Results 1 to 10 of about 448,472 (368)
Intrinsically Disordered Proteins: An Overview. [PDF]
Int J Mol Sci, 2022 Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states.
Trivedi R, Nagarajaram HA.
europepmc +4 more sources
DisProt in 2024: improving function annotation of intrinsically disordered proteins. [PDF]
Nucleic Acids Res, 2023 DisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions.
Aspromonte MC +6 more
europepmc +2 more sources
Protein flexibility and intrinsic disorder [PDF]
Protein Science, 2003 AbstractComparisons were made among four categories of protein flexibility: (1) low‐B‐factor ordered regions, (2) high‐B‐factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high‐B‐factor ordered and short ...
Predrag Radivojac +7 more
openalex +6 more sources
Biophysical Reviews, 2022 Many different intrinsically disordered proteins and proteins with intrinsically disordered regions are associated with neurodegenerative diseases. These types of proteins including amyloid-β, tau, α-synuclein, CHCHD2, CHCHD10, and G-protein coupled receptors are increasingly becoming evaluated as potential drug targets in the pharmaceutical-based ...
Orkid Coskuner-Weber +2 more
semanticscholar +5 more sources
Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins [PDF]
arXiv, 2021 Intrinsically disordered proteins (IDPs) and multidomain proteins with flexible linkers show a high level of structural heterogeneity and are best described by ensembles consisting of multiple conformations with associated thermodynamic weights.
F. E. Thomasen, K. Lindorff-Larsen
arxiv +3 more sources
MobiDB: 10 years of intrinsically disordered proteins. [PDF]
Nucleic Acids Res, 2023 The MobiDB database (URL: https://mobidb.org/) is a knowledge base of intrinsically disordered proteins. MobiDB aggregates disorder annotations derived from the literature and from experimental evidence along with predictions for all known protein ...
Piovesan D +9 more
europepmc +2 more sources
MobiDB: intrinsically disordered proteins in 2021 [PDF]
Nucleic Acids Research, 2020 The MobiDB database (URL: https://mobidb.org/) provides predictions and annotations for intrinsically disordered proteins. Here, we report recent developments implemented in MobiDB version 4, regarding the database format, with novel types of annotations
Damiano Piovesan +14 more
semanticscholar +9 more sources
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
doaj +2 more sources
Intrinsically disordered proteins play diverse roles in cell signaling
Cell Communication and Signaling, 2022 Signaling pathways allow cells to detect and respond to a wide variety of chemical (e.g. Ca2+ or chemokine proteins) and physical stimuli (e.g., sheer stress, light).
Sarah E. Bondos +2 more
doaj +2 more sources
Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders [PDF]
Frontiers in Aging Neuroscience, 2015 The recent years have witnessed a rise in the number of intrinsically disordered proteins (IDPs), also known as hybrid proteins, which possess both structured domains and biologically important intrinsically disordered protein regions (IDPRs). These proteins challenge the “one sequence—one structure—one function” concept by demonstrating that the lack ...
Vladimir N. Uversky +3 more
doaj +5 more sources