Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
about
Oncogenic forms of the neu/HER2 tyrosine kinase are permanently coupled to phospholipase C gammaErbB receptors: from oncogenes to targeted cancer therapiesHuman trk oncogenes activated by point mutation, in-frame deletion, and duplication of the tyrosine kinase domainActivating point mutations in the common beta subunit of the human GM-CSF, IL-3 and IL-5 receptors suggest the involvement of beta subunit dimerization and cell type-specific molecules in signallingCorrelation of the structure of the transmembrane domain of the neu oncogene-encoded p185 protein with its functionExpression of the neu protooncogene in the mammary epithelium of transgenic mice induces metastatic disease.Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasiaA complex containing LPP and α-actinin mediates TGFβ-induced migration and invasion of ErbB2-expressing breast cancer cells.Three dimensional structure of the transmembrane region of the proto-oncogenic and oncogenic forms of the neu protein.A chimeric EGF-R-neu proto-oncogene allows EGF to regulate neu tyrosine kinase and cell transformation.The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade.Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.Amplification of the proto-neu oncogene facilitates oncogenic activation by a single point mutation.Experimental approaches to hypothetical hormones: detection of a candidate ligand of the neu protooncogene.Triplex formation inhibits HER-2/neu transcription in vitroA subdomain in the transmembrane domain is necessary for p185neu* activation.Impact of ERBB2 mutations on in vitro sensitivity of bladder cancer to lapatinib.RETRACTED: Soluble Axl is generated by ADAM10-dependent cleavage and associates with Gas6 in mouse serumSomatic expression of PyMT or activated ErbB2 induces estrogen-independent mammary tumorigenesis.Codon cassette mutagenesis: a general method to insert or replace individual codons by using universal mutagenic cassettes.Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies.Introduction of oncogenes into mammary glands in vivo with an avian retroviral vector initiates and promotes carcinogenesis in mouse models.Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase.Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation.Amplification of the neu/erbB-2 oncogene in a mouse model of mammary tumorigenesis.Cellular transformation by a transmembrane peptide: structural requirements for the bovine papillomavirus E5 oncoprotein.GxxxG motifs, phenylalanine, and cholesterol guide the self-association of transmembrane domains of ErbB2 receptorsInduction of different morphologic features of malignant melanoma and pigmented lesions after transformation of murine melanocytes with bFGF-cDNA and H-ras, myc, neu, and E1a oncogenes.Ligand-independent dimerization of oncogenic v-erbB products involves covalent interactions.Modulatory effect of the transmembrane domain of the protein-tyrosine kinase encoded by oncogene ros: biological function and substrate interaction.Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulumExpression of growth factor receptors in human brain tumours.c-erbB-2 oncoprotein expression in primary and advanced breast cancerTransmembrane domain sequence requirements for activation of the p185c-neu receptor tyrosine kinase.Role of promyelocytic leukemia (PML) protein in tumor suppressionSubstitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1His499 Regulates Dimerization and Prevents Oncogenic Activation by Asparagine Mutations of the Human Thrombopoietin ReceptorTransmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides.Mammary tumors expressing the neu proto-oncogene possess elevated c-Src tyrosine kinase activity.The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine
P2860
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P2860
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
@en
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
@nl
type
label
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
@en
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
@nl
prefLabel
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
@en
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
@nl
P2860
P1433
P1476
Oncogenic activation of the neu-encoded receptor protein by point mutation and deletion
@en
P2093
C I Bargmann
R A Weinberg
P2860
P304
P356
10.1002/J.1460-2075.1988.TB03044.X
P407
P577
1988-07-01T00:00:00Z