Results 41 to 50 of about 66,315 (318)
Intrinsically Disordered Proteins: An Overview
International Journal of Molecular Sciences, 2022 Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states. Such intrinsically disordered proteins or protein segments are highly abundant across proteomes, and are involved in various effector functions.
Rakesh Trivedi +1 more
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mBio, 2020 A distinguishing morphological feature of all herpesviruses is the multiprotein tegument layer located between the nucleocapsid and lipid envelope of the virion. Tegument proteins play multiple roles in viral replication, including viral assembly, but we
Claire M. Metrick +2 more
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Disordered proteins and network disorder in network descriptions of protein structure, dynamics and function. Hypotheses and a comprehensive review [PDF]
, 2011 During the last decade, network approaches became a powerful tool to describe protein structure and dynamics. Here we review the links between disordered proteins and the associated networks, and describe the consequences of local, mesoscopic and global ...
Daniel V. Veres +8 more
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Intrinsically disordered proteins and biomineralization [PDF]
Matrix Biology, 2016 In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners.
Adele L, Boskey +1 more
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MobiDB: intrinsically disordered proteins in 2021 [PDF]
Nucleic Acids Research, 2020 AbstractThe 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 and an improved update process.
Piovesan, Damiano +14 more
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Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Frontiers in Physics, 2019 Recognition of the natural abundance and functional importance of intrinsically disordered proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions (IDPRs) and ordered regions, is changing protein science.
Vladimir N. Uversky, Vladimir N. Uversky
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Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission [PDF]
, 2013 A novel coronavirus, MERS-CoV (NCoV, HCoV-EMC/2012), originating from the Middle-East, has been discovered. Incoming data reveal that the virus is highly virulent to humans.
Dunker, A. Keith +2 more
core +1 more source
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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Expose flexible conformations for intrinsically disordered protein
Current Research in Structural BiologyThe folding conformation of native protein has flexibility in different degrees, which may bring difficulty in presenting the structures, and also it causes complexity in understanding the relationship between structure and functions.
Jiaan Yang +8 more
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Evolutionarily conserved network properties of intrinsically disordered proteins. [PDF]
PLoS ONE, 2015 Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners.
Nivedita Rangarajan +2 more
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