HIV-1プロテアーゼ (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "HIV-1プロテアーゼ" in Japanese language version.

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doi.org

“The structure and function of the aspartic proteinases”. Annual Review of Biophysics and Biophysical Chemistry 19 (1): 189–215. (1990). doi:10.1146/annurev.bb.19.060190.001201. PMID 2194475. https://zenodo.org/record/1234933.
“HIV-1 protease: mechanism and drug discovery”. Organic & Biomolecular Chemistry 1 (1): 5–14. (January 2003). doi:10.1039/b208248a. PMID 12929379.
“The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics”. The Journal of Biological Chemistry 289 (24): 17203–14. (June 2014). doi:10.1074/jbc.M114.571836. PMC 4059161. PMID 24742668.
“HIV protease inhibitors: a review of molecular selectivity and toxicity” (英語). HIV/AIDS: Research and Palliative Care 7: 95–104. (April 2015). doi:10.2147/hiv.s79956. PMC 4396582. PMID 25897264.
“Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides”. Proceedings of the National Academy of Sciences of the United States of America 86 (3): 807–11. (February 1989). Bibcode: 1989PNAS...86..807K. doi:10.1073/pnas.86.3.807. PMC 286566. PMID 2644644.
“Active human immunodeficiency virus protease is required for viral infectivity”. Proceedings of the National Academy of Sciences of the United States of America 85 (13): 4686–90. (July 1988). Bibcode: 1988PNAS...85.4686K. doi:10.1073/pnas.85.13.4686. PMC 280500. PMID 3290901.
“HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs”. Protein Science 13 (4): 1108–23. (April 2004). doi:10.1110/ps.03468904. PMC 2280056. PMID 15044738. オリジナルの2008-12-16時点におけるアーカイブ。.
“Folding regulates autoprocessing of HIV-1 protease precursor”. The Journal of Biological Chemistry 280 (12): 11369–78. (March 2005). doi:10.1074/jbc.M412603200. PMID 15632156.
“Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism”. Journal of Virology 78 (16): 8477–85. (August 2004). doi:10.1128/JVI.78.16.8477-8485.2004. PMC 479095. PMID 15280456.
“Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution”. Science 246 (4934): 1149–52. (December 1989). doi:10.1126/science.2686029. PMID 2686029.
“Autoprocessing of HIV-1 protease is tightly coupled to protein folding”. Nature Structural Biology 6 (9): 868–75. (September 1999). doi:10.1038/12327. PMID 10467100.
“Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein”. Proceedings of the National Academy of Sciences of the United States of America 91 (17): 7970–4. (August 1994). Bibcode: 1994PNAS...91.7970L. doi:10.1073/pnas.91.17.7970. PMC 44526. PMID 8058744.
“A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation”. The Journal of Biological Chemistry 271 (8): 4477–81. (February 1996). doi:10.1074/jbc.271.8.4477. PMID 8626801.
“HIV-1 protease function and structure studies with the simplicial neighborhood analysis of protein packing method”. Proteins 73 (3): 742–53. (November 2008). doi:10.1002/prot.22094. PMC 2765824. PMID 18498108.
“Understanding HIV-1 protease autoprocessing for novel therapeutic development”. Future Medicinal Chemistry 5 (11): 1215–29. (July 2013). doi:10.4155/fmc.13.89. PMC 3826259. PMID 23859204.
“Ionization states of the catalytic residues in HIV-1 protease”. Nature Structural Biology 3 (11): 946–50. (November 1996). doi:10.1038/nsb1196-946. PMID 8901873.
“A combined quantum/classical molecular dynamics study of the catalytic mechanism of HIV protease”. Journal of Molecular Biology 261 (3): 454–69. (August 1996). doi:10.1006/jmbi.1996.0476. PMID 8780786.
“Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor”. Biochemistry 30 (6): 1600–9. (February 1991). doi:10.1021/bi00220a023. PMID 1993177.
“Influence of drug transport proteins on the pharmacokinetics and drug interactions of HIV protease inhibitors”. Journal of Pharmaceutical Sciences 100 (9): 3636–54. (September 2011). doi:10.1002/jps.22655. PMC 3750718. PMID 21698598.
“Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors”. Antimicrobial Agents and Chemotherapy 47 (2): 759–69. (February 2003). doi:10.1128/AAC.47.2.759-769.2003. PMC 151730. PMID 12543689.
“Complete mutagenesis of the HIV-1 protease”. Nature 340 (6232): 397–400. (August 1989). Bibcode: 1989Natur.340..397L. doi:10.1038/340397a0. PMID 2666861.
“New targets for inhibitors of HIV-1 replication”. Nature Reviews. Molecular Cell Biology 1 (1): 40–9. (October 2000). doi:10.1038/35036060. PMID 11413488.
“The design of drugs for HIV and HCV”. Nature Reviews. Drug Discovery 6 (12): 1001–18. (December 2007). doi:10.1038/nrd2424. PMID 18049474.

