The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain.
about
Copine-III interacts with ErbB2 and promotes tumor cell migrationErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent mannerIdentification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent associationProgesterone receptor induces ErbB-2 nuclear translocation to promote breast cancer growth via a novel transcriptional effect: ErbB-2 function as a coactivator of Stat3Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancerAutoinhibition of the insulin-like growth factor I receptor by the juxtamembrane regionDistinct tyrosine autophosphorylation sites negatively and positively modulate neu-mediated transformationCsk homologous kinase, a novel signaling molecule, directly associates with the activated ErbB-2 receptor in breast cancer cells and inhibits their proliferationc-Src modulates ErbB2 and ErbB3 heterocomplex formation and function.Profiling the HER3/PI3K pathway in breast tumors using proximity-directed assays identifies correlations between protein complexes and phosphoproteins.Synergism from combined immunologic and pharmacologic inhibition of HER2 in vivo.Trastuzumab-induced recruitment of Csk-homologous kinase (CHK) to ErbB2 receptor is associated with ErbB2-Y1248 phosphorylation and ErbB2 degradation to mediate cell growth inhibition.Human prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growthHER2/neu: mechanisms of dimerization/oligomerization.Shc is required for ErbB2-induced inhibition of apoptosis but is dispensable for cell proliferation and disruption of cell polarityHER2: the neu prognostic marker for breast cancer.Autophosphorylation: a salient feature of protein kinases.Dual transcriptional control by Ear3/COUP: negative regulation through the DR1 direct repeat and positive regulation through a sequence downstream of the transcriptional start site of the mouse mammary tumor virus promoter.A genetic basis for the variation in the vulnerability of cancer to DNA damage.The carboxyl terminus controls ligand-dependent activation of VEGFR-2 and its signalingPrognostic impact of phosphorylated HER-2 in HER-2+ primary breast cancerHER2 therapy: molecular mechanisms of trastuzumab resistance.Polyclonal HER2-specific antibodies induced by vaccination mediate receptor internalization and degradation in tumor cells.Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1Mechanisms of disease: understanding resistance to HER2-targeted therapy in human breast cancer.A truncated K-sam product lacking the distal carboxyl-terminal portion provides a reduced level of autophosphorylation and greater resistance against induction of differentiationHer-2/neu-triggered intracellular tyrosine kinase activation: in vivo relevance of ligand-independent activation mechanisms and impact upon the efficacy of trastuzumab-based treatment.Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors17 beta-estradiol mimics ligand activity of the c-erbB2 protooncogene product.DNA vaccination controls Her-2+ tumors that are refractory to targeted therapies.Genetic regulation of the response to Her-2 DNA vaccination in human Her-2 transgenic mice.Carboxyl-terminal deletion and point mutations decrease the transforming potential of the activated rat neu oncogene product.Synthetic phosphopeptide immunogens yield activation-specific antibodies to the c-erbB-2 receptor.FRAG1, a gene that potently activates fibroblast growth factor receptor by C-terminal fusion through chromosomal rearrangement.A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP kinase pathway.Aberrant Signaling through the HER2-ERK1/2 Pathway is Predictive of Reduced Disease-Free and Overall Survival in Early Stage Non-Small Cell Lung Cancer (NSCLC) Patients.Deletion of the carboxyl terminus of Tie2 enhances kinase activity, signaling, and function. Evidence for an autoinhibitory mechanism.Mechanisms of tumor cell resistance to the current targeted-therapy agents.Stat3 regulates ErbB-2 expression and co-opts ErbB-2 nuclear function to induce miR-21 expression, PDCD4 downregulation and breast cancer metastasis.Oncogenic Ras abrogates MEK SUMOylation that suppresses the ERK pathway and cell transformation.
P2860
Q22001536-C3C8CDDB-5742-45FE-AECA-DD5413ACF3DBQ24293488-BB9F8607-E887-4B04-9C55-E8E08735ED03Q24297029-FD2A235E-890F-427C-A7C0-E252F1C7B6D6Q24301306-00CC2360-A50D-4C7A-BBB1-3DD75C984E32Q24301665-F21020C8-8E47-4E30-9DE1-08E70CE1642BQ24313159-83B6965E-A231-4001-BF35-D0415F75C3D1Q28577281-40A7F72A-FDA4-4076-906B-D9AB5A76C1CBQ28678895-F70DE75A-EAAF-4B01-94A2-61A4DA853C97Q30442374-2DAB7A99-849E-4635-9177-997395BDD28AQ30997919-57C7D4CF-4DCD-4627-807F-C72B6C4A609EQ33798772-5D174758-7FA8-4B50-870D-43B2E9A760BEQ33989927-026896C9-5D11-45E3-BF21-7A660DB109C0Q34025197-45E6CD39-71FD-4895-A777-0299946A919EQ34130541-53C55D67-6EB2-4CDE-ACBD-570A74BCBF7DQ34169164-C6C7AE32-C32F-44D9-B20F-B9762E7E3CC0Q34248406-FFD158C4-BC22-433E-9E32-2EFA47F42E41Q34323982-46BE7567-04FE-4A97-A01E-80763CC7912BQ34332556-0222CEA2-1921-4F2E-99D9-5E881DE1B7B7Q34523304-191E3D41-90F4-4D8D-BB07-D8FF35125E48Q34623704-7AE6CFA9-AE07-476A-86AF-62BD3C93752AQ35584641-7C4C5E93-6238-44E1-8F17-5E3A8C17A7C0Q35633712-AAF5C57E-BDE2-454C-B65F-52BBCBDC12E6Q36245418-7F86E314-5116-46E9-9DDD-E56E04284B91Q36463488-9B133B4C-7270-4900-B65D-E673DF32E409Q36472437-36A5EDB3-674A-4582-8E3A-8826B4562BDCQ36552571-5C3B5CD9-AC6F-4185-AB62-1487B21D097DQ36648369-68E25AA6-8199-486C-8A6B-495EBE3AE19AQ36668724-C06669AB-C646-4120-A041-3CECA583BF00Q36674311-4462DF9F-715D-4C6F-9944-48254A6126E8Q36924836-4453DEED-739F-4009-92E4-A228AE47183EQ37036281-9C63558C-0846-49D3-971F-AEDA0D2A5AD7Q37146015-65E65F17-A259-4751-9C5A-DB1EC8870F69Q37280359-0CA8D38E-E1F1-4AEE-9170-3CCDE42CCFD8Q37379343-90036E0C-A86B-4685-B17A-7071FDB897DBQ37634563-BE1BC4F2-33D2-4DDA-AA56-5DE22E0146D8Q37667783-AF5DA99D-D415-49B9-B2F3-0F96BE0E9A6EQ38287809-4C38ED0C-5C77-4CC3-BA96-658BA83B8F6EQ38828353-E413A04E-414D-45BA-9945-C67A7DB55149Q38849205-895D5D6E-5096-4515-A022-906822420C55Q39589034-5665F1F5-C1A3-43F6-9AB9-ADEFDCB7098F
P2860
The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
The transforming potential of ...... the carboxyl-terminal domain.
@en
type
label
The transforming potential of ...... the carboxyl-terminal domain.
@en
prefLabel
The transforming potential of ...... the carboxyl-terminal domain.
@en
P2093
P2860
P356
P1476
The transforming potential of ...... the carboxyl-terminal domain.
@en
P2093
P2860
P304
P356
10.1128/MCB.11.2.833
P407
P577
1991-02-01T00:00:00Z