About: Intrinsic protein disorder in complete genomes

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scientific article published on 01 January 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im Johr 2000 veröffentlicht worden isch (gsw) наукова стаття, опублікована в січні 2000 (uk) article scientifique publié en 2000 (fr) im Januar 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 2000 (ast) artikull shkencor i botuar më 01 janar 2000 (sq) scientific article published on 01 January 2000 (en)
publication date	wds:Q77145749-5C825B44-C612-4265-BE6D-F69B05379C97
publication date	2000-01-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q77145749-1AA4F017-1E4E-4D2F-81BD-C323622A80C9 wds:Q77145749-31507CD8-7792-4557-88AB-98C591BEC4F3 wds:Q77145749-5AFE6CC3-79F6-4E35-B261-58533E0EBB56 wds:Q77145749-BC4C2959-0B3D-4904-9160-E508CBFF9439
author name string	P Romero C J Brown A K Dunker Z Obradovic
rdfs:label	Intrinsic protein disorder in complete genomes (en) Intrinsic protein disorder in complete genomes (nl)
skos:prefLabel	Intrinsic protein disorder in complete genomes (en) Intrinsic protein disorder in complete genomes (nl)
name	Intrinsic protein disorder in complete genomes (en) Intrinsic protein disorder in complete genomes (nl)
author	wds:Q77145749-9C62199E-8734-4614-A028-AB2BD3FEE8AF
author	Ethan C Garner
title	wds:Q77145749-3E275B6F-278C-4304-A374-3A69E733A270
title	Intrinsic protein disorder in complete genomes (en)
page(s)	wds:Q77145749-9826C43C-E56D-4D00-92F9-D113ABA6E3F5
page(s)	161-171
instance of	wds:Q77145749-73650402-9388-4B3A-91B4-C7298579DF2F
instance of	scholarly article
PubMed ID	wds:Q77145749-4C507FC1-81CC-467F-90B9-87F56BE58751
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11700597
PubMed ID	11700597
volume	wds:Q77145749-C22598BE-D014-408E-B407-CC804FBB4CB4
volume	11
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q77145749
is cites work of	The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils Structural characterization of an intrinsically unfolded mini-HBX protein from hepatitis B virus CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices The evolution of protein structures and structural ensembles under functional constraint. Toward a quantitative theory of intrinsically disordered proteins and their function Selection on protein structure, interaction, and sequence. Natively unfolded domains in endocytosis: hooks, lines and linkers. Inferring function using patterns of native disorder in proteins Archaic chaos: intrinsically disordered proteins in Archaea Evolution and disorder Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress Distribution and cluster analysis of predicted intrinsically disordered protein Pfam domains The unfoldomics decade: an update on intrinsically disordered proteins. The role of intrinsically unstructured proteins in neurodegenerative diseases Understanding protein non-folding. Malleable machines take shape in eukaryotic transcriptional regulation Expanding the proteome: disordered and alternatively folded proteins Nanoimaging for protein misfolding and related diseases The N-terminal intrinsically disordered domain of Mgm101p is localized to the mitochondrial nucleoid PONDR-FIT: a meta-predictor of intrinsically disordered amino acids Intrinsic disorder in the human spliceosomal proteome Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes Structural disorder promotes assembly of protein complexes Intrinsic disorder in scaffold proteins: getting more from less Characterization of molecular recognition features, MoRFs, and their binding partners Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins The Tail That Wags the Dog: How the Disordered C-Terminal Domain Controls the Transcriptional Activities of the p53 Tumor-Suppressor Protein. At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillation Disorder predictors also predict backbone dynamics for a family of disordered proteins Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation What macromolecular crowding can do to a protein Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions Low-complexity regions within protein sequences have position-dependent roles MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins Experimental parameterization of an energy function for the simulation of unfolded proteins Comprehensive repertoire of foldable regions within whole genomes Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum Concept Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment Unfoldomics of human diseases: linking protein intrinsic disorder with diseases Test and Evaluation of ff99IDPs Force Field for Intrinsically Disordered Proteins The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. Coupled folding and binding of the disordered protein PUMA does not require particular residual structure Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein. The cytoplasmic domain of the T-cell receptor zeta subunit does not form disordered dimers Conformational recognition of an intrinsically disordered protein. Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function Intrinsically disordered regions of p53 family are highly diversified in evolution Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome Protein disorder in the human diseasome: unfoldomics of human genetic diseases In-silico prediction of disorder content using hybrid sequence representation CSpritz: accurate prediction of protein disorder segments with annotation for homology, secondary structure and linear motifs Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases Disease mutations in disordered regions--exception to the rule?

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