A dominant negative mutation suppresses the function of normal epidermal growth factor receptors by heterodimerization.
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Activation of the human c-kit product by ligand-induced dimerization mediates circular actin reorganization and chemotaxisControl of fibroblast growth factor receptor kinase signal transduction by heterodimerization of combinatorial splice variantsA dominant negative mutant of 2-5A-dependent RNase suppresses antiproliferative and antiviral effects of interferonHuman piebald trait resulting from a dominant negative mutant allele of the c-kit membrane receptor geneGene therapy for carcinoma of the breast: Genetic ablation strategiesDominant-negative mutations in the G-protein-coupled alpha-factor receptor map to the extracellular ends of the transmembrane segments.Receptors for fibroblast growth factorsMistargeting hippocampal axons by expression of a truncated Eph receptorDiversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactionsActin binding GFP allows 4D in vivo imaging of myofilament dynamics in the zebrafish heart and the identification of Erbb2 signaling as a remodeling factor of myofibril architecture.CLAVATA1 dominant-negative alleles reveal functional overlap between multiple receptor kinases that regulate meristem and organ development.SplicerAV: a tool for mining microarray expression data for changes in RNA processing.A subdomain in the transmembrane domain is necessary for p185neu* activation.A screen for dominant mutations applied to components in the Drosophila EGF-R pathway.Targeted expression of a dominant-negative FGF receptor mutant in the epidermis of transgenic mice reveals a role of FGF in keratinocyte organization and differentiation.Expression of herstatin, an autoinhibitor of HER-2/neu, inhibits transactivation of HER-3 by HER-2 and blocks EGF activation of the EGF receptor.HER2/neu: mechanisms of dimerization/oligomerization.Antagonism of the prostaglandin E2 EP1 receptor in MDCK cells increases growth through activation of Akt and the epidermal growth factor receptor.Dominant negative mutations of the scavenger receptor. Native receptor inactivation by expression of truncated variants.Dominant-negative activity of an alpha(1B)-adrenergic receptor signal-inactivating point mutation.On the nature of low- and high-affinity EGF receptors on living cells.Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation.Ligand and p185c-neu density govern receptor interactions and tyrosine kinase activation.Cancer gene therapy.Adhesion-mediated squamous cell carcinoma survival through ligand-independent activation of epidermal growth factor receptor.Targeted expression of a dominant-negative EGF-R in the kidney reduces tubulo-interstitial lesions after renal injuryMutations of the KIT (mast/stem cell growth factor receptor) proto-oncogene account for a continuous range of phenotypes in human piebaldism.A structure-based model for ligand binding and dimerization of EGF receptors.Ligand-independent dimerization of oncogenic v-erbB products involves covalent interactions.Trans receptor inhibition of human glioblastoma cells by erbB family ectodomains.Biological activity of the receptor for macrophage colony-stimulating factor in the human endometrial cancer cell line, Ishikawa.Loss of functional cell surface transforming growth factor beta (TGF-beta) type 1 receptor correlates with insensitivity to TGF-beta in chronic lymphocytic leukemia.Ligand-independent activation of platelet-derived growth factor receptor is a necessary intermediate in lysophosphatidic, acid-stimulated mitogenic activity in L cells.Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system.Therapeutic potential of EGFR-related protein, a universal EGFR family antagonist.Interactions between Type III receptor tyrosine phosphatases and growth factor receptor tyrosine kinases regulate tracheal tube formation in Drosophila.Identification of tyrosine kinase Trk as a nerve growth factor receptor.Disruption of cellular translational control by a viral truncated eukaryotic translation initiation factor 2alpha kinase homolog.Both stromal cell and colonocyte epidermal growth factor receptors control HCT116 colon cancer cell growth in tumor xenografts.A dominant negative erythropoietin (EPO) receptor inhibits EPO-dependent growth and blocks F-gp55-dependent transformation.
P2860
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P2860
A dominant negative mutation suppresses the function of normal epidermal growth factor receptors by heterodimerization.
description
1991 nî lūn-bûn
@nan
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
1991年论文
@zh
1991年论文
@zh-cn
name
A dominant negative mutation s ...... ceptors by heterodimerization.
@en
type
label
A dominant negative mutation s ...... ceptors by heterodimerization.
@en
prefLabel
A dominant negative mutation s ...... ceptors by heterodimerization.
@en
P2093
P2860
P356
P1476
A dominant negative mutation s ...... ceptors by heterodimerization.
@en
P2093
Schlessinger J
P2860
P304
P356
10.1128/MCB.11.3.1454
P407
P577
1991-03-01T00:00:00Z