The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Myristoylation-dependent replication and assembly of human immunodeficiency virus 1.
Open accessAbstract
Covalent linkage of myristic acid to the N-terminal glycine residue of Pr55gag, the precursor of the major structural proteins of human immunodeficiency virus 1 (HIV-1), facilitates an essential step in virus assembly and propagation. Substitution of the myristoyl-acceptor glycine with alanine, in a functional clone of HIV-1, eliminates virus replication. Complementation of this defect, in trans, restores infectious particle production. The nonmyristoylated (myr-) gag precursor accumulates in infected cells and is not processed into the mature capsid components of the intact virion. However, myr- Pr55gag can be processed by purified HIV protease in vitro, demonstrating that the myristoyl moiety is not required for cleavage by the protease. Myristoylation of Pr55gag is not necessary for localization but is required for stable membrane association and assembly of HIV-1.
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
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Göttlinger, H. G., Sodroski, J. G., & Haseltine, W. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5781 · Cited by 841
Biochemical and immunological analysis of human immunodeficiency virus gag gene products p17 and p24
Veronese, F. D., Copeland, T. D., Oroszlan, S., Gallo, R. C., & Sarngadharan, M. G. (1988) · Journal of Virology · doi:10.1128/jvi.62.3.795-801.1988 · Cited by 203
Cited by
Resh, M. D. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00075-0 · Cited by 1,250
HIV-1 Gag proteins: diverse functions in the virus life cycle
Freed, E. O. (1998) · Virology · doi:10.1006/viro.1998.9398 · Cited by 717
Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
Göttlinger, H. G., Dorfman, T., Sodroski, J. G., & Haseltine, W. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3195 · Cited by 647
Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55 Gag
VerPlank, L., Bouamr, F., LaGrassa, T. J., Agresta, B., Kikonyogo, A., Leis, J., & Carter, C. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.131059198 · Cited by 584
Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
Saad, J. S., Miller, J., Tai, J., Kim, A., Ghanam, R. H., & Summers, M. F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602818103 · Cited by 545
Metadata
- Authors
- Bryant, M., & Ratner, L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1990-01
- Volume
- 87
- Issue
- 2
- Pages
- 523-527
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2028156315
- Cited by
- 627
- References
- 6
- FWCI
- 7.70
- Type
- journal article
- Language
- en
- Open access
- green
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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.