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Active-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant.
Hong L, Hartsuck JA, Foundling S, Ermolieff J, Tang J. Hong L, et al. Among authors: tang j. Protein Sci. 1998 Feb;7(2):300-5. doi: 10.1002/pro.5560070209. Protein Sci. 1998. PMID: 9521105 Free PMC article.
Comparison of the mutant enzyme structure with that of the wild-type HIV-1 protease bound to the same inhibitor (Hong L, Treharne A, Hartsuck JA, Foundling S, Tang J, 1996, Biochemistry 35:10627-10633) revealed double occupancy for the Ser28 hydroxyl group, which fo …
Comparison of the mutant enzyme structure with that of the wild-type HIV-1 protease bound to the same inhibitor (Hong L, Treharne A, Hartsuc …
Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases.
Hong L, Treharne A, Hartsuck JA, Foundling S, Tang J. Hong L, et al. Among authors: tang j. Biochemistry. 1996 Aug 20;35(33):10627-33. doi: 10.1021/bi960481s. Biochemistry. 1996. PMID: 8718851
L., Thaisrivongs, S., Leelamanit, W., Raterman, D., Shah, M., Dunn, B.M., & Tang, J. (1995) Biochemistry 34, 1143-1152]. Unfavorable van der Waals interactions between the inhibitor and the mutated side chains at position 82 are consistent with diminished affini …
L., Thaisrivongs, S., Leelamanit, W., Raterman, D., Shah, M., Dunn, B.M., & Tang, J. (1995) Biochemistry 34, 1143-1152]. U …
Kinetic properties of saquinavir-resistant mutants of human immunodeficiency virus type 1 protease and their implications in drug resistance in vivo.
Ermolieff J, Lin X, Tang J. Ermolieff J, et al. Among authors: tang j. Biochemistry. 1997 Oct 7;36(40):12364-70. doi: 10.1021/bi971072e. Biochemistry. 1997. PMID: 9315877
Using a previously described kinetic model [Tang, J., & Hartsuck, J. A. (1995) FEBS Lett. 367, 112-116], the relative processing activities of HIV-1 protease variants were estimated in the saquinavir concentration range of 0-10(-7) M. ...
Using a previously described kinetic model [Tang, J., & Hartsuck, J. A. (1995) FEBS Lett. 367, 112-116], the relati …
Crystal structure of an in vivo HIV-1 protease mutant in complex with saquinavir: insights into the mechanisms of drug resistance.
Hong L, Zhang XC, Hartsuck JA, Tang J. Hong L, et al. Among authors: tang j. Protein Sci. 2000 Oct;9(10):1898-904. doi: 10.1110/ps.9.10.1898. Protein Sci. 2000. PMID: 11106162 Free PMC article.
Kinetic studies on these mutants demonstrate a 13.5-, 3-, and 419-fold increase in Ki values, respectively, compared to the wild-type enzyme (Ermolieff J, Lin X, Tang J, 1997, Biochemistry 36:12364-12370). To gain an understanding of how these mutations modul …
Kinetic studies on these mutants demonstrate a 13.5-, 3-, and 419-fold increase in Ki values, respectively, compared to the wild-type enzyme …
pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants.
Lin Y, Fusek M, Lin X, Hartsuck JA, Kezdy FJ, Tang J. Lin Y, et al. Among authors: tang j. J Biol Chem. 1992 Sep 15;267(26):18413-8. J Biol Chem. 1992. PMID: 1526982 Free article.
The pKe1 of rhizopuspepsin (2.8) is near that of a normal carboxyl group and near the pKe1 of human immunodeficiency virus type 1 (HIV-1) protease (3.32) (Ido, E., Han, H. P., Kezdy, F. J., and Tang, J. (1991) J. Biol. Chem. 266, 24359-24366). The pKe1 …
The pKe1 of rhizopuspepsin (2.8) is near that of a normal carboxyl group and near the pKe1 of human immunodeficiency virus type 1 (HIV-1) pr …
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