Mapping of the Human Skeletal Muscle Mitochondrial Network. Cell Rep 26, 996-1009 e1004.
Waschbusch, D., Hubel, N., Ossendorf, E., Lobbestael, E., Baekelandt, V., Lindsay, A.J., McCaffrey, M.W., Khan, A.R., and Barnekow, A. (2019). Rab32 interacts with SNX6 and affects retromer-dependent Golgi trafficking. PLoS One 14, e0208889.
Weir, H.J., Yao, P., Huynh, F.K., Escoubas, C.C., Goncalves, R.L., Burkewitz, K., Laboy, R., Hirschey, M.D., and Mair, W.B. (2017). Dietary Restriction and AMPK Increase Lifespan via Mitochondrial Network and Peroxisome Remodeling. Cell Metab 26, 884-896 e885.
Wiley, S.E., Murphy, A.N., Ross, S.A., van der Geer, P., and Dixon, J.E. (2007). MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. Proceedings of the National Academy of Sciences of the United States of America 104, 5318-5323.
Winklhofer, K.F., and Haass, C. (2010). Mitochondrial dysfunction in Parkinson's disease. Biochim Biophys Acta 1802, 29-44.
Wolfram, D. (1938). Diabetes mellitus and simple optic atrophy among siblings: Report of 4 cases. 13, 715-718.
Yamada, T., Murata, D., Adachi, Y., Itoh, K., Kameoka, S., Igarashi, A., Kato, T., Araki, Y., Huganir, R.L., Dawson, T.M., et al. (2018). Mitochondrial Stasis Reveals p62-Mediated Ubiquitination in Parkin-Independent Mitophagy and Mitigates Nonalcoholic Fatty Liver Disease. Cell Metab 28, 588-604 e585.
Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J.W., Yang, L., Beal, M.F., Vogel, H., and Lu, B. (2006). Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proceedings of the National Academy of Sciences of the United States of America 103, 10793-10798.
Youle, R.J., and Strasser, A. (2008). The BCL-2 protein family: opposing activities that mediate cell death. Nature reviews Molecular cell biology 9, 47-59.
Yu, T., Sheu, S.S., Robotham, J.L., and Yoon, Y. (2008). Mitochondrial fission mediates high glucose-induced cell death through elevated production of reactive oxygen species. Cardiovasc Res 79, 341-351.
Yu, W., Sun, Y., Guo, S., and Lu, B. (2011). The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons. Human molecular genetics 20, 3227-3240.
Zerial, M., and McBride, H. (2001). Rab proteins as membrane organizers. Nature reviews Molecular cell biology 2, 107-117.
Zhang, X., Zuo, X., Yang, B., Li, Z., Xue, Y., Zhou, Y., Huang, J., Zhao, X., Zhou, J., Yan, Y., et al. (2014). MicroRNA directly enhances mitochondrial translation during muscle differentiation. Cell 158, 607-619.
