The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A.
Open accessAbstract
The protease encoded by the human immunodeficiency virus (HIV) processes the viral gag and gag-pol protein precursor by posttranslational cleavage. In this study we have demonstrated by site-specific mutagenesis (Asp----Thr) and by pepstatin A inhibition that the recombinant HIV protease is an aspartic-type protease. Furthermore, incubation of HIV-infected H9 cells with pepstatin A inhibited part of the intracellular processing of the HIV gag protein yet had no apparent toxicity on HIV-infected cells during 48 hr of incubation.
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Cites
The Efficacy of Azidothymidine (AZT) in the Treatment of Patients with AIDS and AIDS-Related Complex
Fischl, M. A., Richman, D. D., Grieco, M. H., Gottlieb, M. S., Volberding, P. A., Laskin, O. L., Leedom, J. M., Groopman, J. E., Mildvan, D., Schooley, R. T., et al. (1987) · New England Journal of Medicine · doi:10.1056/nejm198707233170401 · Cited by 2,995
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
Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1
Navia, M. A., Fitzgerald, P. M. D., McKeever, B. M., Leu, C.-T., Heimbach, J. C., Herber, W. K., Sigal, I. S., Darke, P. L., & Springer, J. P. (1989) · Nature · doi:10.1038/337615a0 · Cited by 894
INHIBITORS OF HIV-1 PROTEASE: A Major Success of Structure-Assisted Drug Design
Wlodawer, A., & Vondrasek, J. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.249 · Cited by 734
An NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
Complete mutagenesis of the HIV-1 protease
Loeb, D. D., Swanstrom, R., Everitt, L., Manchester, M., Stamper, S. E., & Hutchison, C. A. (1989) · Nature · doi:10.1038/340397a0 · Cited by 327
Structural and biochemical studies of retroviral proteases
Wlodawer, A., & Gustchina, A. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00267-8 · Cited by 166
Metadata
- Authors
- Seelmeier, S., Schmidt, H., Turk, V, & von der Helm, K.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1988-09
- Volume
- 85
- Issue
- 18
- Pages
- 6612-6616
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2065631521
- Cited by
- 328
- References
- 2
- FWCI
- 5.84
- Type
- journal article
- Language
- en
- Open access
- green
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- Seelmeier, S., Schmidt, H., Turk, V, & von der Helm, K. (1988). Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.85.18.6612
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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