Статті в журналах з теми "RETROVIRAL PROTEASE"
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Blusch, Jürgen H., Sigrid Seelmeir, and Klaus von der Helm. "Molecular and Enzymatic Characterization of the Porcine Endogenous Retrovirus Protease." Journal of Virology 76, no. 15 (August 1, 2002): 7913–17. http://dx.doi.org/10.1128/jvi.76.15.7913-7917.2002.
Повний текст джерелаLehmann-Che, Jacqueline, Marie-Lou Giron, Olivier Delelis, Martin Löchelt, Patricia Bittoun, Joelle Tobaly-Tapiero, Hugues de Thé, and Ali Saïb. "Protease-Dependent Uncoating of a Complex Retrovirus." Journal of Virology 79, no. 14 (July 2005): 9244–53. http://dx.doi.org/10.1128/jvi.79.14.9244-9253.2005.
Повний текст джерелаDavis, David A., Cara A. Brown, Fonda M. Newcomb, Emily S. Boja, Henry M. Fales, Joshua Kaufman, Stephen J. Stahl, Paul Wingfield, and Robert Yarchoan. "Reversible Oxidative Modification as a Mechanism for Regulating Retroviral Protease Dimerization and Activation." Journal of Virology 77, no. 5 (March 1, 2003): 3319–25. http://dx.doi.org/10.1128/jvi.77.5.3319-3325.2003.
Повний текст джерелаWeber, Irene T., Yuan-Fang Wang, and Robert W. Harrison. "HIV Protease: Historical Perspective and Current Research." Viruses 13, no. 5 (May 6, 2021): 839. http://dx.doi.org/10.3390/v13050839.
Повний текст джерелаPettit, Steven C., Sergei Gulnik, Lori Everitt, and Andrew H. Kaplan. "The Dimer Interfaces of Protease and Extra-Protease Domains Influence the Activation of Protease and the Specificity of GagPol Cleavage." Journal of Virology 77, no. 1 (January 1, 2003): 366–74. http://dx.doi.org/10.1128/jvi.77.1.366-374.2003.
Повний текст джерелаYoungren, S. D., J. D. Boeke, N. J. Sanders, and D. J. Garfinkel. "Functional organization of the retrotransposon Ty from Saccharomyces cerevisiae: Ty protease is required for transposition." Molecular and Cellular Biology 8, no. 4 (April 1988): 1421–31. http://dx.doi.org/10.1128/mcb.8.4.1421-1431.1988.
Повний текст джерелаYoungren, S. D., J. D. Boeke, N. J. Sanders, and D. J. Garfinkel. "Functional organization of the retrotransposon Ty from Saccharomyces cerevisiae: Ty protease is required for transposition." Molecular and Cellular Biology 8, no. 4 (April 1988): 1421–31. http://dx.doi.org/10.1128/mcb.8.4.1421.
Повний текст джерелаÁlvarez, Enrique, Luis Menéndez-Arias, and Luis Carrasco. "The Eukaryotic Translation Initiation Factor 4GI Is Cleaved by Different Retroviral Proteases." Journal of Virology 77, no. 23 (December 1, 2003): 12392–400. http://dx.doi.org/10.1128/jvi.77.23.12392-12400.2003.
Повний текст джерелаHartl, Maximilian J., Kristian Schweimer, Martin H. Reger, Stephan Schwarzinger, Jochen Bodem, Paul Rösch, and Birgitta M. Wöhrl. "Formation of transient dimers by a retroviral protease." Biochemical Journal 427, no. 2 (March 29, 2010): 197–203. http://dx.doi.org/10.1042/bj20091451.
Повний текст джерелаGolda, Mária, János András Mótyán, Mohamed Mahdi, and József Tőzsér. "Functional Study of the Retrotransposon-Derived Human PEG10 Protease." International Journal of Molecular Sciences 21, no. 7 (March 31, 2020): 2424. http://dx.doi.org/10.3390/ijms21072424.
Повний текст джерелаMótyán, János András, Márió Miczi, and József Tőzsér. "Dimer Interface Organization is a Main Determinant of Intermonomeric Interactions and Correlates with Evolutionary Relationships of Retroviral and Retroviral-Like Ddi1 and Ddi2 Proteases." International Journal of Molecular Sciences 21, no. 4 (February 17, 2020): 1352. http://dx.doi.org/10.3390/ijms21041352.
Повний текст джерелаKelleher, Anthony D., Andrew K. Sewell, and David A. Price. "Dyslipidemia due to retroviral protease inhibitors." Nature Medicine 8, no. 4 (April 1, 2002): 308. http://dx.doi.org/10.1038/nm0402-308a.
