Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src.
about
C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptorNegative regulation of PYK2/related adhesion focal tyrosine kinase signal transduction by hematopoietic tyrosine phosphatase SHPTP1Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell linesTrafficking of Lyn through the Golgi caveolin involves the charged residues on alphaE and alphaI helices in the kinase domainRegulation of cytochrome c oxidase activity by c-Src in osteoclastsThe rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residueSubdomain X of the kinase domain of Lck binds CD45 and facilitates dephosphorylationRegulation of FynT function by dual domain docking on PAG/CbpTyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphataseStructural and functional studies of the intracellular tyrosine kinase MATK gene and its translated productIdentification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signalingCsk inhibition of c-Src activity requires both the SH2 and SH3 domains of SrcAssociation of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cellsIdentification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatasesIn vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinaseAssociation of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cellsTranslocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated plateletsTyrosine phosphorylation of p62(Dok) induced by cell adhesion and insulin: possible role in cell migrationPositive and negative regulation of T-cell activation through kinases and phosphatasesDok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signalingThe human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activityMutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactionsAutophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60srcThe role of Src in solid tumorsOverexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreadingDifferential effects of B cell receptor and B cell receptor-FcgammaRIIB1 engagement on docking of Csk to GTPase-activating protein (GAP)-associated p62Expressed protein ligation: a general method for protein engineeringSrc kinase becomes preferentially associated with the VEGFR, KDR/Flk-1, following VEGF stimulation of vascular endothelial cells.Structure of the carboxyl-terminal Src kinase, CskThe crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loopCD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic acid-dependent ovarian tumor cell migrationProtein-tyrosine Phosphatase and Kinase Specificity in Regulation of SRC and Breast Tumor KinaseA novel adaptor-like protein which is a substrate for the non-receptor tyrosine kinase, BRKConserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHKInterleukin-6, CD45 and the src-kinases in myeloma cell proliferationSpecific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphataseProtein tyrosine phosphatase PTPN22 in human autoimmunityThe Csk-like proteins Lsk, Hyl, and Matk represent the same Csk homologous kinase (Chk) and are regulated by stem cell factor in the megakaryoblastic cell line MO7eSequence requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein kinase p50(csk)Regulation of mouse PECAM-1 tyrosine phosphorylation by the Src and Csk families of protein-tyrosine kinases
P2860
Q22008788-A6A421CF-3451-4C01-85EA-54597948F1EDQ22010652-A97EC418-E7D0-4909-90AE-8C64EFE3AC51Q24290329-44DC22C8-4116-4A35-8DC5-CB2422B64D88Q24294813-4BC2B2AE-BB3B-43FB-AFB1-2DE5A3C89EEDQ24296720-ACC26F2C-E6EC-400D-AA85-D1CDC8D433DFQ24296923-D6B80A0F-3CE2-4388-A520-76D15688DBFEQ24300044-F35F5EE7-4F94-4E36-A334-7911BBBF11C9Q24302122-57F00779-E6A1-4CD9-8402-2A8659252A80Q24304981-ADFC4DCD-1209-4248-9E5C-335A53CD0848Q24306629-558061E9-D382-4235-880C-0BE768ADCF4AQ24309099-F5D5E4EF-6514-45D0-AD6F-80AD341BA95FQ24310206-55DB0E11-1484-4F25-BB27-88102C0C8B0CQ24314260-D1121511-5FD0-4CAB-965A-9778796C3191Q24314502-3D58A7B4-67AB-4655-9391-366C768F8712Q24314627-E40D52C8-4C04-4235-8CC8-93D34051A628Q24315982-BF1AB553-77EC-4109-81C2-5415A121AE01Q24532179-33700B44-6F29-408B-B8DE-0F453D6100B5Q24534026-B95084DA-53CE-4556-92B4-6EFD6D578832Q24535649-2896D87A-A1DE-493D-8DCE-C0CEA0FF3426Q24554273-D990A757-8044-4880-8547-58EC9CF120C6Q24555677-86E28BF1-037B-4BFA-85C0-BC1DD64F4AF2Q24568352-ED9744A5-26D6-43B6-A779-F7B7C74830EBQ24614033-5BE41BB3-E164-4A4C-88B3-96D2F6F19CC4Q24616659-3ECE6FDC-55BF-43A4-BAF7-DB9B1ADAAACCQ24646895-4134D9EF-DD1E-41E7-A248-B667BA8EA91FQ24653005-7CCF7E95-82AD-4627-B05A-FA72B02440ACQ24657669-EA0A62A8-0005-4369-BCFC-317AA5BC3677Q24796859-2BD8CE22-1F5B-47F6-A0DD-8865CBDC5553Q27638251-E64DC072-EB70-43DC-9154-06D356EE8FEEQ27729357-9E050CDA-03E5-4603-A9B0-51CFAF725811Q28116092-144DEA5F-8F85-40B9-8DA9-8DD20D039DF3Q28116384-EAD68D93-BA2E-455E-B110-493E62CBE416Q28138242-15769590-884A-4F2D-8011-4F436A61C355Q28208149-9F0E2149-8936-4141-93D8-8729CC0492C1Q28210841-8D8C8BA6-186D-44FB-BBD5-120546EC5F22Q28211340-A33A9B66-E575-4C1C-BD2D-D60B350B6DA5Q28242744-784242A9-F656-48CA-8692-C8BB65D8127DQ28246125-27896989-372E-4D96-B648-4666F118D8A1Q28270491-B6B2C57A-815B-498D-A316-365BA001BBADQ28273557-E05207A6-A2E2-4DBE-B7DF-43B17C51A78B
P2860
Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src.
description
1991 nî lūn-bûn
@nan
1991 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@ast
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@en
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@nl
type
label
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@ast
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@en
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@nl
prefLabel
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@ast
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@en
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@nl
P2093
P356
P1433
P1476
Cloning of a complementary DNA ...... e regulatory site of p60c-src.
@en
P2093
P2888
P356
10.1038/351069A0
P407
P577
1991-05-01T00:00:00Z
P6179
1045337250