214 related articles for article (PubMed ID: 11396919)
1. The binding energetics of first- and second-generation HIV-1 protease inhibitors: implications for drug design.
Velazquez-Campoy A; Kiso Y; Freire E
Arch Biochem Biophys; 2001 Jun; 390(2):169-75. PubMed ID: 11396919
[TBL] [Abstract][Full Text] [Related]
2. A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease.
Vega S; Kang LW; Velazquez-Campoy A; Kiso Y; Amzel LM; Freire E
Proteins; 2004 May; 55(3):594-602. PubMed ID: 15103623
[TBL] [Abstract][Full Text] [Related]
3. Multidrug resistance to HIV-1 protease inhibition requires cooperative coupling between distal mutations.
Ohtaka H; Schön A; Freire E
Biochemistry; 2003 Nov; 42(46):13659-66. PubMed ID: 14622012
[TBL] [Abstract][Full Text] [Related]
4. A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance.
Muzammil S; Ross P; Freire E
Biochemistry; 2003 Jan; 42(3):631-8. PubMed ID: 12534275
[TBL] [Abstract][Full Text] [Related]
5. Overcoming drug resistance in HIV-1 chemotherapy: the binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug-resistant mutants of the HIV-1 protease.
Ohtaka H; Velázquez-Campoy A; Xie D; Freire E
Protein Sci; 2002 Aug; 11(8):1908-16. PubMed ID: 12142445
[TBL] [Abstract][Full Text] [Related]
6. Importance of polar solvation and configurational entropy for design of antiretroviral drugs targeting HIV-1 protease.
Kar P; Lipowsky R; Knecht V
J Phys Chem B; 2013 May; 117(19):5793-805. PubMed ID: 23614718
[TBL] [Abstract][Full Text] [Related]
7. Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes.
Velazquez-Campoy A; Vega S; Freire E
Biochemistry; 2002 Jul; 41(27):8613-9. PubMed ID: 12093278
[TBL] [Abstract][Full Text] [Related]
8. Thermodynamic basis of resistance to HIV-1 protease inhibition: calorimetric analysis of the V82F/I84V active site resistant mutant.
Todd MJ; Luque I; Velázquez-Campoy A; Freire E
Biochemistry; 2000 Oct; 39(39):11876-83. PubMed ID: 11009599
[TBL] [Abstract][Full Text] [Related]
9. Compensating enthalpic and entropic changes hinder binding affinity optimization.
Lafont V; Armstrong AA; Ohtaka H; Kiso Y; Mario Amzel L; Freire E
Chem Biol Drug Des; 2007 Jun; 69(6):413-22. PubMed ID: 17581235
[TBL] [Abstract][Full Text] [Related]
10. Resistance to HIV protease inhibitors: a comparison of enzyme inhibition and antiviral potency.
Klabe RM; Bacheler LT; Ala PJ; Erickson-Viitanen S; Meek JL
Biochemistry; 1998 Jun; 37(24):8735-42. PubMed ID: 9628735
[TBL] [Abstract][Full Text] [Related]
11. Optimization and computational evaluation of a series of potential active site inhibitors of the V82F/I84V drug-resistant mutant of HIV-1 protease: an application of the relaxed complex method of structure-based drug design.
Perryman AL; Lin JH; Andrew McCammon J
Chem Biol Drug Des; 2006 May; 67(5):336-45. PubMed ID: 16784458
[TBL] [Abstract][Full Text] [Related]
12. Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets.
Ohtaka H; Muzammil S; Schön A; Velazquez-Campoy A; Vega S; Freire E
Int J Biochem Cell Biol; 2004 Sep; 36(9):1787-99. PubMed ID: 15183345
[TBL] [Abstract][Full Text] [Related]
13. Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: mechanism for binding and drug resistance.
Hou T; Yu R
J Med Chem; 2007 Mar; 50(6):1177-88. PubMed ID: 17300185
[TBL] [Abstract][Full Text] [Related]
14. Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor.
Velazquez-Campoy A; Luque I; Todd MJ; Milutinovich M; Kiso Y; Freire E
Protein Sci; 2000 Sep; 9(9):1801-9. PubMed ID: 11045625
[TBL] [Abstract][Full Text] [Related]
15. Some insights into mechanism for binding and drug resistance of wild type and I50V V82A and I84V mutations in HIV-1 protease with GRL-98065 inhibitor from molecular dynamic simulations.
Hu GD; Zhu T; Zhang SL; Wang D; Zhang QG
Eur J Med Chem; 2010 Jan; 45(1):227-35. PubMed ID: 19910081
[TBL] [Abstract][Full Text] [Related]
16. Comparative studies on inhibitors of HIV protease: a target for drug design.
Jayaraman S; Shah K
In Silico Biol; 2008; 8(5-6):427-47. PubMed ID: 19374129
[TBL] [Abstract][Full Text] [Related]
17. Comparing the accumulation of active- and nonactive-site mutations in the HIV-1 protease.
Clemente JC; Moose RE; Hemrajani R; Whitford LR; Govindasamy L; Reutzel R; McKenna R; Agbandje-McKenna M; Goodenow MM; Dunn BM
Biochemistry; 2004 Sep; 43(38):12141-51. PubMed ID: 15379553
[TBL] [Abstract][Full Text] [Related]
18. Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants.
Kozísek M; Bray J; Rezácová P; Sasková K; Brynda J; Pokorná J; Mammano F; Rulísek L; Konvalinka J
J Mol Biol; 2007 Dec; 374(4):1005-16. PubMed ID: 17977555
[TBL] [Abstract][Full Text] [Related]
19. Molecular dynamic and free energy studies of primary resistance mutations in HIV-1 protease-ritonavir complexes.
Aruksakunwong O; Wolschann P; Hannongbua S; Sompornpisut P
J Chem Inf Model; 2006; 46(5):2085-92. PubMed ID: 16995739
[TBL] [Abstract][Full Text] [Related]
20. Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV.
Jadhav PK; Ala P; Woerner FJ; Chang CH; Garber SS; Anton ED; Bacheler LT
J Med Chem; 1997 Jan; 40(2):181-91. PubMed ID: 9003516
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
