The 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.
about
Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasiaProfound ligand-independent kinase activation of fibroblast growth factor receptor 3 by the activation loop mutation responsible for a lethal skeletal dysplasia, thanatophoric dysplasia type IICellular transformation by a transmembrane peptide: structural requirements for the bovine papillomavirus E5 oncoprotein.The v-sis oncoprotein loses transforming activity when targeted to the early Golgi complexBovine papillomavirus E5 and E7 oncoproteins in naturally occurring tumors: are two better than one?Growth factor PDGF-B/v-sis confers a tumorigenic phenotype to human tumor cells bearing PDGF receptors but not to cells devoid of receptors: evidence for an autocrine, but not a paracrine, mechanism.
P2860
The 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.
description
1993 nî lūn-bûn
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1993年の論文
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name
The v-sis protein retains biol ...... apilloma virus E5 oncoprotein.
@ast
The v-sis protein retains biol ...... apilloma virus E5 oncoprotein.
@en
type
label
The v-sis protein retains biol ...... apilloma virus E5 oncoprotein.
@ast
The v-sis protein retains biol ...... apilloma virus E5 oncoprotein.
@en
prefLabel
The v-sis protein retains biol ...... apilloma virus E5 oncoprotein.
@ast
The v-sis protein retains biol ...... apilloma virus E5 oncoprotein.
@en
P2093
P2860
P356
P1476
The v-sis protein retains biol ...... apilloma virus E5 oncoprotein.
@en
P2093
P2860
P304
P356
10.1083/JCB.123.3.549
P407
P577
1993-11-01T00:00:00Z