Evidence that the Rous sarcoma virus transforming gene product phosphorylates phosphatidylinositol and diacylglycerol
about
Phosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulationTyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transductionShould individual PI3 kinase isoforms be targeted in cancer?Expression and characterization of the p85 subunit of the phosphatidylinositol 3-kinase complex and a related p85 beta protein by using the baculovirus expression systemPhosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: the p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinaseCloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85The PI3K pathway as drug target in human cancerTargeting the PI3K/AKT/mTOR signaling axis in children with hematologic malignanciesPhosphoinositides: tiny lipids with giant impact on cell regulationStructure-Based Design of an Organoruthenium Phosphatidyl-inositol-3-kinase Inhibitor Reveals a Switch Governing Lipid Kinase Potency and SelectivityThe hunting of the SrcActivation of diacylglycerol kinase alpha is required for VEGF-induced angiogenic signaling in vitroDirect association of Grb2 with the p85 subunit of phosphatidylinositol 3-kinaseThe catalytic subunit of phosphatidylinositol 3-kinase is a substrate for the activated platelet-derived growth factor receptor, but not for middle-T antigen-pp60c-src complexesPI3K/PTEN signaling in angiogenesis and tumorigenesisRegulation of diacylglycerol kinase alpha by phosphoinositide 3-kinase lipid productsNew insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathwayCooperation of Src homology domains in the regulated binding of phosphatidylinositol 3-kinase. A role for the Src homology 2 domain.Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells.Phosphorylation and activation of epidermal growth factor receptors in cells transformed by the src oncogeneInduction of neurite outgrowth by v-src mimics critical aspects of nerve growth factor-induced differentiation.Rous sarcoma virus variants that encode src proteins with an altered carboxy terminus are defective for cellular transformation.Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptorsTranscriptional regulation of PIK3CA oncogene by NF-kappaB in ovarian cancer microenvironment.Expression of activated PIK3CA in ovarian surface epithelium results in hyperplasia but not tumor formation.Activated type I phosphatidylinositol kinase is associated with the epidermal growth factor (EGF) receptor following EGF stimulationModulation of cellular apoptotic potential: contributions to oncogenesis.Structure and nucleotide sequence of a Drosophila melanogaster protein kinase C gene.Phosphatidylinositol turnover and transformation of cells by Abelson murine leukaemia virus.PI3K: from the bench to the clinic and back.Phosphatidylinositol 3-kinase: the oncoprotein.Phosphatidylinositol kinase is activated in membranes derived from cells treated with epidermal growth factor.Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-srcA protein kinase antigenically related to pp60v-src possibly involved in yeast cell cycle control: positive in vivo regulation by sterol.SRF-dependent gene expression is required for PI3-kinase-regulated cell proliferation.Phosphorylation and inactivation of protein phosphatase 1 by pp60v-srcPurification of the platelet-derived growth factor receptor by using an anti-phosphotyrosine antibodyPhosphatidylinositol metabolism and polyoma-mediated transformation.Dissociation of inositol trisphosphate from diacylglycerol production in Rous sarcoma virus-transformed fibroblastsThe action of v-src on gap junctional permeability is modulated by pH