Повний текст джерелаWeber, Irene T. "Structural alignment of retroviral protease sequences." Gene 85, no. 2 (December 1989): 565–66. http://dx.doi.org/10.1016/0378-1119(89)90453-8.
Повний текст джерелаYip, Matthew C. J., Nicholas O. Bodnar, and Tom A. Rapoport. "Ddi1 is a ubiquitin-dependent protease." Proceedings of the National Academy of Sciences 117, no. 14 (March 19, 2020): 7776–81. http://dx.doi.org/10.1073/pnas.1902298117.
Повний текст джерелаGolda, Mária, János András Mótyán, Mohamed Mahdi, and József Tőzsér. "Study of the Retrotransposon-Derived Human PEG10 Protease." Proceedings 50, no. 1 (July 1, 2020): 110. http://dx.doi.org/10.3390/proceedings2020050110.
Повний текст джерелаMiller, Maria, Jonathan Leis, and Alexander Wlodawer. "Preliminary crystallographic study of a retroviral protease." Journal of Molecular Biology 204, no. 1 (November 1988): 211–12. http://dx.doi.org/10.1016/0022-2836(88)90610-9.
Повний текст джерелаHoráková, Dana, Michaela Rumlová, Iva Pichová, and Tomáš Ruml. "Luminometric method for screening retroviral protease inhibitors." Analytical Biochemistry 345, no. 1 (October 2005): 96–101. http://dx.doi.org/10.1016/j.ab.2005.07.013.
Повний текст джерелаWang, Shainn-Wei, Kristin Noonan, and Anna Aldovini. "Nucleocapsid-RNA Interactions Are Essential to Structural Stability but Not to Assembly of Retroviruses." Journal of Virology 78, no. 2 (January 15, 2004): 716–23. http://dx.doi.org/10.1128/jvi.78.2.716-723.2004.
Повний текст джерелаDavis, David A., Haydar Bulut, Prabha Shrestha, Hiroaki Mitsuya, and Robert Yarchoan. "Regulation of Retroviral and SARS-CoV-2 Protease Dimerization and Activity through Reversible Oxidation." Antioxidants 11, no. 10 (October 18, 2022): 2054. http://dx.doi.org/10.3390/antiox11102054.
Повний текст джерелаBagossi, Péter, Tamás Sperka, Anita Fehér, János Kádas, Gábor Zahuczky, Gabriella Miklóssy, Péter Boross, and József Tözsér. "Amino Acid Preferences for a Critical Substrate Binding Subsite of Retroviral Proteases in Type 1 Cleavage Sites." Journal of Virology 79, no. 7 (April 1, 2005): 4213–18. http://dx.doi.org/10.1128/jvi.79.7.4213-4218.2005.
Повний текст джерелаMiller, Maria, Mariusz Jaskólski, J. K. Mohana Rao, Jonathan Leis, and Alexander Wlodawer. "Crystal structure of a retroviral protease proves relationship to aspartic protease family." Nature 337, no. 6207 (February 1989): 576–79. http://dx.doi.org/10.1038/337576a0.
Повний текст джерелаSadiq, S. Kashif. "Reaction–diffusion basis of retroviral infectivity." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 374, no. 2080 (November 13, 2016): 20160148. http://dx.doi.org/10.1098/rsta.2016.0148.
Повний текст джерелаWosicki, Stanislaw, Miroslaw Gilski, Helena Zabranska, Iva Pichova, and Mariusz Jaskolski. "Comparison of a retroviral protease in monomeric and dimeric states." Acta Crystallographica Section D Structural Biology 75, no. 10 (September 20, 2019): 904–17. http://dx.doi.org/10.1107/s2059798319011355.
Повний текст джерелаBühler, Bernd, Ying-Chuan Lin, Garrett Morris, Arthur J. Olson, Chi-Huey Wong, Douglas D. Richman, John H. Elder, and Bruce E. Torbett. "Viral Evolution in Response to the Broad-Based Retroviral Protease Inhibitor TL-3." Journal of Virology 75, no. 19 (October 1, 2001): 9502–8. http://dx.doi.org/10.1128/jvi.75.19.9502-9508.2001.
Повний текст джерелаDAVIS, David A., Fonda M. NEWCOMB, Jackob MOSKOVITZ, Paul T. WINGFIELD, Stephen J. STAHL, Joshua KAUFMAN, Henry M. FALES, Rodney L. LEVINE, and Robert YARCHOAN. "HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase." Biochemical Journal 346, no. 2 (February 22, 2000): 305–11. http://dx.doi.org/10.1042/bj3460305.
