Results 31 to 40 of about 23,171 (195)
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 ...
openaire +3 more sources
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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A Site-Aware Representation Learning Framework For Unified Molecular Interaction Modeling and Generative Design. [PDF]
Adv Sci (Weinh)MolDBG is a site‐aware, sequence‐only framework that unifies drug‐target affinity prediction, binding‐site identification, and affinity‐conditioned molecular generation for structured proteins. Guided by multi‐task binding‐site supervision, it aligns interaction‐critical residues before learning drug‐target representations and simultaneously infers ...
Luo G +6 more
europepmc +2 more sources
Frontiers in Molecular Biosciences, 2015 Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles.
Gabriel eThieulin-Pardo +3 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
openaire +2 more sources
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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CARs-DB: A Database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins
Frontiers in Molecular Biosciences, 2022 Proteome-wide analyses suggest that most globular proteins contain at least one amyloidogenic region, whereas these aggregation-prone segments are thought to be underrepresented in intrinsically disordered proteins (IDPs).
Carlos Pintado-Grima +7 more
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Intrinsically disordered proteins: controlled chaos or random walk
International Journal of Plant Biology, 2016 Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins.
T.C. Howton +3 more
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A novel mode of interaction between intrinsically disordered proteins
Biophysics and Physicobiology, 2020 An increasing number of proteins, which have neither regular secondary nor well-defined tertiary structures, have been found to be present in cells. The structure of these proteins is highly flexible and disordered under physiological (native) conditions,
Emi Hibino, Masaru Hoshino
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