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HIV-1 proteáza (Czech Wikipedia)

Analysis of information sources in references of the Wikipedia article "HIV-1 proteáza" in Czech language version.

refsWebsite
Global rank Czech rank
22doi.org
2nd place
4th place
22nih.gov
4th place
8th place
5semanticscholar.org
11th place
313th place
4harvard.edu
18th place
99th place
1zenodo.org
621st place
2,192nd place

doi.org

dx.doi.org

  • Davies DR. The structure and function of the aspartic proteinases. Annual Review of Biophysics and Biophysical Chemistry. 1990, s. 189–215. Dostupné online. DOI 10.1146/annurev.bb.19.060190.001201. PMID 2194475. 
  • Brik A, Wong CH. HIV-1 protease: mechanism and drug discovery. Organic & Biomolecular Chemistry. January 2003, s. 5–14. DOI 10.1039/b208248a. PMID 12929379. 
  • Huang X, Britto MD, Kear-Scott JL, Boone CD, Rocca JR, Simmerling C, Mckenna R, Bieri M, Gooley PR, Dunn BM, Fanucci GE. The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics. The Journal of Biological Chemistry. June 2014, s. 17203–14. DOI 10.1074/jbc.M114.571836. PMID 24742668. 
  • Lv Z, Chu Y, Wang Y. HIV protease inhibitors: a review of molecular selectivity and toxicity. HIV/AIDS: Research and Palliative Care. April 2015, s. 95–104. DOI 10.2147/hiv.s79956. PMID 25897264. (anglicky) 
  • Kräusslich HG, Ingraham RH, Skoog MT, Wimmer E, Pallai PV, Carter CA. 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. February 1989, s. 807–11. DOI 10.1073/pnas.86.3.807. PMID 2644644. Bibcode 1989PNAS...86..807K. 
  • Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RA, Scolnick EM, Sigal IS. Active human immunodeficiency virus protease is required for viral infectivity. Proceedings of the National Academy of Sciences of the United States of America. July 1988, s. 4686–90. DOI 10.1073/pnas.85.13.4686. PMID 3290901. Bibcode 1988PNAS...85.4686K. 
  • Chatterjee A, Mridula P, Mishra RK, Mittal R, Hosur RV. Folding regulates autoprocessing of HIV-1 protease precursor. The Journal of Biological Chemistry. March 2005, s. 11369–78. DOI 10.1074/jbc.M412603200. PMID 15632156. 
  • Pettit SC, Everitt LE, Choudhury S, Dunn BM, Kaplan AH. Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism. Journal of Virology. August 2004, s. 8477–85. DOI 10.1128/JVI.78.16.8477-8485.2004. PMID 15280456. 
  • Miller M, Schneider J, Sathyanarayana BK, Toth MV, Marshall GR, Clawson L, Selk L, Kent SB, Wlodawer A. Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution. Science. December 1989, s. 1149–52. DOI 10.1126/science.2686029. PMID 2686029. 
  • Louis JM, Clore GM, Gronenborn AM. Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nature Structural Biology. September 1999, s. 868–75. DOI 10.1038/12327. PMID 10467100. S2CID 6375519. (En) 
  • Huang L, Chen C. Understanding HIV-1 protease autoprocessing for novel therapeutic development. Future Medicinal Chemistry. July 2013, s. 1215–29. DOI 10.4155/fmc.13.89. PMID 23859204. 
  • Louis JM, Nashed NT, Parris KD, Kimmel AR, Jerina DM. 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. August 1994, s. 7970–4. DOI 10.1073/pnas.91.17.7970. PMID 8058744. Bibcode 1994PNAS...91.7970L. 
  • Wondrak EM, Nashed NT, Haber MT, Jerina DM, Louis JM. A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation. The Journal of Biological Chemistry. February 1996, s. 4477–81. DOI 10.1074/jbc.271.8.4477. PMID 8626801. 
  • Zhang S, Kaplan AH, Tropsha A. HIV-1 protease function and structure studies with the simplicial neighborhood analysis of protein packing method. Proteins. November 2008, s. 742–53. DOI 10.1002/prot.22094. PMID 18498108. 
  • Smith R, Brereton IM, Chai RY, Kent SB. Ionization states of the catalytic residues in HIV-1 protease. Nature Structural Biology. November 1996, s. 946–50. DOI 10.1038/nsb1196-946. PMID 8901873. S2CID 1076528. 
  • Liu H, Müller-Plathe F, van Gunsteren WF. A combined quantum/classical molecular dynamics study of the catalytic mechanism of HIV protease. Journal of Molecular Biology. August 1996, s. 454–69. DOI 10.1006/jmbi.1996.0476. PMID 8780786. 
  • Jaskólski M, Tomasselli AG, Sawyer TK, Staples DG, Heinrikson RL, Schneider J, Kent SB, Wlodawer A. Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor. Biochemistry. February 1991, s. 1600–9. DOI 10.1021/bi00220a023. PMID 1993177. 
  • Griffin L, Annaert P, Brouwer KL. Influence of drug transport proteins on the pharmacokinetics and drug interactions of HIV protease inhibitors. Journal of Pharmaceutical Sciences. September 2011, s. 3636–54. DOI 10.1002/jps.22655. PMID 21698598. 
  • Watkins T, Resch W, Irlbeck D, Swanstrom R. Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors. Antimicrobial Agents and Chemotherapy. February 2003, s. 759–69. DOI 10.1128/AAC.47.2.759-769.2003. PMID 12543689. 
  • Loeb DD, Swanstrom R, Everitt L, Manchester M, Stamper SE, Hutchison CA. Complete mutagenesis of the HIV-1 protease. Nature. August 1989, s. 397–400. DOI 10.1038/340397a0. PMID 2666861. S2CID 4351388. Bibcode 1989Natur.340..397L. (En) 
  • Moore JP, Stevenson M. New targets for inhibitors of HIV-1 replication. Nature Reviews. Molecular Cell Biology. October 2000, s. 40–9. DOI 10.1038/35036060. PMID 11413488. S2CID 10811618. 
  • Moore JP, Stevenson M. New targets for inhibitors of HIV-1 replication. Nature Reviews. Molecular Cell Biology. October 2000, s. 40–9. DOI 10.1038/35036060. PMID 11413488. S2CID 10811618. 