harvard.edu

ui.adsabs.harvard.edu

“Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides”. Proceedings of the National Academy of Sciences of the United States of America 86 (3): 807–11. (February 1989). Bibcode: 1989PNAS...86..807K. doi:10.1073/pnas.86.3.807. PMC 286566. PMID 2644644.
“Active human immunodeficiency virus protease is required for viral infectivity”. Proceedings of the National Academy of Sciences of the United States of America 85 (13): 4686–90. (July 1988). Bibcode: 1988PNAS...85.4686K. doi:10.1073/pnas.85.13.4686. PMC 280500. PMID 3290901.
“Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein”. Proceedings of the National Academy of Sciences of the United States of America 91 (17): 7970–4. (August 1994). Bibcode: 1994PNAS...91.7970L. doi:10.1073/pnas.91.17.7970. PMC 44526. PMID 8058744.
“Complete mutagenesis of the HIV-1 protease”. Nature 340 (6232): 397–400. (August 1989). Bibcode: 1989Natur.340..397L. doi:10.1038/340397a0. PMID 2666861.

nih.gov

pubmed.ncbi.nlm.nih.gov

“The structure and function of the aspartic proteinases”. Annual Review of Biophysics and Biophysical Chemistry 19 (1): 189–215. (1990). doi:10.1146/annurev.bb.19.060190.001201. PMID 2194475. https://zenodo.org/record/1234933.
“HIV-1 protease: mechanism and drug discovery”. Organic & Biomolecular Chemistry 1 (1): 5–14. (January 2003). doi:10.1039/b208248a. PMID 12929379.
“The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics”. The Journal of Biological Chemistry 289 (24): 17203–14. (June 2014). doi:10.1074/jbc.M114.571836. PMC 4059161. PMID 24742668.
“HIV protease inhibitors: a review of molecular selectivity and toxicity” (英語). HIV/AIDS: Research and Palliative Care 7: 95–104. (April 2015). doi:10.2147/hiv.s79956. PMC 4396582. PMID 25897264.
“Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides”. Proceedings of the National Academy of Sciences of the United States of America 86 (3): 807–11. (February 1989). Bibcode: 1989PNAS...86..807K. doi:10.1073/pnas.86.3.807. PMC 286566. PMID 2644644.
“Active human immunodeficiency virus protease is required for viral infectivity”. Proceedings of the National Academy of Sciences of the United States of America 85 (13): 4686–90. (July 1988). Bibcode: 1988PNAS...85.4686K. doi:10.1073/pnas.85.13.4686. PMC 280500. PMID 3290901.
“HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs”. Protein Science 13 (4): 1108–23. (April 2004). doi:10.1110/ps.03468904. PMC 2280056. PMID 15044738. オリジナルの2008-12-16時点におけるアーカイブ。.
“Folding regulates autoprocessing of HIV-1 protease precursor”. The Journal of Biological Chemistry 280 (12): 11369–78. (March 2005). doi:10.1074/jbc.M412603200. PMID 15632156.
“Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism”. Journal of Virology 78 (16): 8477–85. (August 2004). doi:10.1128/JVI.78.16.8477-8485.2004. PMC 479095. PMID 15280456.
“Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution”. Science 246 (4934): 1149–52. (December 1989). doi:10.1126/science.2686029. PMID 2686029.
“Autoprocessing of HIV-1 protease is tightly coupled to protein folding”. Nature Structural Biology 6 (9): 868–75. (September 1999). doi:10.1038/12327. PMID 10467100.
“Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein”. Proceedings of the National Academy of Sciences of the United States of America 91 (17): 7970–4. (August 1994). Bibcode: 1994PNAS...91.7970L. doi:10.1073/pnas.91.17.7970. PMC 44526. PMID 8058744.
“A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation”. The Journal of Biological Chemistry 271 (8): 4477–81. (February 1996). doi:10.1074/jbc.271.8.4477. PMID 8626801.
“HIV-1 protease function and structure studies with the simplicial neighborhood analysis of protein packing method”. Proteins 73 (3): 742–53. (November 2008). doi:10.1002/prot.22094. PMC 2765824. PMID 18498108.
“Understanding HIV-1 protease autoprocessing for novel therapeutic development”. Future Medicinal Chemistry 5 (11): 1215–29. (July 2013). doi:10.4155/fmc.13.89. PMC 3826259. PMID 23859204.
“Ionization states of the catalytic residues in HIV-1 protease”. Nature Structural Biology 3 (11): 946–50. (November 1996). doi:10.1038/nsb1196-946. PMID 8901873.
“A combined quantum/classical molecular dynamics study of the catalytic mechanism of HIV protease”. Journal of Molecular Biology 261 (3): 454–69. (August 1996). doi:10.1006/jmbi.1996.0476. PMID 8780786.
“Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor”. Biochemistry 30 (6): 1600–9. (February 1991). doi:10.1021/bi00220a023. PMID 1993177.
“Influence of drug transport proteins on the pharmacokinetics and drug interactions of HIV protease inhibitors”. Journal of Pharmaceutical Sciences 100 (9): 3636–54. (September 2011). doi:10.1002/jps.22655. PMC 3750718. PMID 21698598.
“Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors”. Antimicrobial Agents and Chemotherapy 47 (2): 759–69. (February 2003). doi:10.1128/AAC.47.2.759-769.2003. PMC 151730. PMID 12543689.
“Complete mutagenesis of the HIV-1 protease”. Nature 340 (6232): 397–400. (August 1989). Bibcode: 1989Natur.340..397L. doi:10.1038/340397a0. PMID 2666861.
“New targets for inhibitors of HIV-1 replication”. Nature Reviews. Molecular Cell Biology 1 (1): 40–9. (October 2000). doi:10.1038/35036060. PMID 11413488.
“The design of drugs for HIV and HCV”. Nature Reviews. Drug Discovery 6 (12): 1001–18. (December 2007). doi:10.1038/nrd2424. PMID 18049474.

pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

“The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics”. The Journal of Biological Chemistry 289 (24): 17203–14. (June 2014). doi:10.1074/jbc.M114.571836. PMC 4059161. PMID 24742668.
“HIV protease inhibitors: a review of molecular selectivity and toxicity” (英語). HIV/AIDS: Research and Palliative Care 7: 95–104. (April 2015). doi:10.2147/hiv.s79956. PMC 4396582. PMID 25897264.
“Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides”. Proceedings of the National Academy of Sciences of the United States of America 86 (3): 807–11. (February 1989). Bibcode: 1989PNAS...86..807K. doi:10.1073/pnas.86.3.807. PMC 286566. PMID 2644644.
“Active human immunodeficiency virus protease is required for viral infectivity”. Proceedings of the National Academy of Sciences of the United States of America 85 (13): 4686–90. (July 1988). Bibcode: 1988PNAS...85.4686K. doi:10.1073/pnas.85.13.4686. PMC 280500. PMID 3290901.
“Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism”. Journal of Virology 78 (16): 8477–85. (August 2004). doi:10.1128/JVI.78.16.8477-8485.2004. PMC 479095. PMID 15280456.
“Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein”. Proceedings of the National Academy of Sciences of the United States of America 91 (17): 7970–4. (August 1994). Bibcode: 1994PNAS...91.7970L. doi:10.1073/pnas.91.17.7970. PMC 44526. PMID 8058744.
“HIV-1 protease function and structure studies with the simplicial neighborhood analysis of protein packing method”. Proteins 73 (3): 742–53. (November 2008). doi:10.1002/prot.22094. PMC 2765824. PMID 18498108.
“Understanding HIV-1 protease autoprocessing for novel therapeutic development”. Future Medicinal Chemistry 5 (11): 1215–29. (July 2013). doi:10.4155/fmc.13.89. PMC 3826259. PMID 23859204.
“Influence of drug transport proteins on the pharmacokinetics and drug interactions of HIV protease inhibitors”. Journal of Pharmaceutical Sciences 100 (9): 3636–54. (September 2011). doi:10.1002/jps.22655. PMC 3750718. PMID 21698598.
“Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors”. Antimicrobial Agents and Chemotherapy 47 (2): 759–69. (February 2003). doi:10.1128/AAC.47.2.759-769.2003. PMC 151730. PMID 12543689.

stanford.edu

ai.stanford.edu

“HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs”. Protein Science 13 (4): 1108–23. (April 2004). doi:10.1110/ps.03468904. PMC 2280056. PMID 15044738. オリジナルの2008-12-16時点におけるアーカイブ。.

web.archive.org

“HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs”. Protein Science 13 (4): 1108–23. (April 2004). doi:10.1110/ps.03468904. PMC 2280056. PMID 15044738. オリジナルの2008-12-16時点におけるアーカイブ。.

zenodo.org

“The structure and function of the aspartic proteinases”. Annual Review of Biophysics and Biophysical Chemistry 19 (1): 189–215. (1990). doi:10.1146/annurev.bb.19.060190.001201. PMID 2194475. https://zenodo.org/record/1234933.