Intrinsically disordered proteins and intrinsically disordered protein regions
CJ Oldfield, AK Dunker - Annual review of biochemistry, 2014 - annualreviews.org
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 …
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …
The spliceosome: the ultimate RNA chaperone and sculptor
P Papasaikas, J Valcárcel - Trends in biochemical sciences, 2016 - cell.com
The spliceosome, one of the most complex machineries of eukaryotic cells, removes intronic
sequences from primary transcripts to generate functional messenger and long noncoding …
sequences from primary transcripts to generate functional messenger and long noncoding …
Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human
Diseases | Chemical Reviews ACS ACS Publications C&EN CAS Find my institution Log In …
Diseases | Chemical Reviews ACS ACS Publications C&EN CAS Find my institution Log In …
[HTML][HTML] Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates
VN Uversky, IM Kuznetsova, KK Turoverov… - FEBS letters, 2015 - Elsevier
Here, we hypothesize that intrinsically disordered proteins (IDPs) serve as important drivers
of the intracellular liquid–liquid phase separations that generate various membrane-less …
of the intracellular liquid–liquid phase separations that generate various membrane-less …
Disordered nucleiome: Abundance of intrinsic disorder in the DNA‐and RNA‐binding proteins in 1121 species from Eukaryota, Bacteria and Archaea
Intrinsically disordered proteins (IDPs) are abundant in various proteomes, where they play
numerous important roles and complement biological activities of ordered proteins. Among …
numerous important roles and complement biological activities of ordered proteins. Among …
Intrinsically disordered proteins link alternative splicing and post-translational modifications to complex cell signaling and reulation
Intrinsically disordered regions (IDRs) make up ca. 30% of the proteome of most eukaryotes,
and are involved in a diverse set of functions. Conventional sequence alignment tools …
and are involved in a diverse set of functions. Conventional sequence alignment tools …
Compartmentalization and functionality of nuclear disorder: intrinsic disorder and protein-protein interactions in intra-nuclear compartments
The cell nucleus contains a number of membrane-less organelles or intra-nuclear
compartments. These compartments are dynamic structures representing liquid-droplet …
compartments. These compartments are dynamic structures representing liquid-droplet …
Disordered proteinaceous machines
Many full-length proteins and protein regions lack stable tertiary and/or secondary structure
under physiological conditions in vitro. These proteins and regions, known as intrinsically …
under physiological conditions in vitro. These proteins and regions, known as intrinsically …
Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators
VN Uversky - Frontiers in Molecular Biosciences, 2014 - frontiersin.org
Biologically active proteins without stable tertiary structure are common in all known
proteomes. Functions of these intrinsically disordered proteins (IDPs) are typically related to …
proteomes. Functions of these intrinsically disordered proteins (IDPs) are typically related to …
Analyzing IDPs in interactomes
VN Uversky - Intrinsically Disordered Proteins: Methods and …, 2020 - Springer
Intrinsically disordered proteins (IDPs) and regions (IDRs) are commonly found in all
proteomes analyzed so far. These proteins/regions are subject to numerous …
proteomes analyzed so far. These proteins/regions are subject to numerous …