Requirement for a signal sequence in biological expression of the v-sis oncogene.
about
Nucleotide sequence of transforming human c-sis cDNA clones with homology to platelet-derived growth factorAutocrine transformation by chimeric signal peptide-basic fibroblast growth factor: reversal by suramin.The v-sis/PDGF-2 transforming gene product localizes to cell membranes but is not a secretory protein.The B chain of PDGF alone is sufficient for mitogenesis.Secretory protein traffic. Chromogranin A contains a dominant targeting signal for the regulated pathwayCell surface expression of membrane-anchored v-sis gene products: glycosylation is not required for cell surface transportAutocrine stimulation by the v-sis gene product requires a ligand-receptor interaction at the cell surfaceThe v-sis protein retains biological activity as a type II membrane protein when anchored by various signal-anchor domains, including the hydrophobic domain of the bovine papilloma virus E5 oncoprotein.A small v-sis/platelet-derived growth factor (PDGF) B-protein domain in which subtle conformational changes abrogate PDGF receptor interaction and transforming activity.Identification of nonessential disulfide bonds and altered conformations in the v-sis protein, a homolog of the B chain of platelet-derived growth factorDeletions in the N-terminal coding region of the v-sis gene: determination of the minimal transforming regionHigh mutation rate of a spleen necrosis virus-based retrovirus vectorActivation of oncogenicity of the c-rel proto-oncogene.Deletions in the C-terminal coding region of the v-sis gene: dimerization is required for transformation.Biosynthesis of the v-sis gene product: signal sequence cleavage, glycosylation, and proteolytic processing.Identification of a signal for nuclear targeting in platelet-derived-growth-factor-related molecules.Biologically active mutants with deletions in the v-mos oncogene assayed with retroviral vectors.Transformation by the v-fms oncogene product: role of glycosylational processing and cell surface expression.In vitro mutagenesis of the v-sis transforming gene defines functional domains of its growth factor-related product.Lysine residue 121 in the proposed ATP-binding site of the v-mos protein is required for transformation.Structure and nucleotide sequence of the 5' region of the human and feline c-sis proto-oncogenes.Genetic organization of the c-sis transcription unit.The phenotypic characteristics of simian sarcoma virus-transformed human fibroblasts suggest that the v-sis gene product acts solely as a PDGF receptor agonist in cell transformation.
P2860
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P2860
Requirement for a signal sequence in biological expression of the v-sis oncogene.
description
1984 nî lūn-bûn
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1984年の論文
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1984年学术文章
@wuu
1984年学术文章
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1984年学术文章
@zh-cn
1984年学术文章
@zh-hans
1984年学术文章
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1984年学术文章
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1984年學術文章
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1984年學術文章
@zh-hant
name
Requirement for a signal sequence in biological expression of the v-sis oncogene.
@en
Requirement for a signal sequence in biological expression of the v-sis oncogene.
@nl
type
label
Requirement for a signal sequence in biological expression of the v-sis oncogene.
@en
Requirement for a signal sequence in biological expression of the v-sis oncogene.
@nl
prefLabel
Requirement for a signal sequence in biological expression of the v-sis oncogene.
@en
Requirement for a signal sequence in biological expression of the v-sis oncogene.
@nl
P356
P1433
P1476
Requirement for a signal sequence in biological expression of the v-sis oncogene.
@en
P2093
Donoghue DJ
P304
P356
10.1126/SCIENCE.6095451
P407
P577
1984-12-01T00:00:00Z