The v-sis/PDGF-2 transforming gene product localizes to cell membranes but is not a secretory protein.
about
Structural and functional studies on platelet-derived growth factorInhibition of tumor growth by a monoclonal antibody reactive with an oncogene-encoded tumor antigenIdentification of the protein encoded by the human diffuse B-cell lymphoma (dbl) oncogeneStructural characterization of the human platelet-derived growth factor A-chain cDNA and gene: alternative exon usage predicts two different precursor proteinsPlatelet-derived growth factor gene expression in human atherosclerotic plaques and normal artery wall.The B chain of PDGF alone is sufficient for mitogenesis.Autocrine mechanism for v-sis transformation requires cell surface localization of internally activated growth factor receptors.Ultrastructural localization of a platelet-derived growth factor/v-sis-related protein(s) in cytoplasm and nucleus of simian sarcoma virus-transformed cells.The human transforming growth factor type alpha coding sequence is not a direct-acting oncogene when overexpressed in NIH 3T3 cellsThe extracellular regulation of growth factor actionSuramin, an experimental chemotherapeutic drug, activates the receptor for epidermal growth factor and promotes growth of certain malignant cells.Cultured human endothelial cells express platelet-derived growth factor A chain.Activation of coagulation releases endothelial cell mitogensCell 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 oncoprotein loses transforming activity when targeted to the early Golgi complexThe 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.Compartmentalization of PDGF on extracellular binding sites dependent on exon-6-encoded sequences.Intracellular retention of membrane-anchored v-sis protein abrogates autocrine signal transductionA 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 factorPartially transformed, anchorage-independent human diploid fibroblasts result from overexpression of the c-sis oncogene: mitogenic activity of an apparent monomeric platelet-derived growth factor 2 species.Expression of recombinant platelet-derived growth factor A- and B-chain homodimers in rat-1 cells and human fibroblasts reveals differences in protein processing and autocrine effects.Identification and characterization of the herpesvirus saimiri oncoprotein STP-C488.Expression and purification of biologically active v-sis/platelet-derived growth factor B protein by using a baculovirus vector system.Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 geneDeletions in the N-terminal coding region of the v-sis gene: determination of the minimal transforming regionDeletions in the C-terminal coding region of the v-sis gene: dimerization is required for transformation.Identification of a signal for nuclear targeting in platelet-derived-growth-factor-related molecules.The int-1 proto-oncogene products are glycoproteins that appear to enter the secretory pathway.Platelet-derived growth factor: mechanism of action and possible in vivo function.Identification of a cell retention signal in the B-chain of platelet-derived growth factor and in the long splice version of the A-chain.Transformation of mouse BALB/c 3T3 cells with human basic fibroblast growth factor cDNA.Expression of acidic fibroblast growth factor cDNA confers growth advantage and tumorigenesis to Swiss 3T3 cellsAlpha-thrombin induces release of platelet-derived growth factor-like molecule(s) by cultured human endothelial cells.Expression of human basic fibroblast growth factor cDNA in baby hamster kidney-derived cells results in autonomous cell growth.High glucose concentration induces the overexpression of transforming growth factor-beta through the activation of a platelet-derived growth factor loop in human mesangial cells.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
Q24555662-B3242735-705B-4357-9FB8-9E787224B610Q24628627-E5033B32-9DF6-43E6-BD3E-6E55901ACC5CQ24628785-00A7A632-768E-47AE-9A4D-E2B0880C79EFQ24632602-C507CEBB-BE6F-4878-BDA0-2E28089AE77DQ33567932-24687709-F028-4919-A2EF-EF2BEFCE3EDDQ33932076-0E08EDE5-B64E-4D05-8139-67DDE36B7B3EQ34313642-7E0F89B8-2151-44F1-933C-966E8AE2082FQ34613380-20B841CB-6778-4EA3-BDDF-5DA485C89951Q34627570-FC9139E4-2876-4663-9007-C06116EFEB09Q35465713-2BB7E480-6FE7-47D4-B0F3-A465F2A84F12Q35600805-3351020E-6AE8-49A3-891C-CDB341E48C1DQ35855846-88F92264-2A9B-47A6-80EF-1BD4C0C06131Q36213145-EB7AAF40-D6BC-4DC2-A4BD-528FD1CAECB3Q36216647-724DEC1F-4914-4D2E-A55B-BC1443AD42EBQ36219059-45D30990-E3C6-435A-A5A6-3FF94F3FF392Q36234954-A18BDA19-B3D8-4E15-A194-644404BBB65FQ36383213-3E551F05-57DC-49F4-881A-BAD29A7D4016Q36530768-2952EB55-F54A-4A15-B168-AE5105E534BDQ36531805-90B08BD6-D1EE-48F8-AE55-E1EEC0C3AF72Q36729640-D27EE334-6A9F-456D-A559-CA60C29D9BE6Q36784625-CAA3A16C-5ED7-4F04-BCC7-28FDDDE69463Q36788861-241B3D70-5F18-4C90-9D80-4C21540797AFQ36791505-2F7DB415-0657-4C56-B344-E8B78E6CF879Q36828959-426130CA-E491-4DE1-94F0-9D4D4DEE0AFCQ36829386-347A53B6-EDD1-4D30-B974-C01FA6FAB5A7Q36851389-38B1042F-814E-479F-90EB-CE5E63D58FA8Q36864605-78FEFCC0-3744-4103-A6EE-500210C810E1Q36912493-3A88B34F-E5E9-49F6-BBCC-1CAB69D2AA02Q36922350-010125B4-F1D2-4292-A163-5D162D006D42Q36923580-D4A8BC6D-9C43-47F7-99AE-51589D8FD64AQ37565963-40633561-A751-494B-8F82-8EAF02C5BB3FQ40642668-925BD4FD-E695-4A13-8029-1DA745378156Q40648863-44BAAC2B-EAE6-44D9-A8F1-E535E7066F59Q41091747-863D76E3-612D-49A2-9EC7-255EEE56B4C9Q41508649-2370980B-E9FE-489E-9779-61E3A344BFE2Q41546404-547297F9-E6C9-46EA-95EE-F969D10F32EAQ41760360-B78D0666-D877-4F64-B968-86A31A23BD99Q42571055-5B980A03-1243-4BC1-9BA2-F5916042B87F
P2860
The v-sis/PDGF-2 transforming gene product localizes to cell membranes but is not a secretory protein.
description
1985 nî lūn-bûn
@nan
1985 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1985 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
name
The v-sis/PDGF-2 transforming ...... ut is not a secretory protein.
@ast
The v-sis/PDGF-2 transforming ...... ut is not a secretory protein.
@en
type
label
The v-sis/PDGF-2 transforming ...... ut is not a secretory protein.
@ast
The v-sis/PDGF-2 transforming ...... ut is not a secretory protein.
@en
prefLabel
The v-sis/PDGF-2 transforming ...... ut is not a secretory protein.
@ast
The v-sis/PDGF-2 transforming ...... ut is not a secretory protein.
@en
P2093
P2860
P1433
P1476
The v-sis/PDGF-2 transforming ...... ut is not a secretory protein.
@en
P2093
P2860
P304
P407
P577
1985-07-01T00:00:00Z