DisBind: A database of classified functional binding sites in disordered and structured regions of intrinsically disordered proteins [PDF]
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 ...
Wang, Ji-Hua +17 more
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Proteome-wide signatures of function in highly diverged intrinsically disordered regions.
eLife, 2019 Intrinsically disordered regions make up a large part of the proteome, but the sequence-to-function relationship in these regions is poorly understood, in part because the primary amino acid sequences of these regions are poorly conserved in alignments ...
Bob Strome +11 more
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Functions of Intrinsically Disordered Regions. [PDF]
Biology (Basel)Intrinsically disordered regions (IDRs), defined as protein segments lacking stable tertiary structures, are ubiquitously present in the human proteome and enriched with disease-associated mutations. IDRs harbor molecular recognition features (MoRFs) and
Xiao L, Xia K.
europepmc +2 more sources
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 +6 more sources
Decoding intrinsically disordered regions in biomolecular condensates. [PDF]
Fundam ResBiomolecular condensates comprise a diverse array of molecular entities, with intrinsically disordered regions (IDRs) receiving mounting attention due to their pivotal roles. In recent years, significant progress has been made in understanding the linear
Shi M, Wu Z, Zhang Y, Li T.
europepmc +2 more sources
The Origin of Discrepancies between Predictions and Annotations in Intrinsically Disordered Proteins
Biomolecules, 2023 Disorder prediction methods that can discriminate between ordered and disordered regions have contributed fundamentally to our understanding of the properties and prevalence of intrinsically disordered proteins (IDPs) in proteomes as well as their ...
Mátyás Pajkos +2 more
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Prediction of folding patterns for intrinsic disordered protein
Scientific Reports, 2023 The conformation flexibility of natural protein causes both complexity and difficulty to understand the relationship between structure and function. The prediction of intrinsically disordered protein primarily is focusing on to disclose the regions with ...
Jiaan Yang +4 more
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Epichromatin and chromomeres: a ‘fuzzy’ perspective [PDF]
Open Biology, 2018 ‘Epichromatin’, the surface of chromatin beneath the interphase nuclear envelope (NE) or at the surface of mitotic chromosomes, was discovered by immunostaining with a specific bivalent mouse monoclonal anti-nucleosome antibody (mAb PL2-6). ‘Chromomeres’,
Donald E. Olins, Ada L. Olins
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Evolutionary Study of Disorder in Protein Sequences
Biomolecules, 2020 Intrinsically disordered proteins (IDPs) contain regions lacking intrinsic globular structure (intrinsically disordered regions, IDRs). IDPs are present across the tree of life, with great variability of IDR type and frequency even between closely ...
Kristina Kastano +6 more
doaj +1 more source
Intrinsically disordered regions in TRPV2 mediate protein-protein interactions
Communications Biology, 2023 Transient 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.
Raghavendar R. Sanganna Gari +6 more
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