Results 31 to 40 of about 3,579,241 (217)
iScience, 2022 Summary: Yes-associated protein (YAP) is a partly intrinsically disordered protein (IDP) that plays a major role as the downstream element of the Hippo pathway.
Michael Feichtinger +6 more
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Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs [PDF]
Intrinsically Disordered Proteins, 2014 This review opens a new series entitled "Unreported intrinsic disorder in proteins." The goal of this series is to bring attention of researchers to an interesting phenomenon of missed (or overlooked, or ignored, or unreported) disorder. This series serves as a companion to "Digested Disorder" which provides a quarterly review of papers on ...
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Modeling disordered protein interactions from biophysical principles.
PLoS Computational Biology, 2017 Disordered protein-protein interactions (PPIs), those involving a folded protein and an intrinsically disordered protein (IDP), are prevalent in the cell, including important signaling and regulatory pathways.
Lenna X Peterson +4 more
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Structural characterization of intrinsically disordered proteins by NMR spectroscopy. [PDF]
, 2013 Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and ...
Contreras-Martos, Sara +7 more
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PhosIDP: a web tool to visualize the location of phosphorylation sites in disordered regions
Scientific Reports, 2021 Charge is a key determinant of intrinsically disordered protein (IDP) and intrinsically disordered region (IDR) properties. IDPs and IDRs are enriched in sites of phosphorylation, which alters charge.
Sonia T. Nicolaou +4 more
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RFPR-IDP: reduce the false positive rates for intrinsically disordered protein and region prediction by incorporating both fully ordered proteins and disordered proteins [PDF]
Briefings in Bioinformatics, 2020 AbstractAs an important type of proteins, intrinsically disordered proteins/regions (IDPs/IDRs) are related to many crucial biological functions. Accurate prediction of IDPs/IDRs is beneficial to the prediction of protein structures and functions. Most of the existing methods ignore the fully ordered proteins without IDRs during training and test ...
Yumeng Liu, Xiaolong Wang, Bin Liu
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Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins
Biomolecules, 2019 Intrinsically disordered proteins (IDP) are abundant in the human genome and have recently emerged as major therapeutic targets for various diseases. Unlike traditional proteins that adopt a definitive structure, IDPs in free solution are disordered and ...
Supriyo Bhattacharya, Xingcheng Lin
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The IDP-Specific Force Field ff14IDPSFF Improves the Conformer Sampling of Intrinsically Disordered Proteins [PDF]
Journal of Chemical Information and Modeling, 2017 Intrinsically disordered proteins (IDPs) or intrinsically disordered regions do not have a fixed tertiary structure but play key roles in signal regulation, molecule recognition, and drug targeting. However, it is difficult to study the structure and function of IDPs by traditional experimental methods because of their diverse conformations ...
Dong Song, Ray Luo 0001, Hai-Feng Chen
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Scientific Reports, 2017 Intrinsically disordaered proteins (IDPs) are a prevalent phenomenon with over 30% of human proteins estimated to have long disordered regions. Computational methods are widely used to study IDPs, however, nearly all treat disorder in a binary fashion ...
Tomasz Kosciolek +2 more
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Evolutionarily conserved network properties of intrinsically disordered proteins. [PDF]
PLoS ONE, 2015 Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners.
Nivedita Rangarajan +2 more
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