The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
Truncated gag-related proteins are produced by large deletion mutants of Rous sarcoma virus and form virus particles
Open accessAbstract
Large deletion (LD) mutants of Prague strain Rous sarcoma virus subgroup B (PrB), derived by serial undiluted passage through chicken (C/E) cells, contain two deletions relative to wild-type virus. One of these joins gag sequences in the p12 coding region to env sequences in region encoding gp37; the other deletion spans the src region. Analysis of the viral proteins of QT6 cell clones containing only LD proviruses by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a major truncated gag-related phosphoprotein of 60,000 to 66,000 daltons (P63LD). P63LD was stable, but could be cleaved in vitro to the predicted products by p15gag. A second gag-related LD protein of about 68,000 to 74,000 molecular weight (P70LD) was also found which often reacted with an anti-gp37 serum. P70LD was unstable and may represent a short-lived gag-gp37 fusion protein. Finally, immunoprecipitation indicated that particles containing P63LD were shed from QT6-LD clones. Thin section preparations of these clones viewed in an electron microscope showed enveloped budding particles of "immature" morphology. Thus, the synthesis and release of particles from infected cells does not require cleavage of the gag precursor, nor does it require the presence of p15 or (most of) p12.
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“Such structural differences have been observed in viruses that assemble at the plasma membrane, such MLV and HIV-1, as well as those that preassemble in the cytoplasm before budding, such as MPMV and MMTV”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Voynow and Coffin 1985
Citations
Cites
Nucleotide sequence of rous sarcoma virus
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Continuous tissue culture cell lines derived from chemically induced tumors of Japanese quail
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Bister, K., Hayman, M. J., & Vogt, P. K. (1977) · Virology · doi:10.1016/0042-6822(77)90017-4 · Cited by 259
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Nermut, M. V., Frank, H., & Schäfer, W. (1972) · Virology · doi:10.1016/0042-6822(72)90487-4 · Cited by 161
Defectiveness of avian erythroblastosis virus: synthesis of a 75K gag-related protein
Hayman, M. J., Royer‐Pokora, B., & Graf, T. (1979) · Virology · doi:10.1016/0042-6822(79)90212-5 · Cited by 155
Tsichlis, P. N., & Coffin, J. M. (1980) · Journal of Virology · doi:10.1128/jvi.33.1.238-249.1980 · Cited by 129
Self-citationLocalization of RNA tumor virus polypeptides
Bolognesi, D. P., Luftig, R. B., & Shaper, J. H. (1973) · Virology · doi:10.1016/0042-6822(73)90057-3 · Cited by 123
Biochemical properties of p15-associated protease in an avian RNA tumor virus
Dittmar, K. J., & Moelling, K. (1978) · Journal of Virology · doi:10.1128/jvi.28.1.106-118.1978 · Cited by 112
The genome-associated, specific RNA binding proteins of avian and mammalian type C viruses
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Properties of a Ribonucleoprotein Particle Isolated from Nonidet P-40-Treated Rous Sarcoma Virus
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Cited by
Crystal structure of a retroviral protease proves relationship to aspartic protease family
Miller, M., Jaskólski, M., Rao, J. K. M., Leis, J., & Wlodawer, A. (1989) · Nature · doi:10.1038/337576a0 · Cited by 343
Protein delivery using engineered virus-like particles
Kaczmarczyk, S. J., Sitaraman, K., Young, H. A., Hughes, S. H., & Chatterjee, D. K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101874108 · Cited by 234
Genetic Diversity and Evolution of Retroviruses
Coffin, J. M. (1992) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-77011-1_10 · Cited by 217
Self-citationMéric, C., & Spahr, P. F. (1986) · Journal of Virology · doi:10.1128/jvi.60.2.450-459.1986 · Cited by 187
Proteolytic Processing and Particle Maturation
Vogt, V. M. (1996) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-80145-7_4 · Cited by 163
Metadata
- Authors
- Voynow, S. L., & Coffin, J. M.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 1985-07
- Volume
- 55
- Issue
- 1
- Pages
- 79-85
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC254900
- OpenAlex
- W1493165726
- Cited by
- 40
- References
- 38
- Citations by year
- 2025: 1 · 2016: 1 · 2015: 2 · 2014: 2 · 2012: 2
- FWCI
- 1.31
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- journals.asm.org/non-commercial-tdm-license (tdm)
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA27108)
- National Institute of General Medical Sciences (GM 07310)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Health Sciences › Medicine › Infectious Diseases › Infectious Diseases and Mycology
- Keywords
- viral assembly, immature virus particles, provirus
- MeSH terms
- Animals, Avian Sarcoma Viruses, Cells, Cultured, Chickens, Chromosome Deletion, Microscopy, Electron, Molecular Weight, Morphogenesis, Mutation, Protein Precursors, Viral Proteins, Virion, Virus Replication, Gene Products, gag
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Cite CoChat for the checks on this page, and the paper for its own findings.
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- CoChat. (2026). Citation check: Truncated gag-related proteins are produced by large deletion mutants of Rous sarcoma virus and form virus particles. https://app.cochat.ai/papers/10.1128/jvi.55.1.79-85.1985
- The paper
- Voynow, S. L., & Coffin, J. M. (1985). Truncated gag-related proteins are produced by large deletion mutants of Rous sarcoma virus and form virus particles. Journal of Virology. https://doi.org/10.1128/jvi.55.1.79-85.1985
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
