Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites
about
Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein responseCancer-associated loss-of-function mutations implicate DAPK3 as a tumor-suppressing kinaseInsights into the evolution of divergent nucleotide-binding mechanisms among pseudokinases revealed by crystal structures of human and mouse MLKLDecoding the phosphorylation code in Hedgehog signal transductionSmall-molecule inhibition and activation-loop trans-phosphorylation of the IGF1 receptorAuto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinaseTuning a Three-Component Reaction For Trapping Kinase Substrate ComplexesThe unfolded protein response signals through high-order assembly of Ire1Crystal structure of domain-swapped STE20 OSR1 kinase domainStructural Basis of Human p70 Ribosomal S6 Kinase-1 Regulation by Activation Loop PhosphorylationStructural Comparison of Human Mammalian Ste20-Like KinasesCrystal Structures of ABL-Related Gene (ABL2) in Complex with Imatinib, Tozasertib (VX-680), and a Type I Inhibitor of the Triazole Carbothioamide ClassCrystal Structure of Human Aurora B in Complex with INCENP and VX-680Characterization of Staphylococcus aureus EssB, an integral membrane component of the Type VII secretion system: atomic resolution crystal structure of the cytoplasmic segmentA Conserved Glu–Arg Salt Bridge Connects Coevolved Motifs That Define the Eukaryotic Protein Kinase FoldStructural Basis for the Regulation of Protein Kinase A by Activation Loop PhosphorylationStructures of Down Syndrome Kinases, DYRKs, Reveal Mechanisms of Kinase Activation and Substrate RecognitionMolecular basis of Tank-binding kinase 1 activation by transautophosphorylationStructure of cyclin G-associated kinase (GAK) trapped in different conformations using nanobodiesMolecular mechanism of Aurora A kinase autophosphorylation and its allosteric activation by TPX2Domain-Swapping Switch Point in Ste20 Protein Kinase SPAKDe Novo Fragment Design for Drug Discovery and Chemical BiologyGerminal-center kinase-like kinase co-crystal structure reveals a swapped activation loop and C-terminal extensionUnphosphorylated SR-like protein Npl3 stimulates RNA polymerase II elongation.The NDR/LATS family kinase Cbk1 directly controls transcriptional asymmetryRegulation of the Ste20-like kinase, SLK: involvement of activation segment phosphorylationSte20-like protein kinase SLK (LOSK) regulates microtubule organization by targeting dynactin to the centrosomeAutoactivation of transforming growth factor beta-activated kinase 1 is a sequential bimolecular processIdentifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinasesIdentification of human IKK-2 inhibitors of natural origin (part I): modeling of the IKK-2 kinase domain, virtual screening and activity assaysThe Ldb1 and Ldb2 transcriptional cofactors interact with the Ste20-like kinase SLK and regulate cell migrationInsights into protein kinase regulation and inhibition by large scale structural comparisonBiophysical characterization of recombinant proteins: a key to higher structural genomics successRegulation of Ste20-like kinase, SLK, activity: Dimerization and activation segment phosphorylation.Global consequences of activation loop phosphorylation on protein kinase A.Rational Redesign of a Functional Protein Kinase-Substrate Interaction.Bone morphogenetic protein-2 and -6 heterodimer illustrates the nature of ligand-receptor assemblyThe p38β mitogen-activated protein kinase possesses an intrinsic autophosphorylation activity, generated by a short region composed of the α-G helix and MAPK insert.Podocyte injury and albuminuria in mice with podocyte-specific overexpression of the Ste20-like kinase, SLK.Thr-370 is responsible for CDK11(p58) autophosphorylation, dimerization, and kinase activity.
