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HIV Protease mutants

S. V. Gulnik, L. I. Suvorov, B. Liu, B. Yu, B. Anderson, H. Mitsuya, J. W. Erickson, Kinetic Characterization and Cross-Resistance Patterns of HIV-1 Protease Mutants Selected under Drug Pressure , Biochemisry 1995, 34, 9282-9287. [Pg.368]

Gulnik SV, Suvorov LI, Liu B, Yu B, Anderson B, Mitsuya H, Erickson JW. Kinetic characterization and cross-resistance patters of HIV-1 protease mutants selected under in vitro drug pressure. Biochemistry 1995 34 9282-9287. [Pg.40]

Schaffer, L. and Verkhivker, G. M. (1998) Predicting structural effects in HIV-1 protease mutant complexes with flexible ligand docking and protein side-chain optimization. Proteins Struct. Fund. Gen. 33,295-310. [Pg.91]

Gulnik, S. V., Suvorov, L. L, Liu, B. et al. 1995. Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure. Biochemistry 34(29) 9282-9287. [Pg.68]

Kovalevsky, A. Y, Liu, R, Leshchenko, S. et al. 2006. Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114. J. Mol. Biol. 363 161-173. [Pg.68]

Chen, Z., Li, Y, Schock, H. B., et al., 1995. Three-dimensional structure of a mutant HIV-1 protease displaying cros.s-resi.stance to all protease inhibitors in clinical txiAs. Journal of Biological Chemistry 270 21433-21436. [Pg.532]

J ,3J ,4J ,5J )-2,5-bis(benzyloxy)-3,4-dihydroxy-Nd -bis (lS)-2-methyl-l-[(methylamino)carbonyl]propyl hexanediamide is a C2-symmetric HIV-1 protease inhibitor [29]. Derivatization in the para positions of the benzyl-oxy groups via microwave-assisted Stille reaction on the corresponding di-brominated inhibitor smoothly yielded the desired heteroarylated derivatives (Scheme 10). Interestingly, the 1,3-thiazole derivative showed a higher antiviral activity on the wild type virus than the lead compound. The activity remained at the same level in the presence of seriun. Unfortimately, a low activity was observed on mutants. [Pg.161]

Allaire M, Chernaia MM, Malcolm BA, James MN (1994) Picomaviral 3C cysteine proteinases have a fold similar to chymotrypsin-Kke serine proteinases. Nature 369 72-76 Altman MD, Nalivaika EA, Prabu-Jeyabalan M, Schiffer CA, Tidor B (2008) Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease. Proteins 70 678-694... [Pg.103]

L. Hong, A. Treharne, J. A. Hartsuck, S. Foundling, J. Tang, Crystal Structures of Complexes of a Peptidic Inhibitor with Wild Type and Two Mutants HIV-1 Proteases , Biochemistry 1996, 35, 10627-10633. [Pg.60]

The growing body of structural and thermodynamic data has revealed similarities and differences in molecular origins for inhibitors specificity against HIV-1 protease and its various mutant forms. The crystal structures of three... [Pg.294]

A widely accepted two-step mechanism of HIV-1 protease binding implies the creation of a loose complex with the open form of the enzyme, followed by the conformational change involving the closure of the flap region over the active site and formation of the final bound complex. Consequently, binding affinity differences between the HIV-1 protease and its mutants may also result from the changes in the internal equilibrium between the bound form of the protease with closed flaps conformation and the unbound open form... [Pg.297]

Ohtaka, H., Veldzquez-Campoy, A., Xie, D., Freire, E. Overcoming drug resistance in HIV-1 chemotherapy the binding thermodynamics of Amprenavir and TMC-126 to wild-type and drag resistant mutants of the HIV-1 protease. Protein Science. 2002,11, 1908-1916. [Pg.634]

Todd, M. J., Luque, I., Velazquez-Campoy, A., and Freire, E. (2000) Thermodynamic basis of resistance to HIV-1 protease inhibition Calorimetric analysis of the V82F/ I84V active site resistant mutant. Biochemistry 39,11876-11883. [Pg.150]

Bannwarth L, Reboud-Ravaux M (2007) An alternative strategy for inhibiting multidrug-resistant mutants of the dimeric HIV-1 protease by targeting the subunit interface. Biochem Soc Trans 35 551-554... [Pg.164]


See other pages where HIV Protease mutants is mentioned: [Pg.294]    [Pg.296]    [Pg.298]    [Pg.312]    [Pg.312]    [Pg.319]    [Pg.321]    [Pg.322]    [Pg.325]    [Pg.327]    [Pg.73]    [Pg.294]    [Pg.296]    [Pg.298]    [Pg.312]    [Pg.312]    [Pg.319]    [Pg.321]    [Pg.322]    [Pg.325]    [Pg.327]    [Pg.73]    [Pg.206]    [Pg.207]    [Pg.507]    [Pg.516]    [Pg.252]    [Pg.50]    [Pg.483]    [Pg.220]    [Pg.235]    [Pg.30]    [Pg.32]    [Pg.40]    [Pg.168]    [Pg.294]    [Pg.295]    [Pg.303]    [Pg.305]    [Pg.306]    [Pg.313]    [Pg.313]    [Pg.577]    [Pg.225]    [Pg.140]   
See also in sourсe #XX -- [ Pg.295 , Pg.321 ]




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