Повний текст джерелаRaugi, Dana N., Robert A. Smith, and Geoffrey S. Gottlieb. "Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors." Journal of Virology 90, no. 2 (November 11, 2015): 1062–69. http://dx.doi.org/10.1128/jvi.01772-15.
Повний текст джерелаSturley, Stephen L., Oliver Distler, Jun-Shan Liang, David A. Cooper, Richard J. Deckelbaum, and Henry N. Ginsberg. "Reply to 'Dyslipidemia due to retroviral protease inhibitors'." Nature Medicine 8, no. 4 (April 1, 2002): 308–9. http://dx.doi.org/10.1038/nm0402-308b.
Повний текст джерелаGerminario, Ralph. "Anti-Retroviral Protease Inhibitors -'A Two Edged Sword?'." IUBMB Life 55, no. 2 (February 1, 2003): 67–70. http://dx.doi.org/10.1080/1521654031000090922.
Повний текст джерелаMiller, Maria. "The early years of retroviral protease crystal structures." Biopolymers 94, no. 4 (June 30, 2010): 521–29. http://dx.doi.org/10.1002/bip.21387.
Повний текст джерелаGerminario, Ralph J. "Anti-Retroviral Protease Inhibitors - ‘A Two Edged Sword?’." IUBMB Life 55, no. 2 (February 13, 2008): 67–70. http://dx.doi.org/10.1002/tbmb.718540874.
Повний текст джерелаGolda, Mária, János András Mótyán, Katalin Nagy, Krisztina Matúz, Tibor Nagy, and József Tőzsér. "Biochemical Characterization of Human Retroviral-Like Aspartic Protease 1 (ASPRV1)." Biomolecules 10, no. 7 (July 6, 2020): 1004. http://dx.doi.org/10.3390/biom10071004.
Повний текст джерелаWlodawer, A., M. Miller, M. Jaskolski, B. Sathyanarayana, E. Baldwin, I. Weber, L. Selk, L. Clawson, J. Schneider, and S. Kent. "Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease." Science 245, no. 4918 (August 2, 1989): 616–21. http://dx.doi.org/10.1126/science.2548279.
Повний текст джерелаOnchieku, Noah Machuki, Sonam Kumari, Rajan Pandey, Vaibhav Sharma, Mohit Kumar, Arunaditya Deshmukh, Inderjeet Kaur, et al. "Artemisinin Binds and Inhibits the Activity of Plasmodium falciparum Ddi1, a Retroviral Aspartyl Protease." Pathogens 10, no. 11 (November 11, 2021): 1465. http://dx.doi.org/10.3390/pathogens10111465.
Повний текст джерелаRein, Alan. "Murine Leukemia Viruses: Objects and Organisms." Advances in Virology 2011 (2011): 1–14. http://dx.doi.org/10.1155/2011/403419.
Повний текст джерелаEizert, Helga, Pálma Bander, Péter Bagossi, Tamás Sperka, Gabriella Miklóssy, Péter Boross, Irene T. Weber, and József Tözsér. "Amino Acid Preferences of Retroviral Proteases for Amino-Terminal Positions in a Type 1 Cleavage Site." Journal of Virology 82, no. 20 (August 13, 2008): 10111–17. http://dx.doi.org/10.1128/jvi.00418-08.
Повний текст джерелаKotler, M., W. Danho, R. A. Katz, J. Leis, and A. M. Skalka. "Avian Retroviral Protease and Cellular Aspartic Proteases are Distinguished by Activities on Peptide Substrates." Journal of Biological Chemistry 264, no. 6 (February 1989): 3428–35. http://dx.doi.org/10.1016/s0021-9258(18)94085-8.
Повний текст джерелаSwanstrom, Ronald, and Wesley I. Sundquist. "Stephan Oroszlan and the Proteolytic Processing of Retroviral Proteins: Following A Pro." Viruses 13, no. 11 (November 4, 2021): 2218. http://dx.doi.org/10.3390/v13112218.
Повний текст джерелаKotler, M., R. A. Katz, and A. M. Skalka. "Activity of avian retroviral protease expressed in Escherichia coli." Journal of Virology 62, no. 8 (1988): 2696–700. http://dx.doi.org/10.1128/jvi.62.8.2696-2700.1988.
