Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.
about
Cys-140 is critical for metabotropic glutamate receptor-1 dimerizationIdentification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent associationMechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segmentPhosphorylation of ErbB4 on tyrosine 1056 is critical for ErbB4 coupling to inhibition of colony formation by human mammary cell linesStructural requirements of the interleukin-6 signal transducer gp130 for its interaction with Janus kinase 1: the receptor is crucial for kinase activationInhibition of ErbB-2 mitogenic and transforming activity by RALT, a mitogen-induced signal transducer which binds to the ErbB-2 kinase domainA specific interface between integrin transmembrane helices and affinity for ligandTyrosine kinase signalling in breast cancer: ErbB family receptor tyrosine kinasesThe Under-Appreciated Promiscuity of the Epidermal Growth Factor Receptor FamilyDimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alphaIdentification and characterization of two members of a novel class of the interleukin-1 receptor (IL-1R) family. Delineation of a new class of IL-1R-related proteins based on signalingControlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimersLigand-independent dimerization and activation of the oncogenic Xmrk receptor by two mutations in the extracellular domain.Normal activation of discoidin domain receptor 1 mutants with disulfide cross-links, insertions, or deletions in the extracellular juxtamembrane region: mechanistic implicationsComplexity of signal transduction mediated by ErbB2: clues to the potential of receptor-targeted cancer therapy.HER2/neu: mechanisms of dimerization/oligomerization.Nerve growth factor signals via preexisting TrkA receptor oligomersOncogenic IL7R gain-of-function mutations in childhood T-cell acute lymphoblastic leukemia.Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association.Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase.Melanoma development and pigment cell transformation in xiphophorus.Juxtamembrane autoinhibition in receptor tyrosine kinases.Vascular endothelial growth factor A competitively inhibits platelet-derived growth factor (PDGF)-dependent activation of PDGF receptor and subsequent signaling events and cellular responsesMutational activation of ErbB family receptor tyrosine kinases: insights into mechanisms of signal transduction and tumorigenesis.Functional selectivity of EGF family peptide growth factors: implications for cancer.Suppression of proliferation of two independent NF1 malignant peripheral nerve sheath tumor cell lines by the pan-ErbB inhibitor CI-1033.Transmembrane helix-helix interactions involved in ErbB receptor signaling.Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling.Self-association of the transmembrane domain of RET underlies oncogenic activation by MEN2A mutations.Molecular modeling of nearly full-length ErbB2 receptor.The epidermal growth factor receptor (EGFR)-S442F mutant displays increased affinity for neuregulin-2beta and agonist-independent coupling with downstream signalling events.Structural requirements of the extracellular to transmembrane domain junction for erythropoietin receptor function.Gene expression profiling of ErbB receptor and ligand-dependent transcription.Activated eIF4E-binding protein slows G1 progression and blocks transformation by c-myc without inhibiting cell growth.Epidermal growth factor receptor: association of extracellular domain negatively regulates intracellular kinase activation in the absence of ligand.Definition of an inhibitory juxtamembrane WW-like domain in the platelet-derived growth factor beta receptor.Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization.Ligand discrimination in signaling through an ErbB4 receptor homodimer.Bovine papillomavirus E5 protein induces the formation of signal transduction complexes containing dimeric activated platelet-derived growth factor beta receptor and associated signaling proteins.
P2860
Q24290099-53E44883-FD25-43C5-82E7-AE1B90C3ACB9Q24297029-C72C6E71-18C6-4037-A7BC-5661E9A1C46DQ24309071-F6D11EA2-49EA-4686-94C7-F810E1FD73A4Q24318725-9FB82964-A7AD-4B03-A5BB-D12FDCC1DB50Q24533565-C4A257BE-0776-42A6-B5F5-101E5C9A82FFQ24551173-DBDD7B8A-EC59-482E-BD4F-D155EDAB330AQ24793060-C4A9CF7F-58B4-4324-A311-1AC178D0E51BQ24802950-4E734471-9470-4525-BE0E-A0328B09DCB5Q28073335-9E1373AD-2BCB-462C-BCE9-6ECBD0136231Q28374431-4E6DAC82-8F8B-4A3C-B064-4E71CB15CDB8Q28592094-D89D384C-AD6D-4639-AA57-FBC0842F9559Q28679173-C920154F-6764-4F6C-B18D-FAC002202F63Q31473336-9F6BCFDA-DF4D-41A1-9ABC-C367B1E5DBEDQ33676762-822CB27B-2A3A-42B7-9076-020C115AC979Q33801908-7A30CC30-DAF2-4552-B7C5-778D466D60E3Q34130541-7EA842F7-EE84-4AF8-8A33-CCD84AE7BB4EQ34178490-103BCFF9-07CE-4A17-B288-F49BA6A1AB38Q34213539-C466B4E1-F623-4E5B-87DB-5B4FC17543D5Q34488179-44600F41-1DF4-4418-B8AB-C7696AC6E0FDQ34626693-DF0965A9-5F3E-4C53-A4A7-17170C0FDF5EQ34769307-C7F82102-5855-41A1-B5E6-A206CC3B3262Q34872771-F28E0038-7CA9-4228-9B7D-A2A5EA423725Q35790329-98E28F7C-3747-4E42-8BA4-676BC3818C08Q35943908-2A61F1DC-E88C-4C04-9A75-C14E5D10CA9CQ36824808-EFDE67F2-2FEA-47B6-A7BF-E2679E880695Q37149729-6F34F697-B582-4CAC-822C-EE6F92855816Q37582080-6829982D-35D8-42DC-92B0-15DA6E96B522Q37704902-B31177A9-CF06-478A-8DB4-BE0CD3AFE299Q39616171-677441F3-29E9-4449-8E97-BDC86B7ADB41Q40274230-3F562F37-1594-4341-BF22-7CE866FCF7A7Q40316579-68278EE5-2139-4312-B9AD-97E0D375757FQ40323538-7EA55715-6CC3-4354-B28E-34D1E4E6204FQ40469656-D9E7757D-6C01-4CC7-82BF-4C73AF9420B0Q40587910-D7293CC4-FCD4-4192-AFD5-204B1373A0C8Q40618406-88A13CE8-B2F3-4572-9137-E6A3B2440010Q40641352-BE6AF5B9-DCE0-41AF-8C54-24532B8298E8Q40710486-7632EF79-9BE6-43E7-A9FA-14D1D9DFADAEQ40732382-23582B50-A9BA-458B-ABBA-C079285E259FQ40871706-5B2238EA-71E9-4343-AAC1-38CC7D0BCE70Q40891304-57813462-A036-4F08-8A64-D94B0B61C08A
P2860
Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Activation of Neu (ErbB-2) med ...... rosine kinase dimer interface.
@ast
Activation of Neu (ErbB-2) med ...... rosine kinase dimer interface.
@en
type
label
Activation of Neu (ErbB-2) med ...... rosine kinase dimer interface.
@ast
Activation of Neu (ErbB-2) med ...... rosine kinase dimer interface.
@en
prefLabel
Activation of Neu (ErbB-2) med ...... rosine kinase dimer interface.
@ast
Activation of Neu (ErbB-2) med ...... rosine kinase dimer interface.
@en
P2860
P356
P1476
Activation of Neu (ErbB-2) med ...... rosine kinase dimer interface.
@en
P2093
P2860
P304
P356
10.1128/MCB.18.9.5371
P407
P577
1998-09-01T00:00:00Z