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Journal Abstract Search
262 related items for PubMed ID: 8967903
1. Triterpenes as potential dimerization inhibitors of HIV-1 protease. Quéré L, Wenger T, Schramm HJ. Biochem Biophys Res Commun; 1996 Oct 14; 227(2):484-8. PubMed ID: 8967903 [Abstract] [Full Text] [Related]
2. The inhibition of HIV-1 protease by interface peptides. Schramm HJ, Billich A, Jaeger E, Rücknagel KP, Arnold G, Schramm W. Biochem Biophys Res Commun; 1993 Jul 30; 194(2):595-600. PubMed ID: 8343146 [Abstract] [Full Text] [Related]
3. A folding inhibitor of the HIV-1 protease. Broglia RA, Provasi D, Vasile F, Ottolina G, Longhi R, Tiana G. Proteins; 2006 Mar 01; 62(4):928-33. PubMed ID: 16385559 [Abstract] [Full Text] [Related]
12. Dimerization inhibitors of HIV-1 protease. Boggetto N, Reboud-Ravaux M. Biol Chem; 2002 Sep 01; 383(9):1321-4. PubMed ID: 12437124 [Abstract] [Full Text] [Related]
13. Sidechain-linked inhibitors of HIV-1 protease dimerization. Bowman MJ, Chmielewski J. Bioorg Med Chem; 2009 Feb 01; 17(3):967-76. PubMed ID: 18337105 [Abstract] [Full Text] [Related]
14. Small-molecule dimerization inhibitors of wild-type and mutant HIV protease: a focused library approach. Shultz MD, Ham YW, Lee SG, Davis DA, Brown C, Chmielewski J. J Am Chem Soc; 2004 Aug 18; 126(32):9886-7. PubMed ID: 15303839 [Abstract] [Full Text] [Related]
15. Synthesis of dammarane-type triterpene derivatives and their ability to inhibit HIV and HCV proteases. Wei Y, Ma CM, Hattori M. Bioorg Med Chem; 2009 Apr 15; 17(8):3003-10. PubMed ID: 19339186 [Abstract] [Full Text] [Related]
16. Anti-HIV triterpene acids from Geum japonicum. Xu HX, Zeng FQ, Wan M, Sim KY. J Nat Prod; 1996 Jul 15; 59(7):643-5. PubMed ID: 8759159 [Abstract] [Full Text] [Related]
17. Inhibition of HIV-1 protease by short peptides derived from the terminal segments of the protease. Schramm HJ, Breipohl G, Hansen J, Henke S, Jaeger E, Meichsner C, Riess G, Ruppert D, Rücknagel KP, Schäfer W. Biochem Biophys Res Commun; 1992 Apr 30; 184(2):980-5. PubMed ID: 1575762 [Abstract] [Full Text] [Related]
18. Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272. Wang YX, Freedberg DI, Yamazaki T, Wingfield PT, Stahl SJ, Kaufman JD, Kiso Y, Torchia DA. Biochemistry; 1996 Aug 06; 35(31):9945-50. PubMed ID: 8756455 [Abstract] [Full Text] [Related]