Протеаза ВИЧ-1 (Russian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Протеаза ВИЧ-1" in Russian language version.

refsWebsite

Global rank Russian rank

15nih.gov

4^th place

6^th place

15wikipedia.org

low place

9doi.org

2^nd place

3^rd place

1utexas.edu

916^th place

1,381^st place

doi.org

dx.doi.org

Davies D. R. The structure and function of the aspartic proteinases. (англ.) // Annual review of biophysics and biophysical chemistry. — 1990. — Vol. 19. — P. 189—215. — doi:10.1146/annurev.bb.19.060190.001201. — PMID 2194475. [исправить]
Huang X., Britto M. D., Kear-Scott J. L., Boone C. D., Rocca J. R., Simmerling C., Mckenna R., Bieri M., Gooley P. R., Dunn B. M., Fanucci G. E. The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics. (англ.) // The Journal of biological chemistry. — 2014. — Vol. 289, no. 24. — P. 17203—17214. — doi:10.1074/jbc.M114.571836. — PMID 24742668. [исправить]
Yang H., Nkeze J., Zhao R. Y. Effects of HIV-1 protease on cellular functions and their potential applications in antiretroviral therapy. (англ.) // Cell & bioscience. — 2012. — Vol. 2, no. 1. — P. 32. — doi:10.1186/2045-3701-2-32. — PMID 22971934. [исправить]
Kipp D. R., Hirschi J. S., Wakata A., Goldstein H., Schramm V. L. Transition states of native and drug-resistant HIV-1 protease are the same. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 2012. — Vol. 109, no. 17. — P. 6543—6548. — doi:10.1073/pnas.1202808109. — PMID 22493227. [исправить]
Ding F., Layten M., Simmerling C. Solution structure of HIV-1 protease flaps probed by comparison of molecular dynamics simulation ensembles and EPR experiments. (англ.) // Journal of the American Chemical Society. — 2008. — Vol. 130, no. 23. — P. 7184—7185. — doi:10.1021/ja800893d. — PMID 18479129. [исправить]
Hornak V., Okur A., Rizzo R. C., Simmerling C. HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 2006. — Vol. 103, no. 4. — P. 915—920. — doi:10.1073/pnas.0508452103. — PMID 16418268. [исправить]
Huang L., Chen C. Understanding HIV-1 protease autoprocessing for novel therapeutic development. (англ.) // Future medicinal chemistry. — 2013. — Vol. 5, no. 11. — P. 1215—1229. — doi:10.4155/fmc.13.89. — PMID 23859204. [исправить]
Moore J. P., Stevenson M. New targets for inhibitors of HIV-1 replication. (англ.) // Nature reviews. Molecular cell biology. — 2000. — Vol. 1, no. 1. — P. 40—49. — doi:10.1038/35036060. — PMID 11413488. [исправить]
De Clercq E. The design of drugs for HIV and HCV. (англ.) // Nature reviews. Drug discovery. — 2007. — Vol. 6, no. 12. — P. 1001—1018. — doi:10.1038/nrd2424. — PMID 18049474. [исправить]

