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Oligomerization enables the selective targeting of intrinsically disordered regions by small molecules

open access: yes
Bielskutė S   +13 more
europepmc   +1 more source

Intrinsically Disordered Proteins and Proteins With Intrinsically Disordered Regions in Neurodegenerative Diseases [PDF]

open access: yesBiophysical 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 ...
Orkide Coşkuner-Weber, Vladimir Uversky
exaly   +6 more sources

Introduction to Intrinsically Disordered Proteins and Regions

open access: yesIntrinsically Disordered Proteins, 2019
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are fascinating dynamic conformational ensembles that are observed under physiological conditions.
Alan Keith Dunker   +2 more
exaly   +4 more sources

Classification of Intrinsically Disordered Regions and Proteins

open access: yesChemical Reviews, 2014
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Benjamin Lang   +2 more
exaly   +6 more sources

Intrinsically Disordered Proteins: An Overview

open access: yesInternational 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.
Hampapathalu A Nagarajaram   +1 more
exaly   +2 more sources
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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Annual Review of Biochemistry, 2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between ...
Christopher J, Oldfield, A Keith, Dunker
openaire   +2 more sources

Functional Roles of Transiently and Intrinsically Disordered Regions Within Proteins

open access: yesFEBS Journal, 2015
Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well-folded structures.
Vladimir Uversky
exaly   +2 more sources

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