Results 31 to 40 of about 23,829 (240)
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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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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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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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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Unequivocal single-molecule force spectroscopy of intrinsically disordered proteins [PDF]
, 2012 Intrinsically disordered proteins (IDPs) are predicted to represent about one third of the eukaryotic proteome. The dynamic ensemble of conformations of this steadily growing class of proteins has remained hardly accessible for bulk biophysical ...
Rubén Hervás +8 more
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Nature Communications, 2021 Mapping free energy landscapes of complex multi-funneled metamorphic proteins and weakly-funneled intrinsically disordered proteins (IDPs) remains challenging.
Rajeswari Appadurai +2 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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BMC Bioinformatics, 2017 Background Intrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and other genomes,
Jia-Feng Yu +8 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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Briefings in Bioinformatics, 2023 Abstract The biological function of proteins is determined not only by their static structures but also by the dynamic properties of their conformational ensembles. Numerous high-accuracy static structure prediction tools have been recently developed based on deep learning; however, there remains a lack of efficient and accurate methods ...
Junjie Zhu +6 more
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