Docking-based substrate recognition by the catalytic domain of a protein tyrosine kinase, C-terminal Src kinase (Csk).
about
Structural basis for the recognition of c-Src by its inactivator CskProteins at work: a combined small angle X-RAY scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscapeSH2-dependent autophosphorylation within the Tec family kinase Itk.Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases.Signaling properties of a non-metazoan Src kinase and the evolutionary history of Src negative regulationConformational basis for SH2-Tyr(P)527 binding in Src inactivation.c-Src-mediated epithelial cell migration and invasion regulated by PDZ binding site.C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2Identification of new members of the MAPK gene family in plants shows diverse conserved domains and novel activation loop variants.Conformational snapshots of Tec kinases during signaling.Itk tyrosine kinase substrate docking is mediated by a nonclassical SH2 domain surface of PLCgamma1.Structural elements and allosteric mechanisms governing regulation and catalysis of CSK-family kinases and their inhibition of Src-family kinases.Regulation of the SRC family kinases by Csk.Design, Synthesis, and Evaluation of Dasatinib-Amino Acid and Dasatinib-Fatty Acid Conjugates as Protein Tyrosine Kinase Inhibitors.Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine.SRC tail phosphorylation is limited by structural changes in the regulatory tyrosine kinase Csk.Csk-homologous kinase (Chk/Matk): a molecular policeman suppressing cancer formation and progression
P2860
Q24311447-BB17F1F3-377E-455D-8B95-A60F4EA301DAQ30156049-3609DE3C-0443-4779-B5E3-629FC04A8768Q30157228-11182D8C-2138-4DA9-AC57-D8A754866EFFQ30157342-AFA1E1C5-BF6B-4A90-888C-5A0F4E20DFA7Q30157711-31677717-72C1-44F9-A6B8-1F1A64347183Q30159758-9D19AA44-895B-4E03-A146-BDC7A11DF611Q30481162-52BD08F8-68FB-4D7D-AE9E-D9B10EB67145Q33556208-653A442B-79EE-47A6-B68F-7315905CDF44Q35186711-4699006D-1E6D-4FA2-9F00-9547621A81CBQ37416259-AECA6E4B-C8FD-473C-A502-2B5F429D7525Q37452660-1C1040C4-5CBE-4FA2-BCCA-B495C1A2B174Q37754461-F1486932-6051-4368-A407-B9C67B4600AEQ38058787-519C4789-C75D-43F1-A9B6-E0AAD5F01D8EQ38729630-367EFF3B-25BC-4432-B6A5-F7B72FB56F79Q41292352-B93B766D-BA1D-4379-B0EA-8018E99F57B9Q44226943-073BDD18-5586-4314-B53F-0239E7DC91BBQ58134756-A1CC38E8-735E-4B7B-BB4E-3758CC13E732
P2860
Docking-based substrate recognition by the catalytic domain of a protein tyrosine kinase, C-terminal Src kinase (Csk).
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Docking-based substrate recogn ...... , C-terminal Src kinase (Csk).
@en
type
label
Docking-based substrate recogn ...... , C-terminal Src kinase (Csk).
@en
prefLabel
Docking-based substrate recogn ...... , C-terminal Src kinase (Csk).
@en
P2093
P2860
P356
P1476
Docking-based substrate recogn ...... , C-terminal Src kinase (Csk).
@en
P2093
David J Kemble
Gongqin Sun
Keykavous Parang
Marina K Ayrapetov
Sungsoo Lee
P2860
P304
P356
10.1074/JBC.M508120200
P407
P577
2006-01-26T00:00:00Z