dc.identifier.uri http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/62739 -
dc.description.abstract 過去研究指出老化相關疾病常伴隨粒線體形態及功能的異常,且年老的哺乳動物中,粒線體形態有巨大化的現象,顯示粒線體形態與功能的調控與老化息息相關,然而其中調控機制尚未清楚,因此我利用果蠅的肌肉組織為模型,探討粒線體於老化過程中形態及功能變化的詳細機制。我的研究中發現了參與調控老化的重要基因,Dosmit (Downsizing mitochondria)。Dosmit座落於粒線體外膜,其表現量隨老化漸增,並同時促進胞質蛋白進入粒線體,暗示此行為與老化相關,但機制仍未清楚。在Dosmit高量表現的條件下,粒線體呈現巨大化且內部產生許多含有胞質蛋白的雙層膜囊泡,而此囊泡被推測具有運輸功能。透過追蹤粒線體外膜蛋白Tom20,證明此雙層膜囊泡的膜系源自粒線體外膜。本論文進一步證明GTPase,Rab32不僅與Dosmit有蛋白間交互作用,且與Dosmit共同調控粒線體的巨大化及囊泡生成。於老化的果蠅中也可以觀察到粒線體巨大化及囊泡的產生,並發現泛素化蛋白大量在粒線體的囊泡中累積,且在粒線體蛋白酶Lon的缺失下,將引起更劇烈的泛素化蛋白累積現象,指出泛素化蛋白可能透過囊泡進入粒線體,並藉由蛋白酶Lon使其降解而維持粒線體功能平衡。Dosmit在哺乳動物中區分為Cisd1及Cisd2,而Dosmit卻融合了此二基因的序列,我將小鼠的Cisd1及Cisd2融合成重組基因,發現此重組基因能救回Dosmit剔除時所產生的粒線體缺陷。Dosmit的研究成果將為粒線體所造成的老化疾病提供新的治療途徑。 zh_TW
dc.description.abstract Mitochondrial aging, which results in mitochondrial dysfunction, is strongly linked to many age-related diseases. Aging is associated with mitochondrial enlargement and changes in the transport of cytosolic proteins into mitochondria. The underlying homeostatic mechanisms that regulate mitochondrial morphology and function, and breakdown during aging, remain unclear, though various important cytosolic proteins are known to be imported into mitochondria via a canonical pathway mediated by mitochondrial translocases (the TIM/TOM complex). Here I identify a novel pathway for mitochondrial protein trafficking in Drosophila melanogaster, involving the mitochondria-associated protein Dosmit. I found that Dosmit induces the formation of double-membraned vesicles within mitochondria, that the rate of vesicle formation increases with age, and that increased expression of Dosmit causes mitochondrial enlargement. When cytosolic green fluorescent protein (GFP) was ectopically expressed with Dosmit, intramitochondrial vesicles imported GFP from the cytosol. The outer-mitochondrial-membrane marker Tom20 was also associated with these vesicles, suggesting they originate from the outer mitochondrial membrane. The membrane trafficking process was mediated by the mitochondria-associated Rab protein Rab32. Dosmit expression levels were closely linked to the rate of aggregation of ubiquitinated proteins, which are themselves associated with age-related diseases. Finally, I found that expression of a hybrid form of the Dosmit mouse homolog resulted in a similar phenotype to that found with Drosophila Dosmit expression, suggesting a high level of evolutional conservation. This novel mitochondrial protein trafficking route mediated by Dosmit offers a promising target for future therapies targeting age-related mitochondrial diseases. en
dc.description.provenance Made available in DSpace on 2021-06-16T16:09:02Z (GMT). No. of bitstreams: 1
ntu-109-D04b43001-1.pdf: 18555781 bytes, checksum: 07eaa612c0aaf1d4fc653bf8c3bcf8bf (MD5)
Previous issue date: 2020 en
dc.description.tableofcontents 致謝 i
中文摘要 ii
Abstract iii
1. Introduction 1
1.1 Mitochondrial function and dynamics 1
1.2 Mitochondrial defects in age-related neurological disorders 3
1.3 Mitochondria and aging 5
1.4 Mitochondrial import 6
1.5 Vesicular trafficking 7
1.6 Cisd protein family 10
2. Specific aims 13
3. Materials and Methods 14
3.1 Fly stocks and maintenance 14
3.2 Plasmids 15
3.3 Antibodies 16
3.4 Immunofluorescent staining of Drosophila muscle 16
3.5 Western blotting 17
3.6 Lifespan assay 18
3.7 Climbing assay 18
3.8 Co-immunoprecipitation (Co-IP) assay 18
3.9 Digitonin/proteinase K assay for S2 cells and tissue 19
3.10 Transmission electron microscopy 20
3.11 Immunoelectron microscopy and immunolabelling 20
3.12 Isolation of mitochondria from Drosophila flight-muscle tissue 21
