Results 21 to 30 of about 1,811,289 (287)
Generating Ensembles of Dynamic Misfolding Proteins
Frontiers in Neuroscience, 2022 The early stages of protein misfolding and aggregation involve disordered and partially folded protein conformers that contain a high degree of dynamic disorder.
Theodoros K. Karamanos +2 more
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Comparative evaluation of AlphaFold2 and disorder predictors for prediction of intrinsic disorder, disorder content and fully disordered proteins [PDF]
Computational and Structural Biotechnology Journal, 2023 Lukasz Kurgan +2 more
exaly +2 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
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Introducing Protein Intrinsic Disorder [PDF]
Chemical Reviews, 2014 Central to this model is the notion that the correct shape of the substrate can fit into the active site of the enzyme for enabling an efficient and specific catalysis, as observed for enzymes that hydrolyze β-but not α-glycosidic bonds. 1 Throughout the 20 th century, tens of thousands of structures have been solved and deposited in the Protein Data ...
Habchi, Johnny +3 more
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Biomolecules, 2020 Viral BCL2 proteins (vBCL2s) help to sustain chronic infection of host proteins to inhibit apoptosis and autophagy. However, details of conformational changes in vBCL2s that enable binding to BH3Ds remain unknown.
Arvind Ramanathan +4 more
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NMR illuminates intrinsic disorder. [PDF]
Curr Opin Struct Biol, 2021 Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This method continues to offer rich insights into the nature of IDPs in solution, especially in combination with other biophysical methods such as small-angle scattering, single ...
Dyson HJ, Wright PE.
europepmc +3 more sources
CAID prediction portal: a comprehensive service for predicting intrinsic disorder and binding regions in proteins. [PDF]
Nucleic Acids Res, 2023 Intrinsic disorder (ID) in proteins is well-established in structural biology, with increasing evidence for its involvement in essential biological processes.
Del Conte A +7 more
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Protein flexibility and intrinsic disorder [PDF]
Protein Science, 2004 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 ...
Radivojac, P. +7 more
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Databases for intrinsically disordered proteins [PDF]
Acta Crystallographica Section D Structural Biology, 2022 Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature.
Piovesan, Damiano +3 more
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IndiSPENsable for X Chromosome Inactivation and Gene Silencing
Epigenomes, 2023 For about 30 years, SPEN has been the subject of research in many different fields due to its variety of functions and its conservation throughout a wide spectrum of species, like worms, arthropods, and vertebrates.
Corinne Kaufmann, Anton Wutz
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