Results 21 to 30 of about 1,763,945 (204)
IDP-LM: Prediction of protein intrinsic disorder and disorder functions based on language models
PLOS Computational Biology, 2023 Intrinsically disordered proteins (IDPs) and regions (IDRs) are a class of functionally important proteins and regions that lack stable three-dimensional structures under the native physiologic conditions. They participate in critical biological processes and thus are associated with the pathogenesis of many severe human diseases.
Yihe Pang, Bin Liu
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AWSEM-IDP: A Coarse-Grained Force Field for Intrinsically Disordered Proteins [PDF]
The Journal of Physical Chemistry B, 2018 The associative memory, water-mediated, structure and energy model (AWSEM) has been successfully used to study protein folding, binding, and aggregation problems. In this work, we introduce AWSEM-IDP, a new AWSEM branch for simulating intrinsically disordered proteins (IDPs), where the weights of the potentials determining secondary structure formation
Hao Wu +2 more
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Communications Biology, 2023 Intrinsically disordered proteins (IDPs) are comprised of significant numbers of residues that form neither helix, sheet, nor any other canonical type of secondary structure.
Andrew J. Miles +2 more
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How multisite phosphorylation impacts the conformations of intrinsically disordered proteins.
PLoS Computational Biology, 2021 Phosphorylation of intrinsically disordered proteins (IDPs) can produce changes in structural and dynamical properties and thereby mediate critical biological functions.
Fan Jin, Frauke Gräter
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The Amazing World of IDPs in Human Diseases II
Biomolecules, 2022 Intrinsically Disordered Proteins (IDPs) lack stable tertiary and secondary structures and are extensively distributed across eukaryotic cells, playing critical roles in cell signaling and regulation [...]
Simona Maria Monti +2 more
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Polycation-π Interactions Are a Driving Force for Molecular Recognition by an Intrinsically Disordered Oncoprotein Family [PDF]
, 2013 Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng +19 more
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Biophysical and Structural Study of Intrinsically Disordered Protein (IDP), Nopp140 [PDF]
Biophysical Journal, 2013 Human Nopp140 is a highly phosphorylated nucleolus protein and involved in the biogenesis of the nucleolus. It interacts with a variety of proteins related to the synthesis and assembly of the ribosome including a ubiquitous protein kinase CK2 which mediates cell growth and prevents apoptosis.
Na, Jung-Hyun +4 more
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Molecules, 2021 Intrinsically disordered proteins (IDPs) are critical players in the dynamic control of diverse cellular processes, and provide potential new drug targets because their dysregulation is closely related to many diseases.
Yusuke Hosoya, Junko Ohkanda
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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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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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