Results 31 to 40 of about 4,606,382 (149)
Molecular Therapy: Nucleic Acids, 2019 Accurate identification of intrinsically disordered proteins/regions (IDPs/IDRs) is critical for predicting protein structure and function. Previous studies have shown that IDRs of different lengths have different characteristics, and several ...
Yumeng Liu +3 more
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Intrinsically disordered proteins: modes of binding with emphasis on disordered domains
Open Biology, 2021 Our notions of protein function have long been determined by the protein structure–function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly ...
Owen Michael Morris +2 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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DMFpred: Predicting protein disorder molecular functions based on protein cubic language model.
PLoS Computational Biology, 2022 Intrinsically disordered proteins and regions (IDP/IDRs) are widespread in living organisms and perform various essential molecular functions. These functions are summarized as six general categories, including entropic chain, assembler, scavenger ...
Yihe Pang, Bin Liu
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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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Prediction of protein-protein interaction sites in intrinsically disordered proteins
Frontiers in Molecular Biosciences, 2022 Intrinsically disordered proteins (IDPs) participate in many biological processes by interacting with other proteins, including the regulation of transcription, translation, and the cell cycle.
Ranran Chen +10 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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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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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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