about
Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regionsDigested disorder: Quarterly intrinsic disorder digest (January/February/March, 2013).Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 ConceptClassification of intrinsically disordered regions and proteinsFunction and structure of inherently disordered proteinsFluorescent Proteins as Biomarkers and Biosensors: Throwing Color Lights on Molecular and Cellular ProcessesGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flavivirusesAlternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organismspE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteinsSPINE-D: accurate prediction of short and long disordered regions by a single neural-network based methodProtein tandem repeats - the more perfect, the less structuredDisProt: the Database of Disordered ProteinsWrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulatorsAn intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregationSolution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-"Bergeracs"Intrinsically Disordered Side of the Zika Virus ProteomeFunctional roles of transiently and intrinsically disordered regions within proteinsAnalysis of molecular recognition features (MoRFs)The PTEN Long N-tail is intrinsically disordered: increased viability for PTEN therapyPredictive Power Estimation Algorithm (PPEA)--a new algorithm to reduce overfitting for genomic biomarker discoveryCommon features at the start of the neurodegeneration cascadeMetal-controlled interdomain cooperativity in parvalbuminsEffects of HMGN variants on the cellular transcription profileDisordered proteinaceous machinesA decade and a half of protein intrinsic disorder: biology still waits for physicsFree cysteine modulates the conformation of human C/EBP homologous proteinIntrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stressDancing retro: solution structure and micelle interactions of the retro-SH3-domain, retro-SHH-'Bergerac'.Identifying novel cell cycle proteins in Apicomplexa parasites through co-expression decision analysisToward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species.Human alpha-fetoprotein as a Zn(2+)-binding protein. Tight cation binding is not accompanied by global changes in protein structure and stability.Biophysical constraints for protein structure prediction.Comparing and combining predictors of mostly disordered proteins.Flexible nets. The roles of intrinsic disorder in protein interaction networks.Effect of salt additives on protein partition in polyethylene glycol-sodium sulfate aqueous two-phase systems.The crowd you're in with: effects of different types of crowding agents on protein aggregation.Structural features important for differences in protein partitioning in aqueous dextran-polyethylene glycol two-phase systems of different ionic compositions.Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.
P50
Q21263144-625F8108-0026-4B63-9DEA-A36A8AAC453CQ22061724-4ABFD829-33B6-4153-8A0C-2BB19FDC0B49Q22061726-D12CFAC5-6DD5-4692-9AAF-C323DDE4EE43Q22061736-B16B466E-513A-43E4-984C-028A727ED568Q22061740-22399407-F24C-41ED-8F77-BE0EB2B3B933Q22241334-F5ED5E07-E38A-435F-9F59-142816CEFFC8Q22676705-E586D690-F4DB-45BB-812C-3A746A759661Q24289194-96C46AF5-E926-4285-B3BA-1CA6F94D48BBQ24548466-AEDBD616-5038-4509-BF08-485D855AE929Q24567790-6DAAAB1F-A201-4E25-8832-0DC76FD7131AQ24620741-5154AC51-EE3E-435E-B4D4-903259A7C46CQ24624818-49818DD5-9DE7-450E-A9AD-0F78C9462341Q24675789-74573D6B-E657-4FAE-9C43-7E60E49BFA1EQ27000495-347BFE43-9738-45DD-A4AE-8FD85B6E5BB2Q27312434-EBE2E9F6-53EA-48CB-938C-EBDFF93651C8Q27657339-2C54298B-EB49-44F1-B24D-D3EF444EA809Q27926249-9A13FF40-2606-437F-B2A2-FF435E5C6DEEQ28085662-B0E54096-5974-4F5C-9C01-AC684201C44AQ28260253-83E2CA1A-7A64-42AC-A085-250EEA62933AQ28299026-55ADC827-C452-4A32-AC06-BFD2B6FF2FC4Q28477085-7B28AD70-51BA-4958-9983-CFA8CE37253DQ28483979-795B0556-96DE-4C13-8037-8343406EE71DQ28577917-E743B07F-9EF4-4FAC-9566-1AB64311401CQ28594349-9C8900B3-3A4C-4C18-8C5D-702F8B242EB3Q28652765-56B1F309-3613-415E-9AD8-06B2C59F936BQ28681184-6F54EAD5-7058-45FC-9904-845B9D52F0D4Q28730747-A30331E0-CE75-4818-85AE-22EA3CF73788Q28910465-1B0617EE-87F8-4BDD-9F00-296ED6A17F29Q30009894-735CCD0D-B0C3-459A-A62E-DF5AE80135F3Q30039594-5D7305D6-2B31-4101-9F8C-56B93AC01ACCQ30153386-505D014A-7F06-4FA3-8A5B-8542E0EB36B4Q30329374-2F8B3345-9E5E-4227-926A-AAE8CA04E65CQ30332629-95ABB335-A40C-4E68-9E5E-6AE347F57D06Q30350136-F30A3433-16D5-4C07-9B42-D46454AB9F82Q30351593-23726053-644D-4128-9FCE-52F302A65D56Q30352637-897D5CED-6C2D-4D0D-B5F5-528FE7CD8074Q30355754-6DC39C87-6475-4818-8664-A542A92F2B84Q30358581-683D518C-1E85-4487-BA94-A998AB5D0F08Q30360720-DCEB8D7F-AF70-44C6-B6AF-AA9552A61BF1Q30360723-5946C2E5-5C67-4424-A4A9-E32FC050654F
P50
description
researcher ORCID ID = 0000-0002-4037-5857
@en
wetenschapper
@nl
name
Vladimir N Uversky
@ast
Vladimir N Uversky
@es
Vladimir N Uversky
@nl
Vladimir Uversky
@en
Wladimir Nikolajewitsch Uwerski
@de
Владимир Николаевич Уверский
@ru
type
label
Vladimir N Uversky
@ast
Vladimir N Uversky
@es
Vladimir N Uversky
@nl
Vladimir Uversky
@en
Wladimir Nikolajewitsch Uwerski
@de
Владимир Николаевич Уверский
@ru
altLabel
Uversky VN
@en
Vladimir N Uversky
@en
Wladimir Uwerski
@de
prefLabel
Vladimir N Uversky
@ast
Vladimir N Uversky
@es
Vladimir N Uversky
@nl
Vladimir Uversky
@en
Wladimir Nikolajewitsch Uwerski
@de
Владимир Николаевич Уверский
@ru
P1006
P214
P244
P1006
P106
P21
P214
P244
n2004121839
P31
P4012
P496
0000-0002-4037-5857
P5008
P569
1950-01-01T00:00:00Z
P7859
lccn-n2004121839