P185
Clamp loader ATPases and the evolution of DNA replication machinery.An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptorThe mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinasesStructural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOSInhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interfaceMechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segmentStructural analysis of autoinhibition in the Ras activator Son of sevenlessStructural basis for the recognition of c-Src by its inactivator CskConformational coupling across the plasma membrane in activation of the EGF receptorStructural analysis of autoinhibition in the Ras-specific exchange factor RasGRP1The tyrosine kinase Csk dimerizes through Its SH3 domainOncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerizationA conserved protonation-dependent switch controls drug binding in the Abl kinaseCrystal structure of a DNA polymerase sliding clamp from a Gram-positive bacterium.Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)Nucleotide-induced conformational changes in an isolated Escherichia coli DNA polymerase III clamp loader subunitStructural basis for the autoinhibition of c-Abl tyrosine kinaseCrystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase IITandem histone folds in the structure of the N-terminal segment of the ras activator Son of SevenlessCrystal structure of the chi:psi sub-assembly of the Escherichia coli DNA polymerase clamp-loader complexc-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penaltyStructural basis for the inhibition of tyrosine kinase activity of ZAP-70Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3Structure of a Sliding Clamp on DNAStructure of a small-molecule inhibitor of a DNA polymerase sliding clampActivation of tyrosine kinases by mutation of the gatekeeper threonineThe crystal structure of the catalytic domain of a eukaryotic guanylate cyclaseProbing the Function of Heme Distortion in the H-NOX FamilyTuning a Three-Component Reaction For Trapping Kinase Substrate ComplexesThe structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2)Comparative Analysis of Mutant Tyrosine Kinase Chemical Rescue † ‡Equally Potent Inhibition of c-Src and Abl by Compounds that Recognize Inactive Kinase ConformationsAnalysis of the role of PCNA-DNA contacts during clamp loadingRole of the histone domain in the autoinhibition and activation of the Ras activator Son of SevenlessIntersubunit capture of regulatory segments is a component of cooperative CaMKII activationStructural insights into the molecular mechanism of H-NOX activationModulating Heme Redox Potential through Protein-Induced Porphyrin DistortionA Mechanism for Tunable Autoinhibition in the Structure of a Human Ca2+/Calmodulin- Dependent Kinase II HoloenzymeTunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain
P50
Q21245381-0592D42A-9131-4420-98D0-8BE1E0AA2C79Q24293598-5A6626BC-5827-4203-BAFD-EB903A8D0E80Q24294888-29B02EEB-A74D-45E9-AB3A-57CFA481BEB1Q24296951-1DFDB416-70BD-4324-8206-01680040BC96Q24297384-CC2B2C11-916C-4D5D-B331-B79F93D86A75Q24301761-14841110-A769-4C83-A249-D5B57A2199D3Q24309071-7F6C982D-CF0E-4A53-8B0F-060BA048F4AEQ24309253-A8591618-2CCA-4B59-A041-95E3B2602597Q24311447-9D0AF2DD-9972-4C8A-9C39-75148BA72FFBQ24313122-1658A86F-4118-4228-9E55-2D52EA853A1AQ24313621-1017CC66-CE4B-4025-ACA2-423C3F280BDEQ24314372-652090F8-3F86-4EB8-9F20-70EA85D0DEF8Q24321210-2B9A0A91-F808-4959-B0BD-0B4C105A764CQ24657421-BF33AF91-E393-43C7-86FB-A9399017E027Q25257835-90C85457-07CB-4977-B8AC-E1D234963574Q27639449-29D89C08-A64E-4402-AEB8-E23746C222EAQ27640640-50BB1444-74A9-4FB0-9BB2-764C44E95A30Q27640773-B3F0B01E-6DF6-48DD-8577-03A1EE84E5C5Q27641331-3A6FAE0F-0174-4951-9564-CC594C67D12FQ27642703-2FDD4D29-0D73-45EB-AC0E-23CABAFAB1C8Q27642924-D2D4B9ED-F9BE-4AC1-9D91-08B728F0C1C5Q27644039-1218C8E4-6000-4595-AECD-9EA3D4D59679Q27644831-84BF4BE7-1158-4EF5-AE92-6D3058223CBFQ27646596-59737246-15EB-4818-BD24-783B8B93BEF0Q27649528-191CEEB1-3B62-43C6-8308-C3EF026FECFBQ27651408-222AA638-24B9-4492-B3F2-33BDD0868893Q27652166-E67295C0-F21D-435E-B84D-7905ACFDA2AAQ27652454-FFB0A989-9A83-47AA-86ED-D6BA1240EDD1Q27652988-8D95B8D4-49FD-491F-88BC-AF483F2B0092Q27653046-4BBD4F7A-4AB4-4FC4-A509-29F6CDF506B1Q27653890-C8064C01-05FA-4CF1-B91F-4C21669B7D9BQ27654012-7A1743F6-B0F8-44BE-B324-587D329EA9D1Q27654059-464CA353-3DF6-4697-8597-B32242709787Q27659293-B9C2B208-D9C4-4D53-8140-92A118882C3CQ27659565-7A604C08-3116-4650-9544-C1195E53781EQ27659633-04BE5F22-380D-4025-8E37-56B25D5ADFCEQ27659887-E27E14A3-4BDF-4DC2-A608-A54FB4148B97Q27664148-61394464-C685-47CA-BDE8-638444FF689FQ27672798-F4972B80-6525-403E-9AED-628CC580C53EQ27675023-834B8311-3C0D-4B26-8E10-B74EE56772F9
P50
description
American biochemist
@en
US-amerikanischer Chemiker und Molekularbiologe
@de
amerikansk biokemiker
@da
biochemicus
@nl
biocimiciste american
@lfn
usona biokemiisto
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name
John Kuriyan
@af
John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
@da
type
label
John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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John Kuriyan
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prefLabel
John Kuriyan
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John Kuriyan
@an
John Kuriyan
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John Kuriyan
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John Kuriyan
@br
John Kuriyan
@ca
John Kuriyan
@co
John Kuriyan
@cs
John Kuriyan
@cy
John Kuriyan
@da
P463
P1015
P214
P244
P269
P646
P1015
P1153
7006724588
P1412
P184
P2002
johnkuriyan
P2070
john-kuriyan-11776