Повний текст джерелаSirkis, Roy, Jeffrey E. Gerst, and Deborah Fass. "Ddi1, a Eukaryotic Protein With the Retroviral Protease Fold." Journal of Molecular Biology 364, no. 3 (December 2006): 376–87. http://dx.doi.org/10.1016/j.jmb.2006.08.086.
Повний текст джерелаHafenrichter, Rudolf, Frank Weiland, Josef Schneider, and Heinz-Jürgen Thiel. "Properties of retroviral protease responsible for gag precursor cleavage." Virology 172, no. 1 (September 1989): 355–58. http://dx.doi.org/10.1016/0042-6822(89)90139-6.
Повний текст джерелаSlabaugh, M. B., and N. A. Roseman. "Retroviral protease-like gene in the vaccinia virus genome." Proceedings of the National Academy of Sciences 86, no. 11 (June 1, 1989): 4152–55. http://dx.doi.org/10.1073/pnas.86.11.4152.
Повний текст джерелаLi, Mi, Alla Gustchina, Rui Cruz, Marisa Simões, Pedro Curto, Juan Martinez, Carlos Faro, Isaura Simões, and Alexander Wlodawer. "Structure of RC1339/APRc fromRickettsia conorii, a retropepsin-like aspartic protease." Acta Crystallographica Section D Biological Crystallography 71, no. 10 (September 30, 2015): 2109–18. http://dx.doi.org/10.1107/s1399004715013905.
Повний текст джерелаOnchieku, Noah Machuki, Reagan Mogire, Loise Ndung'u, Peter Mwitari, Francis Kimani, Damaris Matoke-Muhia, Daniel Kiboi, and Gabriel Magoma. "Deciphering the targets of retroviral protease inhibitors in Plasmodium berghei." PLOS ONE 13, no. 8 (August 1, 2018): e0201556. http://dx.doi.org/10.1371/journal.pone.0201556.
Повний текст джерелаKontijevskis, Aleksejs, Peteris Prusis, Ramona Petrovska, Sviatlana Yahorava, Felikss Mutulis, Ilze Mutule, Jan Komorowski, and Jarl E. S. Wikberg. "A Look Inside HIV Resistance through Retroviral Protease Interaction Maps." PLoS Computational Biology 3, no. 3 (March 9, 2007): e48. http://dx.doi.org/10.1371/journal.pcbi.0030048.
Повний текст джерелаKontijevskis, Aleksejs, Peteris Prusis, Ramona Petrovska, Sviatlana Yahorava, Felikss Mutulis, Ilze Mutule, Jan Komorowski, and Jarl E. Wikberg. "A Look inside HIV Resistance through Retroviral Protease Interaction Maps." PLoS Computational Biology preprint, no. 2007 (2005): e48. http://dx.doi.org/10.1371/journal.pcbi.0030048.eor.
Повний текст джерелаTOH, HIROYUKI, MASAO ONO, KAORU SAIGO, and TAKASHI MIYATA. "Retroviral protease-like sequence in the yeast transposon Ty 1." Nature 315, no. 6021 (June 1985): 691. http://dx.doi.org/10.1038/315691a0.
Повний текст джерелаKatoh, Iyoko, Teruo Yasunaga, Yoji Ikawa, and Yoshiyuki Yoshinaka. "Inhibition of retroviral protease activity by an aspartyl proteinase inhibitor." Nature 329, no. 6140 (October 1987): 654–56. http://dx.doi.org/10.1038/329654a0.
Повний текст джерелаLlido, S., B. Langlois d"Estaintot, A. Dautant, S. Geoffre, P. Picard, and G. Precigoux. "Conformational study of a putative HLTV-1 retroviral protease inhibitor." Acta Crystallographica Section D Biological Crystallography 49, no. 3 (May 1, 1993): 344–48. http://dx.doi.org/10.1107/s0907444992013623.
Повний текст джерелаKotler, M., R. A. Katz, W. Danho, J. Leis, and A. M. Skalka. "Synthetic peptides as substrates and inhibitors of a retroviral protease." Proceedings of the National Academy of Sciences 85, no. 12 (June 1, 1988): 4185–89. http://dx.doi.org/10.1073/pnas.85.12.4185.
Повний текст джерелаMELLOR, J., S. M. FULTON, M. J. DOBSON, W. WILSON, S. M. KINGSMAN, and A. J. KINGSMAN. "Retroviral protease-like sequence in the yeast transposon Ty 1(reply)." Nature 315, no. 6021 (June 1985): 691–92. http://dx.doi.org/10.1038/315691b0.
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