P2860
0c30b190deebc1774dc11afb76d2f31b44566e9a2a3f55bb6ceb0af2ec86905c4b68aa53d38105b72e06275282b52f2a33d612ae6f54d98a83bf7686391b74a92ac3469314dce900eb15411587488acf3d9fcd427086146c79bfca10bc7e82a4ef23ff634cfd0c1d98d4b6d3c690774b015bf7c321b8169975d5e5526125a0873a2871cbb64d44c23d4460a28b6bd1091eeaacbcfb66052e95181550df5358e7b350d79ccac35f716fb83030b6ab76bd881a631dfab939bf6bb6c83dc32725a6d79e38d58d0d3951
P248
Q24292966-B980D746-3203-4D68-8ED1-2434B20DBB57Q24299650-AF08849E-2834-416B-936E-D25C70990049Q24339564-858DAEDA-FFCC-4C21-B899-CE16736F01DCQ27021981-1055852A-0D90-4BDC-9D96-7B448827995CQ27650906-862C1CE9-CE7B-4ED2-9BDD-E321621BC263Q27652901-DB9F12CB-E505-4F5E-A9F4-C1B11960D980Q27653046-9C45A5A8-3695-4BAF-BF0B-842D169C4985Q27653139-310382B5-6D91-4B45-94FB-1091F285EC48Q27653598-77E69E2B-F553-4D9C-9042-C81CF3E814BAQ27658004-9BD49F27-734A-4B8E-B8CA-6B2A417122D4Q27664129-0029FCE3-E0AD-4644-8FC2-8E9E611F7295Q27667290-CCA4D937-E61E-4BA2-8B24-B40EE8EC9CC1Q27671676-A95EA450-A604-4FAB-BF51-3756E2D93911Q27674716-C717E3DC-FBF5-4530-94EA-945104BBBABCQ27675934-8A35E4F7-7930-4B6A-84C6-B356FC68418AQ27677271-4D137893-7CC5-4DBD-9FD4-739BDD390619Q27678087-AB7F5DD7-6AC1-45EB-9EE7-F21753A20E11Q27679261-D22899B8-7938-41F6-A95E-3BB66B20CD01Q27681380-BC35DF6A-C4F1-40E7-A25D-64AEF1357FE0Q27683971-943FA709-366E-4D34-8D80-49B3A253A23EQ27701638-3DE07835-6547-46B7-AFD9-6F58D610248EQ27702495-44920432-897B-4F6C-B0F0-F1645A6CDDDFQ27728461-941A44A5-34F7-4C6A-9F51-6EF9230D515BQ27931365-1DB4B8D7-36CC-437A-AFD1-9FB7D85C09BAQ27935019-54C6A521-78C4-41F6-8BE7-B9B4E11B853CQ28114828-417020E9-9788-4735-BF84-FEE9E2F8A87CQ28115792-BEB46DDC-F32F-435C-8E36-51F72D88133AQ28117206-66FA8ACC-9706-4E05-9B57-85B20EEAA298Q28270556-AE7446A1-C41C-4EC5-AF58-F4D091B96277Q28477268-A183566C-3FB4-4F38-818C-194557F64C2AQ28512023-F4B36FB9-C323-4146-B4F0-A39457EC5318Q30381908-C25AE0F2-37E4-43DC-BD0A-2C29372656BBQ33577589-7F9FB5F8-66A6-4C0E-BB88-AE3FE58729EAQ33643398-F864971E-A256-4CA1-BD25-71204F9635D0Q33662139-C2C6EFBA-A1CB-45C8-B159-CCB3AFB5AD65Q33721699-830F63BF-D9F2-43D0-B79A-DA703361055AQ33993652-5F0198B4-6552-4C52-A458-480AB44D8360Q34140902-309480D1-8B3E-4D4A-ABD5-056B47867DF5Q34254409-D120ABD4-5774-473E-A4DA-26B417EDCCBDQ34503051-1F52ED03-3244-42DB-A1A8-1520BDAFFD19
P2860
Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites
description
2008 nî lūn-bûn
@nan
2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Activation segment dimerizatio ...... ylation of non-consensus sites
@ast
Activation segment dimerizatio ...... ylation of non-consensus sites
@en
Activation segment dimerizatio ...... ylation of non-consensus sites
@en-gb
Activation segment dimerizatio ...... ylation of non-consensus sites
@nl
type
label
Activation segment dimerizatio ...... ylation of non-consensus sites
@ast
Activation segment dimerizatio ...... ylation of non-consensus sites
@en
Activation segment dimerizatio ...... ylation of non-consensus sites
@en-gb
Activation segment dimerizatio ...... ylation of non-consensus sites
@nl
prefLabel
Activation segment dimerizatio ...... ylation of non-consensus sites
@ast
Activation segment dimerizatio ...... ylation of non-consensus sites
@en
Activation segment dimerizatio ...... ylation of non-consensus sites
@en-gb
Activation segment dimerizatio ...... ylation of non-consensus sites
@nl
P2093
P2860
P50
P921
P3181
P356
P1433
P1476
Activation segment dimerizatio ...... ylation of non-consensus sites
@en
P2093
Andrew Turnbull
Benjamin E Turk
Frank H Niesen
Peter Rellos
Sirlester A Parker
P2860
P304
P3181
P356
10.1038/EMBOJ.2008.8
P407
P577
2008-01-31T00:00:00Z