3.13 Statistics and Reproducibility 21
4. Results 23
4.1 Aged mitochondria increase in size and contain intramitochondrial vesicles 23
4.2 Increase in mitochondrial size is not associated with the mitochondrial dynamic proteins Marf, Opa1, Drp1, and Fis1 25
4.3 Dosmit is a novel mitochondrial outer membrane protein which regulates mitochondrial morphology 27
4.4 Dosmit expression level was associated with aging and mitochondrial size 30
4.5 Ectopic expression of Dosmit enlarges mitochondria and induces the formation of intramitochondrial vesicles 32
4.6 Cytosolic proteins can be taken into intramitochondrial vesicles 35
4.7 Intramitochondrial vesicle membranes contain the outer-membrane protein Tom20 38
4.8 Aged and enlarged mitochondria import cytosolic GFP 40
4.9 Dosmit induces the formation of ubiquitinated proteins-containing vesicles in mitochondria 41
4.10 Rab32 interacts with Dosmit and locates on mitochondria that is mutually dependent 43
4.11 Rab32 plays a critical role in regulating Dosmit-driven mitochondrial enlargement and vesicle formation 45
4.12 Dosmit-induced mitochondrial enlargement may be suppressed by Drp1-induced mitochondrial dynamics 47
4.13 The N-terminus and CDGSH domains were required for Dosmit-induced mitochondrial enlargement 48
4.14 Mouse Cisd-domain hybrid protein may cause mitochondrial enlargement and rescue Drosophila Dosmit mutants 49
5. Discussion 51
6. References 59
7. Figures 71
dc.title 囊泡運輸參與胞質與粒線體間傳遞之功能探討 zh_TW
dc.title A Novel Vesicular-Transport Pathway Mediates the Uptake of Cytoplasmic Proteins into Mitochondria en
dc.date.schoolyear 108-2
dc.description.degree 博士
dc.contributor.oralexamcommittee 吳益群(Yi-Chun Wu),王致恬(Chih-Tien Wang),汪宏達(Horng-Dar Wang),詹智強(Chih-Chiang Chan)
dc.subject.keyword 果蠅,老化,粒線體,囊泡,泛素化蛋白, zh_TW
dc.subject.keyword Drosophila melanogaster,aging,mitochondria,intramitochondrial vesicles,ubiquitinated proteins, en
dc.relation.page 116
dc.identifier.doi 10.6342/NTU202000905
dc.rights.note 有償授權
dc.contributor.author-college 生命科學院 zh_TW
dc.contributor.author-dept 分子與細胞生物學研究所 zh_TW
dc.date.embargo-terms 2300-01-01
dc.date.embargo-lift 2300-01-01 -
Appears in Collections: 分子與細胞生物學研究所
ntu-109-1.pdf
Restricted Access 18.12 MB Adobe PDF


text:
Topaz Gigapixel AI 6.2.2 Free Download For Lifetime
Leave a Comment / Graphic Design, Windows
Topaz Gigapixel AI Overview
Topaz Gigapixel AI 6.2.2 is a powerful software tool for upsampling and resizing images. It uses artificial intelligence to generate high-resolution versions of low-resolution images, making it an excellent choice for photographers and graphic designers looking to improve the quality of their images. You can also download Adobe Photoshop CC 2023 Latest Version. Or, You can visit our Graphics Design Category for more collections.
One of the standout features of Topaz Gigapixel AI 6.2.2 is its ability to intelligently analyze the content of an image and generate new pixels that are visually similar to the existing ones. This results in images that are more detailed and realistic, with minimal loss of quality.
Another advantage of Topaz Gigapixel AI 6.2.2 is its ease of use. The interface is intuitive and straightforward, allowing users to quickly and easily apply the upsampling process to their images. The software also includes a range of presets and customization options, giving users the ability to fine-tune the upsampling process to suit their specific needs.
Overall, Topaz Gigapixel AI is a valuable tool for anyone looking to improve the quality of their images. Its advanced artificial intelligence and ease of use make it a top choice for professionals and enthusiasts alike.
