ArticleJournal of virology1989
Differential requirements of gag and gamma-actin domains for transforming potential of Gardner-Rasheed feline sarcoma virus.
Article in Journal of virology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Characterization of the transforming domain of a feline sarcoma virus encoding a fgr-related tyrosine kinase.Archives of virology · 1994Article
- Syrian hamster embryo cell lines useful for detecting transforming genes in mouse tumours: detection of transforming genes in X-ray-related mouse tumours.British journal of cancer · 1993Article
- Structure and transforming potential of the human cot oncogene encoding a putative protein kinase.Molecular and cellular biology · 1991Article
- Role of gag sequence in the biochemical properties and transforming activity of the avian sarcoma virus UR2-encoded gag-ros fusion protein.Journal of virology · 1990Article
- Hamster cell line suitable for transfection assay of transforming genes.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oncogene of Gardner-Rasheed feline sarcoma virus (GR-FeSV) encodes the 70-kilodalton protein containing gag(p15), gamma-actin, and fgr domains. To determine the role of these domains in the biological activity of P70gag-actin-fgr, we have constructed in-frame deletion and insertion mutants of GR-FeSV. We found, first, that the gamma-actin region could be deleted without affecting the transforming ability of these constructs, although an insertion mutant in the middle of the gamma-actin domain (map position 671) was partially defective in transformation and specifically had a reduced level of in vitro autophosphorylation activity. Second, mutations affecting the C-terminal third of the gag region appeared to abolish the ability to transform NIH 3T3 cells and autophosphorylation activity. These results suggest that the gamma-actin domain is not essentially required for the transforming activity of GR-FeSV but that it may take part in maintaining the conformational integrity of P70gag-actin-fgr and that the gag(p15) domain might have a critical role in modulating the function of P70gag-actin-fgr.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.