nih.gov

ncbi.nlm.nih.gov

Davies D. R. The structure and function of the aspartic proteinases. (англ.) // Annual review of biophysics and biophysical chemistry. — 1990. — Vol. 19. — P. 189—215. — doi:10.1146/annurev.bb.19.060190.001201. — PMID 2194475. [исправить]
Brik A., Wong C. H. HIV-1 protease: mechanism and drug discovery. (англ.) // Organic & biomolecular chemistry. — 2003. — Vol. 1, no. 1. — P. 5—14. — PMID 12929379. [исправить]
Huang X., Britto M. D., Kear-Scott J. L., Boone C. D., Rocca J. R., Simmerling C., Mckenna R., Bieri M., Gooley P. R., Dunn B. M., Fanucci G. E. The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics. (англ.) // The Journal of biological chemistry. — 2014. — Vol. 289, no. 24. — P. 17203—17214. — doi:10.1074/jbc.M114.571836. — PMID 24742668. [исправить]
Kräusslich H. G., Ingraham R. H., Skoog M. T., Wimmer E., Pallai P. V., Carter C. A. Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1989. — Vol. 86, no. 3. — P. 807—811. — PMID 2644644. [исправить]
Kohl N. E., Emini E. A., Schleif W. A., Davis L. J., Heimbach J. C., Dixon R. A., Scolnick E. M., Sigal I. S. Active human immunodeficiency virus protease is required for viral infectivity. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1988. — Vol. 85, no. 13. — P. 4686—4690. — PMID 3290901. [исправить]
Seelmeier S., Schmidt H., Turk V., von der Helm K. Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1988. — Vol. 85, no. 18. — P. 6612—6616. — PMID 3045820. [исправить]
McPhee F., Good A. C., Kuntz I. D., Craik C. S. Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1996. — Vol. 93, no. 21. — P. 11477—11481. — PMID 8876160. [исправить]
Yang H., Nkeze J., Zhao R. Y. Effects of HIV-1 protease on cellular functions and their potential applications in antiretroviral therapy. (англ.) // Cell & bioscience. — 2012. — Vol. 2, no. 1. — P. 32. — doi:10.1186/2045-3701-2-32. — PMID 22971934. [исправить]
Kipp D. R., Hirschi J. S., Wakata A., Goldstein H., Schramm V. L. Transition states of native and drug-resistant HIV-1 protease are the same. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 2012. — Vol. 109, no. 17. — P. 6543—6548. — doi:10.1073/pnas.1202808109. — PMID 22493227. [исправить]
Ding F., Layten M., Simmerling C. Solution structure of HIV-1 protease flaps probed by comparison of molecular dynamics simulation ensembles and EPR experiments. (англ.) // Journal of the American Chemical Society. — 2008. — Vol. 130, no. 23. — P. 7184—7185. — doi:10.1021/ja800893d. — PMID 18479129. [исправить]
Hornak V., Okur A., Rizzo R. C., Simmerling C. HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 2006. — Vol. 103, no. 4. — P. 915—920. — doi:10.1073/pnas.0508452103. — PMID 16418268. [исправить]
Huang L., Chen C. Understanding HIV-1 protease autoprocessing for novel therapeutic development. (англ.) // Future medicinal chemistry. — 2013. — Vol. 5, no. 11. — P. 1215—1229. — doi:10.4155/fmc.13.89. — PMID 23859204. [исправить]
Watkins T., Resch W., Irlbeck D., Swanstrom R. Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors. (англ.) // Antimicrobial agents and chemotherapy. — 2003. — Vol. 47, no. 2. — P. 759—769. — PMID 12543689. [исправить]
Moore J. P., Stevenson M. New targets for inhibitors of HIV-1 replication. (англ.) // Nature reviews. Molecular cell biology. — 2000. — Vol. 1, no. 1. — P. 40—49. — doi:10.1038/35036060. — PMID 11413488. [исправить]
De Clercq E. The design of drugs for HIV and HCV. (англ.) // Nature reviews. Drug discovery. — 2007. — Vol. 6, no. 12. — P. 1001—1018. — doi:10.1038/nrd2424. — PMID 18049474. [исправить]

utexas.edu

iverson.cm.utexas.edu

Brik A., Wong C. H. HIV-1 protease: mechanism and drug discovery. (англ.) // Organic & biomolecular chemistry. — 2003. — Vol. 1, no. 1. — P. 5—14. — PMID 12929379. [исправить]

