Results 61 to 70 of about 6,845,089 (390)
Chaos of protein folding [PDF]
The 2011 International Joint Conference on Neural Networks, 2011 As protein folding is a NP-complete problem, artificial intelligence tools like neural networks and genetic algorithms are used to attempt to predict the 3D shape of an amino acids sequence. Underlying these attempts, it is supposed that this folding process is predictable.
Jacques M. Bahi +2 more
openaire +3 more sources
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 +2 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 +2 more
core +1 more source
Purification tags markedly affect self‐aggregation of CPEB3
FEBS Letters, EarlyView.Although recombinant proteins are used to study protein aggregation in vitro, uncleaved tags can interfere with accurate interpretation. Our findings demonstrate that His₆‐GFP and His₁₂ tags significantly affect liquid droplet and amyloid fibril formation in the intrinsically disordered region (IDR) of mouse cytoplasmic polyadenylation element‐binding ...
Harunobu Saito +6 more
wiley +1 more source
Cellular Biology of Tau Diversity and Pathogenic Conformers
Frontiers in Neurology, 2020 Tau accumulation is a prominent feature in a variety of neurodegenerative disorders and remarkable effort has been expended working out the biochemistry and cell biology of this cytoplasmic protein.
Sang-Gyun Kang +5 more
doaj +1 more source
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 +3 more
doaj +1 more source
Protein folding tames chaos [PDF]
, 2013 Protein folding produces characteristic and functional three-dimensional structures from unfolded polypeptides or disordered coils. The emergence of extraordinary complexity in the protein folding process poses astonishing challenges to theoretical ...
Wei, Guo-Wei, Xia, Kelin
core
FEBS Letters, EarlyView.This study reveals how prime editing guide RNA (pegRNA) secondary structure and reverse transcriptase template length affect prime editing efficiency in correcting the phospholamban R14del cardiomyopathy‐associated mutation. Insights support the design of structurally optimized enhanced pegRNAs for precise gene therapy.
Bing Yao +7 more
wiley +1 more source
Funnels, pathways, and the energy landscape of protein folding: A synthesis [PDF]
Proteins: Structure, Function, and Bioinformatics, 1994 The understanding, and even the description of protein folding is impeded by the complexity of the process. Much of this complexity can be described and understood by taking a statistical approach to the energetics of protein conformation, that is, to ...
J. Bryngelson +3 more
semanticscholar +1 more source
Bioactive Materials, 2021 Evidence suggests that increased level/aggregation of beta-amyloid (Aβ) peptides initiate neurodegeneration and subsequent development of Alzheimer's disease (AD). At present, there is no effective treatment for AD. In this study, we reported the effects
Bibin G. Anand +6 more
doaj