Results 81 to 90 of about 23,829 (240)
npj Systems Biology and Applications, 2023 Intrinsically disordered proteins (IDPs), which can interact with many partner proteins, are central to many physiological functions and to various pathologies that include neurodegeneration. Here, we introduce the Sherpa hypothesis, according to which a
Vic Norris +4 more
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Proceedings of the National Academy of Sciences of the United States of America, 2021 Significance Cells may compartmentalize proteins via a demixing process known as liquid–liquid phase separation (LLPS), which is often driven by intrinsically disordered proteins (IDPs) and regions.
G. Tesei +3 more
semanticscholar +1 more source
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
core
Toward a consensus in protein structure nomenclature
, 2019 In a recent article, published in Intrinsically Disordered Proteins, a valuable consensus view regarding the nomenclature for disordered proteins was presented.1 In this work the authors present a thoughtful and systemic review of terms that have been ...
DaSilva, Linder C +2 more
core +1 more source
Circuit Topology Approach for the Comparative Analysis of Intrinsically Disordered Proteins
Journal of Chemical Information and Modeling, 2023 Intrinsically disordered proteins (IDPs) lack a stable native conformation, making it challenging to characterize their structure and dynamics. Key topological motifs with fundamental biological relevance are often hidden in the conformational noise ...
Barbara Scalvini +5 more
semanticscholar +1 more source
Intrinsically Disordered Side of the Zika Virus Proteome
Frontiers in Cellular and Infection Microbiology, 2016 Over the last few decades, concepts of protein intrinsic disorder have been implicated in different biological processes. Recent studies have suggested that intrinsically disordered proteins (IDPs) provide structural plasticity and functional diversity ...
Rajanish Giri +3 more
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Portability of a Small-Molecule Binding Site between Disordered Proteins
Biomolecules, 2022 Intrinsically disordered proteins (IDPs) are important in both normal and disease states. Small molecules can be targeted to disordered regions, but we currently have only a limited understanding of the nature of small-molecule binding sites in IDPs ...
Rajesh Jaiprashad +4 more
doaj +1 more source
Diversity of hydrodynamic radii of intrinsically disordered proteins
bioRxiv, 2023 Intrinsically disordered proteins (IDPs) form an important class of biomolecules regulating biological processes in higher organisms. The lack of a fixed spatial structure facilitates them to perform their regulatory functions and allows the efficiency ...
Michał K. Białobrzewski +5 more
semanticscholar +1 more source
The function of intrinsically disordered selenoproteins
, 2023 Rozovsky, SharonSELENOS and SELENOK are intrinsically disordered selenoproteins that take part in the endoplasmic-reticulum-associated degradation (ERAD) pathway, which degrades misfolded proteins and maintains cellular protein hemostasis.
Cheng, Rujin
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SPEADI: Accelerated Analysis of IDP-Ion Interactions from MD-Trajectories
Biology, 2023 The disordered nature of Intrinsically Disordered Proteins (IDPs) makes their structural ensembles particularly susceptible to changes in chemical environmental conditions, often leading to an alteration of their normal functions.
Emile de Bruyn +3 more
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