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KMoore4318
Pistoj Doulos Unum Pluribus
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Re:It's exciting to be part of this!!
2012/03/20 14:23:55
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This is great news, and a wonderful reminder of why we do what we do. Thank you for posting it
  Just clink Link to Register > My Affiliate Code:VTJPDC4OMB 1)965 V-8 E758(77)580 AX1200 2)980 NH-U12P-SE E761(77)2(980) AX1200 3)980X H-70 E770 (77)2(590) AX1200 4)980X H-70 E762(77)2(580) AX1200 5)920 EVGA Super Cooler E756(82)590 HX1000 6)680I 2(560-ti) HX1000W
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blkhole
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Re:It's exciting to be part of this!!
2012/03/20 14:25:09
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troy8d
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Re:It's exciting to be part of this!!
2012/03/20 16:03:59
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Re:It's exciting to be part of this!!
2012/03/20 16:06:23
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Wholly cow that is awesome!
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Viper97
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Re:It's exciting to be part of this!!
2012/03/20 16:36:53
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I'm glad to see that PG is finally putting information out in such a way that people can understand it. Also, I'm glad that all those that fold for whatever team have contributed. I just wish they had done this months ago.
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farthestkris
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Re:It's exciting to be part of this!!
2012/03/20 17:01:54
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staypuft
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Re:It's exciting to be part of this!!
2012/03/20 18:41:50
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EK_Derick
EK Forum Support
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Re:It's exciting to be part of this!!
2012/03/20 21:44:24
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Articles like this make the thousands I've spent on folding completely worth it. Fold on everyone.
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Re:It's exciting to be part of this!!
2012/03/20 21:55:32
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after almost a decade finally something that could come out soon instrest of being papper weight
I MUST FOLD HARDER!!!
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Simba123
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Re:It's exciting to be part of this!!
2012/03/20 22:42:59
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texinga
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Re:It's exciting to be part of this!!
2012/03/21 03:53:17
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Absolutely beautiful...it is terrific to see this fruit from our contributions. Fold-on my Bros!! 
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Re:It's exciting to be part of this!!
2012/03/21 10:01:41
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Awesome news, always nice to see that we are making a difference, keep folding/crunching!!!
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notfordman
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Re:It's exciting to be part of this!!
2012/03/22 12:31:08
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That is wonderfull news!! Mutant's huh? 
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Re:It's exciting to be part of this!!
2012/03/22 13:27:10
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iancook221188
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Re:It's exciting to be part of this!!
2012/03/22 16:46:27
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more very important news we getting somewhere now can make a new thread if wanted http://folding.typepad.com/news/2012/03/index.html From the Official FAH Blog: March 21, 2012
FAH simulations lead to a new therapeutic strategy for Alzheimer's Disease
I'm very excited to finally talk about some key new results from our lab. These results have been a long time in coming and in many ways represents a major achievement for Folding@home (FAH) in general, demonstrating that the approach we started 10 years ago can make significant steps forward in our long term goals.
Specifically, our long term goals have been to 1) develop new methods to tackle the computational challenges of simulating protein folding; 2) apply these methods to gain new insights into protein folding; 3) use these methods and new insights to simulate Aß protein misfolding, a key process in the toxicity of Alzheimer's Disease (AD); and finally 4) to use those simulations to develop new small molecule drug candidates for AD. In the early years of FAH, we concentrated on the first two goals above. In the last 5-7 years, we have worked to accomplish the third goal. I'm now very excited to report our progress on the last goal –– using FAH for the development of new therapeutic strategies for AD.
In a paper just published in the Journal of Medicinal Chemistry, we report on tests of predictions from earlier Folding@home simulations, and how these predictions have led to a new strategy to fight Alzheimer's Disease. While this is not a cure, it is a major step towards our final goal, some light at the end of the tunnel.
The next steps, now underway in our lab, are to take this lead compound and help push it towards a viable drug. It's too early to report on our preliminary results there (I like to only talk publicly about work after it's passed through peer review), I'm very excited that the directions set out in this paper do appear to be bearing fruit in terms of a viable drug (not just a drug candidate). I hope I'll have more to say in the coming months!
Design of β-Amyloid Aggregation Inhibitors from a Predicted Structural Motif
Paul A. Novick†, Dahabada H. Lopes‡, Kim M. Branson†, Alexandra Esteras-Chopo§, Isabella A. Graef§, Gal Bitan‡, and Vijay S. Pande†*
† Department of Chemistry, Stanford University, Stanford, California 94305, United States
‡ Department of Neurology, UCLA, Los Angeles, California 90095, United States; Brain Research Institute, UCLA, Los Angeles, California 90095, United States; Molecular Biology Institute, UCLA, Los Angeles, California 90095, United States
§ Department of Pathology, Stanford University, Stanford, California 94305, United States
*Corresponding author.
Abstract
Drug design studies targeting one of the primary toxic agents in Alzheimer’s disease, soluble oligomers of amyloid β-protein (Aβ), have been complicated by the rapid, heterogeneous aggregation of Aβ and the resulting difficulty to structurally characterize the peptide. To address this, we have developed [Nle35, d-
Pro37]Aβ42, a substituted peptide inspired from molecular dynamics simulations which forms structures stable enough to be analyzed by NMR. We report herein that [Nle35, d-Pro37]Aβ42 stabilizes the trimer and prevents mature fibril and β-sheet formation. Further, [Nle35, d-Pro37]Aβ42 interacts with WT Aβ42 and reduces aggregation levels and fibril formation in mixtures. Using ligand-based drug design based on [Nle35, d-Pro37]Aβ42, a lead compound was identified with effects on inhibition similar to the peptide. The ability of [Nle35, d-Pro37]Aβ42 and the compound to inhibit the aggregation of Aβ42 provides a novel tool to study the structure of Aβ oligomers. More broadly, our data demonstrate how molecular dynamics simulation can guide experiment for further research into AD.
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