Mao B - Search Results

1

Lysine/fibrin binding sites of kringles modeled after the structure of kringle 1 of prothrombin.

Tulinsky A, Park CH, Mao B, Llinás M. Tulinsky A, et al. Among authors: mao b. Proteins. 1988;3(2):85-96. doi: 10.1002/prot.340030203. Proteins. 1988. PMID: 3135547

2

Solution structures of stromelysin complexed to thiadiazole inhibitors.

Stockman BJ, Waldon DJ, Gates JA, Scahill TA, Kloosterman DA, Mizsak SA, Jacobsen EJ, Belonga KL, Mitchell MA, Mao B, Petke JD, Goodman L, Powers EA, Ledbetter SR, Kaytes PS, Vogeli G, Marshall VP, Petzold GL, Poorman RA. Stockman BJ, et al. Among authors: mao b. Protein Sci. 1998 Nov;7(11):2281-6. doi: 10.1002/pro.5560071105. Protein Sci. 1998. PMID: 9827994 Free PMC article.

3

Theoretical and empirical approaches to protein-structure prediction and analysis.

Maggiora GM, Mao B, Chou KC, Narasimhan SL. Maggiora GM, et al. Among authors: mao b. Methods Biochem Anal. 1991;35:1-86. doi: 10.1002/9780470110560.ch1. Methods Biochem Anal. 1991. PMID: 2002769 Review. No abstract available.

4

Mass-weighted molecular dynamics simulation of cyclic polypeptides.

Mao B, Maggiora GM, Chou KC. Mao B, et al. Biopolymers. 1991 Aug;31(9):1077-86. doi: 10.1002/bip.360310907. Biopolymers. 1991. PMID: 1786339

5

Mass-weighted molecular dynamics simulation and conformational analysis of polypeptide.

Mao B. Mao B. Biophys J. 1991 Sep;60(3):611-22. doi: 10.1016/S0006-3495(91)82090-2. Biophys J. 1991. PMID: 1932551 Free PMC article.

6

Mass-weighted molecular dynamics simulation of the protein-ligand complex of rhizopuspepsin and inhibitor.

Mao B. Mao B. Biophys J. 1991 Oct;60(4):966-73. doi: 10.1016/S0006-3495(91)82130-0. Biophys J. 1991. PMID: 1742463 Free PMC article.

7

Quasi-continuum models of twist-like and accordion-like low-frequency motions in DNA.

Chou KC, Maggiora GM, Mao B. Chou KC, et al. Among authors: mao b. Biophys J. 1989 Aug;56(2):295-305. doi: 10.1016/S0006-3495(89)82676-1. Biophys J. 1989. PMID: 2775828 Free PMC article.

8

Renin inhibitory peptides. A beta-aspartyl residue as a replacement for the histidyl residue at the P-2 site.

Thaisrivongs S, Mao B, Pals DT, Turner SR, Kroll LT. Thaisrivongs S, et al. Among authors: mao b. J Med Chem. 1990 May;33(5):1337-43. doi: 10.1021/jm00167a009. J Med Chem. 1990. PMID: 2184238

9

Structure-conformation relationships of synthetic peptide inhibitors of human renin studied by resonance energy transfer and molecular modeling.

Epps DE, Mao B, Staples DJ, Sawyer TK. Epps DE, et al. Among authors: mao b. Int J Pept Protein Res. 1988 Jan;31(1):22-34. doi: 10.1111/j.1399-3011.1988.tb00003.x. Int J Pept Protein Res. 1988. PMID: 3284834

10

Design, structure-activity, and molecular modeling studies of potent renin inhibitory peptides having N-terminal Nin-For-Trp (Ftr): angiotensinogen congeners modified by P1-P1' Phe-Phe, Sta, Leu psi[CH(OH)CH2]Val or leu psi[CH2NH]Val substitutions.

Sawyer TK, Pals DT, Mao B, Staples DJ, de Vaux AE, Maggiora LL, Affholter JA, Kati W, Duchamp D, Hester JB, et al. Sawyer TK, et al. Among authors: mao b. J Med Chem. 1988 Jan;31(1):18-30. doi: 10.1021/jm00396a006. J Med Chem. 1988. PMID: 3275777

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