Results 11 to 20 of about 3,579,241 (217)
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.
Yihe Pang, Bin Liu
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Creating and Exploiting the Intrinsically Disordered Protein Knowledge Graph (IDP-KG). [PDF]
, 2022 There are many data sources containing overlapping information about Intrinsically Disordered Proteins (IDP). IDPcentral aims to be a registry to aid the discovery of data about proteins known to be intrinsically disordered by aggregating the content from these sources. Traditional ETL approaches for populating IDPcentral require the API and data model
Gray, Alasdair +4 more
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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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Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family. [PDF]
PLoS Computational Biology, 2013 Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Jianhui Song +4 more
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Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]
, 2009 Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
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Intrinsically disordered proteins (IDPs) in trypanosomatids [PDF]
BMC Genomics, 2014 Proteins are composed of one or more amino acid chains and exhibit several structure levels. IDPs (intrinsically disordered proteins) represent a class of proteins that do not fold into any particular conformation and exist as dynamic ensembles in their native state.
Ruy, Patrícia +5 more
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Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
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Structural Analysis of Intrinsically Disordered Protein (IDP): TRIOBP [PDF]
Biophysical Journal, 2014 TRIOBP is an actin-bundling protein. Mutations of TRIOBP are associated with human deafness DFNB28. TRIOBP has three isoforms, named TRIOBP-1, TRIOBP-4, and TRIOBP-5. In vitro, TRIOBP isoform 4 (TRIOBP-4) forms dense F-actin bundles resembling the inner ear hair cell rootlet structure.
Gunther, Laura K. +4 more
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Unraveling the Thermodynamics of Ultra-tight Binding of Intrinsically Disordered Proteins
Frontiers in Molecular Biosciences, 2021 Protein interactions mediated by the intrinsically disordered proteins (IDPs) are generally associated with lower affinities compared to those between globular proteins.
Uroš Zavrtanik, San Hadži, Jurij Lah
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Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs) [PDF]
International Journal of Molecular Sciences, 2011 Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as tumor, Parkinson disease, Alzheimer disease, diabetes, and so on.
Jihua Wang +3 more
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