harvard.edu

adsabs.harvard.edu

  • Kräusslich HG, Ingraham RH, Skoog MT, Wimmer E, Pallai PV, Carter CA. 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. February 1989, s. 807–11. DOI 10.1073/pnas.86.3.807. PMID 2644644. Bibcode 1989PNAS...86..807K. 
  • Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RA, Scolnick EM, Sigal IS. Active human immunodeficiency virus protease is required for viral infectivity. Proceedings of the National Academy of Sciences of the United States of America. July 1988, s. 4686–90. DOI 10.1073/pnas.85.13.4686. PMID 3290901. Bibcode 1988PNAS...85.4686K. 
  • Louis JM, Nashed NT, Parris KD, Kimmel AR, Jerina DM. 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. August 1994, s. 7970–4. DOI 10.1073/pnas.91.17.7970. PMID 8058744. Bibcode 1994PNAS...91.7970L. 
  • Loeb DD, Swanstrom R, Everitt L, Manchester M, Stamper SE, Hutchison CA. Complete mutagenesis of the HIV-1 protease. Nature. August 1989, s. 397–400. DOI 10.1038/340397a0. PMID 2666861. S2CID 4351388. Bibcode 1989Natur.340..397L. (En) 

nih.gov

ncbi.nlm.nih.gov

  • Davies DR. The structure and function of the aspartic proteinases. Annual Review of Biophysics and Biophysical Chemistry. 1990, s. 189–215. Dostupné online. DOI 10.1146/annurev.bb.19.060190.001201. PMID 2194475. 
  • Brik A, Wong CH. HIV-1 protease: mechanism and drug discovery. Organic & Biomolecular Chemistry. January 2003, s. 5–14. DOI 10.1039/b208248a. PMID 12929379. 
  • Huang X, Britto MD, Kear-Scott JL, Boone CD, Rocca JR, Simmerling C, Mckenna R, Bieri M, Gooley PR, Dunn BM, Fanucci GE. The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics. The Journal of Biological Chemistry. June 2014, s. 17203–14. DOI 10.1074/jbc.M114.571836. PMID 24742668. 
  • Lv Z, Chu Y, Wang Y. HIV protease inhibitors: a review of molecular selectivity and toxicity. HIV/AIDS: Research and Palliative Care. April 2015, s. 95–104. DOI 10.2147/hiv.s79956. PMID 25897264. (anglicky) 
  • Kräusslich HG, Ingraham RH, Skoog MT, Wimmer E, Pallai PV, Carter CA. 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. February 1989, s. 807–11. DOI 10.1073/pnas.86.3.807. PMID 2644644. Bibcode 1989PNAS...86..807K. 
  • Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RA, Scolnick EM, Sigal IS. Active human immunodeficiency virus protease is required for viral infectivity. Proceedings of the National Academy of Sciences of the United States of America. July 1988, s. 4686–90. DOI 10.1073/pnas.85.13.4686. PMID 3290901. Bibcode 1988PNAS...85.4686K. 
  • Chatterjee A, Mridula P, Mishra RK, Mittal R, Hosur RV. Folding regulates autoprocessing of HIV-1 protease precursor. The Journal of Biological Chemistry. March 2005, s. 11369–78. DOI 10.1074/jbc.M412603200. PMID 15632156. 
  • Pettit SC, Everitt LE, Choudhury S, Dunn BM, Kaplan AH. Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism. Journal of Virology. August 2004, s. 8477–85. DOI 10.1128/JVI.78.16.8477-8485.2004. PMID 15280456. 
  • Miller M, Schneider J, Sathyanarayana BK, Toth MV, Marshall GR, Clawson L, Selk L, Kent SB, Wlodawer A. Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution. Science. December 1989, s. 1149–52. DOI 10.1126/science.2686029. PMID 2686029. 
  • Louis JM, Clore GM, Gronenborn AM. Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nature Structural Biology. September 1999, s. 868–75. DOI 10.1038/12327. PMID 10467100. S2CID 6375519. (En) 
  • Huang L, Chen C. Understanding HIV-1 protease autoprocessing for novel therapeutic development. Future Medicinal Chemistry. July 2013, s. 1215–29. DOI 10.4155/fmc.13.89. PMID 23859204. 