Topaz Gigapixel AI 6.2.2 Top Features
Here, we included some of the latest and top features of Topaz Gigapixel AI, which are listed below—
Advanced artificial intelligence: The software uses AI to analyze the content of an image and generate new pixels that are visually similar to the existing ones, resulting in high-quality upsampled images.
Ease of use: The interface is intuitive and straightforward, making it easy for users to apply the upsampling process to their images.
Customization options: The software includes a range of presets and customization options, allowing users to fine-tune the upsampling process to suit their specific needs.
Support for various image formats: Topaz Gigapixel AI supports a wide range of image formats, including JPG, PNG, TIFF, and more.
Batch processing: The software allows users to process multiple images at once, saving time and effort.
Compatibility with various operating systems: Topaz Gigapixel AI is compatible with Windows and Mac operating systems.
Regular updates: The software is regularly updated with new features and improvements.
Technical Details and System Requirements
Operating System: Windows 7/8/10/11
RAM: 8 GB RAM (16 G.B. recommended)
GPU VRAM: 2 GB RAM (4 G.B. recommended)
Free Hard Disk Space: 10 G.B. or more
Topaz Gigapixel AI 6.2.2 Free Download
To download Topaz Gigapixel AI 6.2.2 latest version, click on the below button to start downloading. Which is a completely offline standalone setup for Windows Operating System.
Download Topaz Gigapixel AI 6.2.2
Password: softzar
Topaz Video AI 3.0.11 Free Download For Lifetime
Topaz DeNoise AI 3.7.1 Free Download For Lifetime
Topaz Sharpen AI 4.1.0 Free Download For Lifetime


– ranches for teens and schools troubled teens.
ANASAZI is an intervention resource for parents and professionals who are reaching out to help a child making at-risk choices. Offer a 42 day, wilderness based, residential treatment program and outpatient services rooted in the belief that all young people possess an inherent "seed of greatness".
Should you need help finding homes for troubled kids, therapeutic boarding schools, Christian boarding schools or residential schools for troubled teens, please let us know. As the parent of a troubled teen, you're faced with even greater challenges. This is especially true if your teen is abusing drugs or alcohol. A troubled teen faces behavioral, emotional, or learning problems beyond the normal teenage issues. While any negative behavior repeated over and over can be a sign of underlying trouble, it's important for parents to understand which behaviors are normal during adolescent development, and which can point to more serious problems.


Fayum located 100 kilometres (62 miles) southwest of Cairo, in the Fayum Oasis. It is one of Egypt's oldest cities due to its strategic location. Archaeological evidence has found occupations around the Fayum dating back to at least the Epipalaeolithic period. The middle Holocene occupations of the area are most widely studied on the north shore of Lake Qarun, where Caton-Thompson and Gardner did a number of excavations of Epipalaeolithic and Neolithic sites, as well as a general survey of the area.
GRENFELL Bernard P. - HUNT Arthur S. - HOGARTH D.G.
The Tebtunis papyri. Vol. III,1. Nos 690-825. Vol. III,2. Nos 826-1093.
(GRENFELL Bernard P.) - HUNT Arthur S. - SMILY J.G.


text:
Home Shipping Cargo ship sinks in strong winds in Taiwan, four crew members missing
Cargo ship sinks in strong winds in Taiwan, four crew members missing
Four of five seafarers on a general cargo ship carrying containers are feared dead after going missing when the vessel sank on 3 January.
In the early morning local time on 3 January, the Mongolian-flagged 2001-built 890 dwt Long Shun, sailing around Matsu Islands in Lienchiang County, sent a distress signal, indicating that it was taking in water after hitting a large wave. The ship is said to be owned by Hua-yu Shipping, a Taiwanese company.
The Taiwan Coast Guard sent one ship, three boats and two helicopters to the rescue, and at the same time requested the support of the air force. China's Maritime Safety Administration also sent three rescue vessels in a joint cross-strait effort. However, when the rescue personnel reached the scene, only one seafarer, who had clung to life by sitting on a floating container, was found. A video clip of the rescue shows the seafarer shivering in level 7 wind amid turbulent waves.