P2860
Q24293143-6DC08EBA-3310-482C-9B87-E7A61FCD38A7Q24303984-34A2170B-E654-4D54-B41F-076233469DF8Q24309044-AA39E966-D0DF-40BF-B7FD-6852621C9757Q24527428-B862B2E4-A088-49D1-A580-A1875CDCD5CCQ24629183-3061CDB9-292D-45F0-B47F-81606A2CECC0Q24629213-39FAB41F-249E-484E-8C65-546ADB6AA5C1Q24632283-E50C216E-B0A6-4660-8576-CC498E75D1C9Q26829652-11C2E8D7-0456-44AE-AD02-F7A570F32433Q27012953-D9CE81EE-D65D-4D85-9B45-DE951615F172Q27650628-79894C10-FBFE-4F55-B86F-698FBDC01C02Q28199081-FCB571E0-DEC6-4009-88EC-983C2B1BF7A2Q28259748-1752DDC1-ADB3-4D54-8F80-38F91E51C56EQ28302000-93310D47-1506-4939-BF72-09EC72EFB1FEQ28367583-2CCB70BD-122C-4E3A-ADF0-082C07C9A651Q28383083-BC9BC4D5-D7C3-44E0-A398-8902D5FE7A67Q28591275-28C2B72A-22D1-4806-8790-6727138D99AFQ29616144-8DEB9B56-2065-4460-8E18-9B491BC2F5A0Q30193526-99562010-B79E-4FB1-AAC5-50E2A8084B3AQ30194870-2467FB59-F8A5-48B2-B31D-0B051D0F62EEQ30441810-45D277C2-1436-4739-BD91-A257CB1BC260Q30450313-BE5BCDE4-52E7-4DA3-B1DA-509BA2A9662CQ30452257-D8117A58-A3D6-47FC-883C-C7003AFC17A3Q31169174-6D8EAD45-5A75-4A7D-AF3D-67F6D752121BQ33323364-DA220A0D-68C8-432E-9398-A6912E47AFD5Q33403197-B99357F1-D1D8-441B-901A-14B9D66AFBC1Q33587507-8F226836-3D9E-4196-9BFA-873519BD91A3Q33771748-8E20D34B-1335-4080-99AC-B9993ADA0E41Q33928836-9BA2A6CA-99F1-4A91-95AC-E0F1EBBF8BABQ33931990-43A6F349-3C00-4433-8246-858D9E13C9BBQ34195495-6A021D58-1E84-4813-803E-E4AF6054B8BCQ34203861-9D27968F-800F-440B-B9EE-4C8871B303FDQ34358119-7C7391C6-C589-4F87-975B-159A8B0574C7Q34469297-C0B6FEE9-094B-456B-8821-CB99493F724DQ34630739-678CDC6A-6044-4678-B152-BCBFB2F4777CQ35123848-CAB3BF4B-5145-4887-9C50-93F208A9DB90Q35585097-5D7CD7D9-3C3F-4BFB-8D44-E1DBABB2212BQ35587864-900F629F-17A2-45C5-B919-7E04A4D6A1F1Q35607272-304E1D44-6873-41DE-AB74-1A50E274DA15Q36220044-1B817DBD-4D6E-4192-AEB1-B3EB8FEC7393Q36222833-6D52BB65-050B-49A0-9B6E-344DDB6BAD8B
P2860
Evidence that the Rous sarcoma virus transforming gene product phosphorylates phosphatidylinositol and diacylglycerol
description
1984 nî lūn-bûn
@nan
1984年の論文
@ja
1984年学术文章
@wuu
1984年学术文章
@zh-cn
1984年学术文章
@zh-hans
1984年学术文章
@zh-my
1984年学术文章
@zh-sg
1984年學術文章
@yue
1984年學術文章
@zh
1984年學術文章
@zh-hant
name
Evidence that the Rous sarcoma ...... dylinositol and diacylglycerol
@ast
Evidence that the Rous sarcoma ...... dylinositol and diacylglycerol
@en
type
label
Evidence that the Rous sarcoma ...... dylinositol and diacylglycerol
@ast
Evidence that the Rous sarcoma ...... dylinositol and diacylglycerol
@en
prefLabel
Evidence that the Rous sarcoma ...... dylinositol and diacylglycerol
@ast
Evidence that the Rous sarcoma ...... dylinositol and diacylglycerol
@en
P2093
P2860
P356
P1476
Evidence that the Rous sarcoma ...... dylinositol and diacylglycerol
@en
P2093
R L Erikson
Y Sugimoto
P2860
P304
P356
10.1073/PNAS.81.7.2117
P407
P577
1984-04-01T00:00:00Z