Results 71 to 80 of about 6,813,928 (408)

Protein folding disorders: Toward a basic biological paradigm [PDF]

, 2010
Mechanistic 'physics' models of protein folding fail to account for the observed spectrum of protein folding and aggregation disorders, suggesting that a more appropriately biological paradigm will be needed for understanding the etiology ...
Rodrick Wallace
core   +3 more sources

Refining the NaV1.7 pharmacophore of a class of venom‐derived peptide inhibitors via a combination of in silico screening and rational engineering

FEBS Letters, EarlyView.
Venom peptides have shown promise in treating pain. Our study uses computer screening to identify a peptide that targets a sodium channel (NaV1.7) linked to chronic pain. We produced the peptide in the laboratory and refined its design, advancing the search for innovative pain therapies.
Gagan Sharma, Jennifer R. Deuis, Xinying Jia, Theo Crawford, Sassan Rahnama, Eivind A. B. Undheim, Irina Vetter, Yanni K. ‐Y. Chin, Mehdi Mobli   +8 more
wiley   +1 more source

Learning inverse folding from millions of predicted structures

bioRxiv, 2022
We consider the problem of predicting a protein sequence from its backbone atom coordinates. Machine learning approaches to this problem to date have been limited by the number of available experimentally determined protein structures.
Chloe Hsu, Robert Verkuil, Jason Liu, Zeming Lin, B. Hie, Tom Sercu, Adam Lerer, Alexander Rives   +7 more
semanticscholar   +1 more source

The power of microRNA regulation—insights into immunity and metabolism

FEBS Letters, EarlyView.
MicroRNAs are emerging as crucial regulators at the intersection of metabolism and immunity. This review examines how miRNAs coordinate glucose and lipid metabolism while simultaneously modulating T‐cell development and immune responses. Moreover, it highlights how cutting‐edge artificial intelligence applications can identify miRNA biomarkers ...
Stefania Oliveto, Nicola Manfrini, Stefano Biffo   +2 more
wiley   +1 more source

Comparing the Folds of Prions and Other Pathogenic Amyloids

Pathogens, 2018
Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt–Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-
José Miguel Flores-Fernández, Vineet Rathod, Holger Wille   +2 more
doaj   +1 more source

Sleep is bi-directionally modified by amyloid beta oligomers

eLife, 2020
Disrupted sleep is a major feature of Alzheimer’s disease (AD), often arising years before symptoms of cognitive decline. Prolonged wakefulness exacerbates the production of amyloid-beta (Aβ) species, a major driver of AD progression, suggesting that ...
Güliz Gürel Özcan, Sumi Lim, Patricia LA Leighton, W Ted Allison, Jason Rihel   +4 more
doaj   +1 more source

White-tailed deer S96 prion protein does not support stable in vitro propagation of most common CWD strains

Scientific Reports, 2021
PrPC variation at residue 96 (G/S) plays an important role in the epidemiology of chronic wasting disease (CWD) in exposed white-tailed deer populations.
Alicia Otero, Camilo Duque Velásquez, Judd Aiken, Debbie McKenzie   +3 more
doaj   +1 more source

FDserver: A web service for protein folding research [PDF]

, 2008
*Summary:* To facilitate the study of protein folding, we have developed a web service for protein folding rate and folding type prediction as well as for the calculation of a variety of topological parameters of protein structure, which is freely ...
Bin-Guang Ma, Hong-Yu Zhang, Ling-Ling Chen   +2 more
core   +1 more source

Protein folding mediated by solvation: water expelling and formation of the hydrophobic core occurs after the structure collapse

, 2002
The interplay between structure-search of the native structure and desolvation in protein folding has been explored using a minimalist model. These results support a folding mechanism where most of the structural formation of the protein is achieved ...
A. E. Garcia, Berg, Bryngelson, Burton, Clementi, Czaplewski, Dill, Eaton, Ferrenberg, Garc  a, Grantcharova, Gruebele, Hillson, Hummer, Hummer, J. N. Onuchic, Klimov, Leopold, M. S. Cheung, Martinez, Mart  nez, Mitsutake, Mok, Musacchio, Nymeyer, Nymeyer, Onuchic, Plaxco, Plotkin, Riddle, Roder, SCHERAGA, Shea, Shea, Sheinerman, Shoemaker, Sosnick, Zhang   +37 more
core   +2 more sources

Discrete molecular dynamics studies of the folding of a protein-like model [PDF]

, 1998
Background: Many attempts have been made to resolve in time the folding of model proteins in computer simulations. Different computational approaches have emerged.
Buldyrev, Sergey V., Dokholyan, Nikolay V., Shakhnovich, Eugene I., Stanley, H. Eugene   +3 more
core   +2 more sources