  • Louis JM, Nashed NT, Parris KD, Kimmel AR, Jerina DM. 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. August 1994, s. 7970–4. DOI 10.1073/pnas.91.17.7970. PMID 8058744. Bibcode 1994PNAS...91.7970L. 
  • Wondrak EM, Nashed NT, Haber MT, Jerina DM, Louis JM. A transient precursor of the HIV-1 protease. Isolation, characterization, and kinetics of maturation. The Journal of Biological Chemistry. February 1996, s. 4477–81. DOI 10.1074/jbc.271.8.4477. PMID 8626801. 
  • Zhang S, Kaplan AH, Tropsha A. HIV-1 protease function and structure studies with the simplicial neighborhood analysis of protein packing method. Proteins. November 2008, s. 742–53. DOI 10.1002/prot.22094. PMID 18498108. 
  • Smith R, Brereton IM, Chai RY, Kent SB. Ionization states of the catalytic residues in HIV-1 protease. Nature Structural Biology. November 1996, s. 946–50. DOI 10.1038/nsb1196-946. PMID 8901873. S2CID 1076528. 
  • Liu H, Müller-Plathe F, van Gunsteren WF. A combined quantum/classical molecular dynamics study of the catalytic mechanism of HIV protease. Journal of Molecular Biology. August 1996, s. 454–69. DOI 10.1006/jmbi.1996.0476. PMID 8780786. 
  • Jaskólski M, Tomasselli AG, Sawyer TK, Staples DG, Heinrikson RL, Schneider J, Kent SB, Wlodawer A. Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor. Biochemistry. February 1991, s. 1600–9. DOI 10.1021/bi00220a023. PMID 1993177. 
  • Griffin L, Annaert P, Brouwer KL. Influence of drug transport proteins on the pharmacokinetics and drug interactions of HIV protease inhibitors. Journal of Pharmaceutical Sciences. September 2011, s. 3636–54. DOI 10.1002/jps.22655. PMID 21698598. 
  • Watkins T, Resch W, Irlbeck D, Swanstrom R. Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors. Antimicrobial Agents and Chemotherapy. February 2003, s. 759–69. DOI 10.1128/AAC.47.2.759-769.2003. PMID 12543689. 
  • Loeb DD, Swanstrom R, Everitt L, Manchester M, Stamper SE, Hutchison CA. Complete mutagenesis of the HIV-1 protease. Nature. August 1989, s. 397–400. DOI 10.1038/340397a0. PMID 2666861. S2CID 4351388. Bibcode 1989Natur.340..397L. (En) 
  • Moore JP, Stevenson M. New targets for inhibitors of HIV-1 replication. Nature Reviews. Molecular Cell Biology. October 2000, s. 40–9. DOI 10.1038/35036060. PMID 11413488. S2CID 10811618. 
  • Moore JP, Stevenson M. New targets for inhibitors of HIV-1 replication. Nature Reviews. Molecular Cell Biology. October 2000, s. 40–9. DOI 10.1038/35036060. PMID 11413488. S2CID 10811618. 

semanticscholar.org

api.semanticscholar.org

  • Louis JM, Clore GM, Gronenborn AM. Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nature Structural Biology. September 1999, s. 868–75. DOI 10.1038/12327. PMID 10467100. S2CID 6375519. (En) 
  • Smith R, Brereton IM, Chai RY, Kent SB. Ionization states of the catalytic residues in HIV-1 protease. Nature Structural Biology. November 1996, s. 946–50. DOI 10.1038/nsb1196-946. PMID 8901873. S2CID 1076528. 
  • Loeb DD, Swanstrom R, Everitt L, Manchester M, Stamper SE, Hutchison CA. Complete mutagenesis of the HIV-1 protease. Nature. August 1989, s. 397–400. DOI 10.1038/340397a0. PMID 2666861. S2CID 4351388. Bibcode 1989Natur.340..397L. (En) 
  • Moore JP, Stevenson M. New targets for inhibitors of HIV-1 replication. Nature Reviews. Molecular Cell Biology. October 2000, s. 40–9. DOI 10.1038/35036060. PMID 11413488. S2CID 10811618. 
  • Moore JP, Stevenson M. New targets for inhibitors of HIV-1 replication. Nature Reviews. Molecular Cell Biology. October 2000, s. 40–9. DOI 10.1038/35036060. PMID 11413488. S2CID 10811618. 

zenodo.org