wikipedia.org

ru.wikipedia.org

Davies D. R. The structure and function of the aspartic proteinases. (англ.) // Annual review of biophysics and biophysical chemistry. — 1990. — Vol. 19. — P. 189—215. — doi:10.1146/annurev.bb.19.060190.001201. — PMID 2194475. [исправить]
Brik A., Wong C. H. HIV-1 protease: mechanism and drug discovery. (англ.) // Organic & biomolecular chemistry. — 2003. — Vol. 1, no. 1. — P. 5—14. — PMID 12929379. [исправить]
Huang X., Britto M. D., Kear-Scott J. L., Boone C. D., Rocca J. R., Simmerling C., Mckenna R., Bieri M., Gooley P. R., Dunn B. M., Fanucci G. E. The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics. (англ.) // The Journal of biological chemistry. — 2014. — Vol. 289, no. 24. — P. 17203—17214. — doi:10.1074/jbc.M114.571836. — PMID 24742668. [исправить]
Kräusslich H. G., Ingraham R. H., Skoog M. T., Wimmer E., Pallai P. V., Carter C. A. Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1989. — Vol. 86, no. 3. — P. 807—811. — PMID 2644644. [исправить]
Kohl N. E., Emini E. A., Schleif W. A., Davis L. J., Heimbach J. C., Dixon R. A., Scolnick E. M., Sigal I. S. Active human immunodeficiency virus protease is required for viral infectivity. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1988. — Vol. 85, no. 13. — P. 4686—4690. — PMID 3290901. [исправить]
Seelmeier S., Schmidt H., Turk V., von der Helm K. Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1988. — Vol. 85, no. 18. — P. 6612—6616. — PMID 3045820. [исправить]
McPhee F., Good A. C., Kuntz I. D., Craik C. S. Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 1996. — Vol. 93, no. 21. — P. 11477—11481. — PMID 8876160. [исправить]
Yang H., Nkeze J., Zhao R. Y. Effects of HIV-1 protease on cellular functions and their potential applications in antiretroviral therapy. (англ.) // Cell & bioscience. — 2012. — Vol. 2, no. 1. — P. 32. — doi:10.1186/2045-3701-2-32. — PMID 22971934. [исправить]
Kipp D. R., Hirschi J. S., Wakata A., Goldstein H., Schramm V. L. Transition states of native and drug-resistant HIV-1 protease are the same. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 2012. — Vol. 109, no. 17. — P. 6543—6548. — doi:10.1073/pnas.1202808109. — PMID 22493227. [исправить]
Ding F., Layten M., Simmerling C. Solution structure of HIV-1 protease flaps probed by comparison of molecular dynamics simulation ensembles and EPR experiments. (англ.) // Journal of the American Chemical Society. — 2008. — Vol. 130, no. 23. — P. 7184—7185. — doi:10.1021/ja800893d. — PMID 18479129. [исправить]
Hornak V., Okur A., Rizzo R. C., Simmerling C. HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations. (англ.) // Proceedings of the National Academy of Sciences of the United States of America. — 2006. — Vol. 103, no. 4. — P. 915—920. — doi:10.1073/pnas.0508452103. — PMID 16418268. [исправить]
Huang L., Chen C. Understanding HIV-1 protease autoprocessing for novel therapeutic development. (англ.) // Future medicinal chemistry. — 2013. — Vol. 5, no. 11. — P. 1215—1229. — doi:10.4155/fmc.13.89. — PMID 23859204. [исправить]
Watkins T., Resch W., Irlbeck D., Swanstrom R. Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors. (англ.) // Antimicrobial agents and chemotherapy. — 2003. — Vol. 47, no. 2. — P. 759—769. — PMID 12543689. [исправить]
Moore J. P., Stevenson M. New targets for inhibitors of HIV-1 replication. (англ.) // Nature reviews. Molecular cell biology. — 2000. — Vol. 1, no. 1. — P. 40—49. — doi:10.1038/35036060. — PMID 11413488. [исправить]
De Clercq E. The design of drugs for HIV and HCV. (англ.) // Nature reviews. Drug discovery. — 2007. — Vol. 6, no. 12. — P. 1001—1018. — doi:10.1038/nrd2424. — PMID 18049474. [исправить]