The strong wind and waves swept the seafarer into the sea, but he was brought ashore. The seafarer subsequently tested positive for Covid-19 and remains quarantined in a Taiwanese military camp in Dongyin. The search for the missing seafarers continues.
Source: Container News
Previous articleMSC to Share Expertise at Fruit Logistica 2023
Next articleMSC ship grounds at mouth of Italy's largest container port


text:
Deciding on Your Membership Model Deciding on Your Membership Model
- 08/03/201907/31/2019 - David Leduc
The Different Types of Membership Sites
There are fundamentally two sorts of enrollment locales. There are free destinations and there are paid for locales. The two kinds of participation destinations make them thing is normal. Their participations are comprised of individuals who offer a typical intrigue or have a typical need.
You can, obviously, purchase a space, set up a site and not charge for enrollments but rather pick who to concede and who not to concede. This is done when the benefit is expected to originate from deals to individuals after they join the site. There are free system destinations that may be utilized for your motivations. Two instances of free participation locales are Group destinations on MSN and gatherings on Yahoo. It costs nothing to set these destinations up and there is no charge at all for an individual to join. There are no paid executives or mediators.
Each site sets its own principles for how to join and the implicit rules for the site. The site points are numerous and fluctuated. There are many "support" locales for those with medical issues or concerns and for the individuals who have endured the loss of friends and family. There are locales for the individuals who are energetic about specialties like sewing or carpentry. There are locales for the individuals who love to travel. There are destinations for various age bunches from youngsters to seniors. The locales incorporate visit programming and a constrained measure of room for posting pictures, records and connections per part. The free locales don't have such things as access to particular information or records. They don't offer access to such things as music exercises.
Paid for enrollment destinations are set up by organizations or people with the goal of making cash by providing hard to discover data, access to particular information or records, or guidance in different fields. Participation locales are claimed and worked by individuals who either possess the destinations or who are contracted by the site proprietors to screen and manage them. The subjects for paid for enrollment destinations are significantly more fluctuated than the free locales and surely progressively particular.
Settling on Your Membership Model
The model you settle on for your enrollment site is absolutely critical and the one you pick relies on your targets. There are essentially two sorts of participation destinations. There are free destinations and there are paid for locales. The two sorts of enrollment destinations make them thing is normal. Their enrollments are comprised of individuals who offer a typical need or have a typical intrigue.
You can, obviously, purchase a space, set up a site and not charge for participations but rather pick who to concede and who not to concede. Or then again you can simply set up a site on an effectively settled system. Two instances of free enrollment locales are Group destinations on MSN and gatherings on Yahoo. It costs nothing to set these destinations up and there is no charge at all for an individual to join.
There are no paid chairmen or arbitrators. Each site sets its very own principles for how to join and the set of principles for the site. The site subjects are numerous and fluctuated. There are many "support" locales for those with medical issues or concerns and for the individuals who have endured the loss of friends and family. There are destinations for the individuals who are enthusiastic about specialties like sewing or carpentry. There are locales for the individuals who love to travel. There are destinations for various age bunches from youngsters to seniors. The locales incorporate talk programming and a constrained measure of room for posting pictures, reports and connections per part. The free destinations don't have such things as access to specific information or records. They don't offer access to such things as music exercises.
Paid for participation destinations are set up by organizations or people with the goal of making cash by providing hard to discover data, access to particular information or records, or guidance in different fields. Participation destinations are claimed and worked by individuals who either possess the locales or who are procured by the site proprietors to screen and regulate them. The subjects for paid for enrollment locales are much more differed than the free destinations and positively increasingly specific.
Please Leave Feedback
Man and woman training with dumbbells neon sign. Fitness club, sport and advertisement design. Night bright neon sign, colorful billboard, light banner. Vector illustration in neon style.
Copyright secured by Digiprove © 2019 David Leduc
Why You Should Start A Membership Site?
It Is Safe To Say That You Are Already Marketing On The Internet