Results 21 to 30 of about 7,902,914 (332)
Membranes, 2022 Intrinsically disordered proteins and protein regions (IDPs/IDPRs) are mainly involved in signaling pathways, where fast regulation, temporal interactions, promiscuous interactions, and assemblies of structurally diverse components including membranes ...
Hana Popelka, Vladimir N. Uversky
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AlphaFold2: A Role for Disordered Protein/Region Prediction?
International Journal of Molecular Sciences, 2022 The development of AlphaFold2 marked a paradigm-shift in the structural biology community. Herein, we assess the ability of AlphaFold2 to predict disordered regions against traditional sequence-based disorder predictors.
Carter J. Wilson, W. Choy, M. Karttunen
semanticscholar +1 more source
Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins
Biomolecules, 2020 Direct interaction between intrinsically disordered proteins (IDPs) is often difficult to characterize hampering the elucidation of their binding mechanism.
Maria Grazia Murrali +2 more
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Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions
Biomolecules, 2022 Intrinsically disordered regions (IDRs) carry out many cellular functions and vary in length and placement in protein sequences. This diversity leads to variations in the underlying compositional biases, which were demonstrated for the short vs. long IDRs. We analyze compositional biases across four classes of disorder: fully disordered proteins; short
Bi Zhao, Lukasz Kurgan
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Nature Communications, 2021 The SARS-CoV-2 nucleocapsid (N) protein binds the viral RNA genome and contains two ordered domains flanked by three intrinsically-disordered regions. Here, the authors show that RNA binding induces liquid-liquid phase separation of N, which is driven by
Shan Lu +8 more
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Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins [PDF]
Protein Science, 2019 AbstractPhosphorylation is a major post‐translational modification that plays a central role in signaling pathways. Protein kinases phosphorylate substrates (phosphoproteins) by adding phosphate at Ser/Thr or Tyr residues (phosphosites). A large amount of data identifying and describing phosphosites in phosphoproteins has been reported but the ...
Ryotaro Koike +3 more
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Analysis of structured and intrinsically disordered regions of transmembrane proteins [PDF]
Molecular BioSystems, 2009 Abstract Integral membraneproteins display two major types of transmembrane structure, helical bundles and beta barrels. The main functional roles of transmembrane proteins are the transport of small molecules and cellsignaling, and sometimes these two roles are coupled.
Xue, Bin +4 more
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Nucleic Acids Research, 2023 Mycobacteria are the major human pathogens with the capacity to become dormant persisters. Mycobacterial DNA-binding protein 1 (MDP1), an abundant histone-like protein in dormant mycobacteria, induces dormancy phenotypes, e.g.
Akihito Nishiyama +12 more
semanticscholar +1 more source
Entropy and Information within Intrinsically Disordered Protein Regions [PDF]
Entropy, 2019 Bioinformatics and biophysical studies of intrinsically disordered proteins and regions (IDRs) note the high entropy at individual sequence positions and in conformations sampled in solution. This prevents application of the canonical sequence-structure-function paradigm to IDRs and motivates the development of new methods to extract information from ...
Iva Pritisanac +3 more
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Intrinsically disordered regions in TRPV2 mediate protein-protein interactions
Communications Biology, 2023 AbstractTransient receptor potential (TRP) ion channels are gated by diverse intra- and extracellular stimuli leading to cation inflow (Na+, Ca2+) regulating many cellular processes and initiating organismic somatosensation. Structures of most TRP channels have been solved.
Sanganna Gari, Raghavendar +6 more
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