about
CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signalingTECPR2 Cooperates with LC3C to Regulate COPII-Dependent ER ExportCircularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.Peak picking NMR spectral data using non-negative matrix factorization.Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy.Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and UfmylationStructural and functional analysis of the GABARAP interaction motif (GIM).Fluorescence-based ATG8 sensors monitor localization and function of LC3/GABARAP proteins.Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins.Ligand binding to 2΄-deoxyguanosine sensing riboswitch in metabolic context.Structure and Biophysical Characterization of the S-Adenosylmethionine-dependent O-Methyltransferase PaMTH1, a Putative Enzyme Accumulating during Senescence of Podospora anserinaFast automated NMR spectroscopy of short-lived biological samples.Assignments of 1H, 15N and 13C resonances of the proline-rich matrix protein of Moloney murine leukemia virus (MA MoMuLV).Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains.Modulation of the Rcs-mediated signal transfer by conformational flexibility.A universal expression tag for structural and functional studies of proteins.Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues.Site-specific inhibition of the small ubiquitin-like modifier (SUMO)-conjugating enzyme Ubc9 selectively impairs SUMO chain formation.Methods for Studying Interactions Between Atg8/LC3/GABARAP and LIR-Containing Proteins.Reversible association of the equilibrium unfolding intermediate of lambda Cro repressor.Two-stage thermal unfolding of [Cys55]-substituted Cro repressor of bacteriophage lambda.Chain Assembly and Disassembly Processes Differently Affect the Conformational Space of Ubiquitin Chains.A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains.NMR assignment of 1H, 13C and 15N resonances of the truncated Escherichia coli RcsC (700-949), including the phosphoreceiver domain.Structural investigation of glycan recognition by the ERAD quality control lectin Yos9Conformational Switches Modulate Protein Interactions in Peptide Antibiotic SynthetasesCooperative thermal transitions of bovine and human apo-α-lactalbumins: evidence for a new intermediate stateHUWE1 E3 ligase promotes PINK1/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKαDomains in lambda Cro repressor. A calorimetric study[Calorimetric studies of the effect of amino acid replacements 16Gln-Leu and 26Tyr-Asp on the structural organization and stability of the Cro-repressor from phage lambda]Secondary structure and oligomerization behavior of equilibrium unfolding intermediates of the lambda cro repressorGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)Structural Characterization of the Interaction of the Fibroblast Growth Factor Receptor with a Small Molecule Allosteric InhibitorSelective autophagy maintains centrosome integrity and accurate mitosis by turnover of centriolar satellitesOxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin bindingAn atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5
P50
Q27697991-CA8D93C9-4860-406E-9B93-633EA61BC07FQ27702230-AC175B09-F509-44E5-87A6-569990EC041FQ30425613-57B7E076-086B-478F-BA8F-AEDDD1D96FBEQ30753425-C66442C0-DD35-487D-BA4D-43CC073C901AQ34399968-FDDC00F0-3EFF-4970-AA62-D8797E5170DDQ36884801-289CD04A-72F4-4A07-A32C-8232DDD4CD20Q38706191-E7A54971-4FD5-4654-A70E-8AF8DBCAAF2EQ38724062-365F6511-61A6-4327-81C0-238130BF9544Q38820046-24742C56-5437-42B6-ACA0-957C3C0E77DBQ41950923-EB173361-42B6-47BD-979C-E5D8338D5E28Q41952467-ACE8FB27-AD15-4432-BA38-AF4C6EBF2042Q44352036-7AAE8478-510D-48E6-90E8-5DC5A889A118Q44372467-9EFED2D3-7CFC-425A-BD46-6976E94CD306Q45100733-8E430EA1-881A-4612-BCE9-FAFC39711687Q46236403-B2B5A364-CB71-4088-B894-358A3698140EQ46637125-5CFFA87F-AB30-442F-AB79-85E739833530Q46741047-86483956-9A75-4BF8-995D-77EE93E1F0F8Q47822842-28F62D11-F2E1-4EC2-8B3A-906A04A0ADD6Q51114955-563AA6C6-011E-4856-98E2-5A3082937EA4Q52310514-5FE382F4-470C-4053-B45A-B463C410ECDBQ52481240-1B622995-C34E-4E99-83EB-357110E08D35Q52735350-86E3EEAF-B4CE-4036-BA15-5E610493A73BQ53596827-6613EA9B-A867-4434-AEEA-809771F905CFQ54453938-1A4066D4-313E-4156-A588-F69112FAE849Q57751763-B98BB04C-AF38-43CE-8B98-4B7CC49D4754Q57903771-FA98460A-4A2D-4651-BA97-7749C88C3162Q58322027-30D8DB6B-7E98-42A9-AD31-EC1134ADA309Q58740883-398137C1-B21A-4CD8-AE3A-CBD18583B4F2Q67974310-8E5CDC50-EFFC-43FE-A9CA-FD1954923318Q72903446-3AEBBC4E-4BD3-4C36-BE9B-24352C201645Q77374662-21C56BEB-026B-46C4-BDD6-DE0F1BE932ECQ87139132-65FE4D82-35D1-494E-B6D3-86F22A341146Q88362285-DBE6AD7F-7508-438E-979C-7662D0E447E8Q90100693-186F382D-378E-4AC2-90A6-F926251AE76FQ92641626-8B5001CC-07ED-43BB-8C0E-5C3E126468CCQ93124367-437F2C32-3434-4E56-AD7B-41A220872BC3
P50
description
Forscher
@de
chercheur
@fr
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
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研究者
@zh
name
Rogov VV
@ast
Rogov VV
@es
Rogov VV
@nl
Vladimir V. Rogov
@en
Wladimir Witaljewitsch Rogow
@de
Владимир Витальевич Рогов
@ru
type
label
Rogov VV
@ast
Rogov VV
@es
Rogov VV
@nl
Vladimir V. Rogov
@en
Wladimir Witaljewitsch Rogow
@de
Владимир Витальевич Рогов
@ru
altLabel
Rogov VV
@en
Wladimir Rogow
@de
prefLabel
Rogov VV
@ast
Rogov VV
@es
Rogov VV
@nl
Vladimir V. Rogov
@en
Wladimir Witaljewitsch Rogow
@de
Владимир Витальевич Рогов
@ru
P106
P21
P31
P496
0000-0002-2164-2323