Scarborough PE - Search Results

1

Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling.

Scarborough PE, Guruprasad K, Topham C, Richo GR, Conner GE, Blundell TL, Dunn BM. Scarborough PE, et al. Protein Sci. 1993 Feb;2(2):264-76. doi: 10.1002/pro.5560020215. Protein Sci. 1993. PMID: 8443603 Free PMC article.

2

Comparison of kinetic properties of native and recombinant human cathepsin D.

Scarborough PE, Richo GR, Kay J, Conner GE, Dunn BM. Scarborough PE, et al. Adv Exp Med Biol. 1991;306:343-7. doi: 10.1007/978-1-4684-6012-4_41. Adv Exp Med Biol. 1991. PMID: 1812725 No abstract available.

3

Redesign of the substrate specificity of human cathepsin D: the dominant role of position 287 in the S2 subsite.

Scarborough PE, Dunn BM. Scarborough PE, et al. Protein Eng. 1994 Apr;7(4):495-502. doi: 10.1093/protein/7.4.495. Protein Eng. 1994. PMID: 7913221

4

Structure-function database for active site binding to the aspartic proteinases.

Rao C, Scarborough PE, Lowther WT, Kay J, Batley B, Rapundalo S, Klutchko S, Taylor MD, Dunn BM. Rao C, et al. Among authors: scarborough pe. Adv Exp Med Biol. 1991;306:143-7. doi: 10.1007/978-1-4684-6012-4_19. Adv Exp Med Biol. 1991. PMID: 1812702 No abstract available.

5

Analysis of proteinase specificity by studies of peptide substrates. The use of UV and fluorescence spectroscopy to quantitate rates of enzymatic cleavage.

Dunn BM, Scarborough PE, Davenport R, Swietnicki W. Dunn BM, et al. Among authors: scarborough pe. Methods Mol Biol. 1994;36:225-43. doi: 10.1385/0-89603-274-4:225. Methods Mol Biol. 1994. PMID: 7697110 Review. No abstract available.

6

Specificity in the binding of inhibitors to the active site of human/primate aspartic proteinases: analysis of P2-P1-P1'-P2' variation.

Rao CM, Scarborough PE, Kay J, Batley B, Rapundalo S, Klutchko S, Taylor MD, Lunney EA, Humblet CC, Dunn BM. Rao CM, et al. Among authors: scarborough pe. J Med Chem. 1993 Sep 3;36(18):2614-20. doi: 10.1021/jm00070a004. J Med Chem. 1993. PMID: 8410973

7

Comparison of the active site specificity of the aspartic proteinases based on a systematic series of peptide substrates.

Dunn BM, Scarborough PE, Lowther WT, Rao-Naik C. Dunn BM, et al. Among authors: scarborough pe. Adv Exp Med Biol. 1995;362:1-9. doi: 10.1007/978-1-4615-1871-6_1. Adv Exp Med Biol. 1995. PMID: 8540305 No abstract available.

8

Comparison of the specificity of the aspartic proteinases towards internally consistent sets of oligopeptide substrates.

Dunn BM, Oda K, Kay J, Rao-Naik C, Lowther WT, Beyer BM, Scarborough PE, Bukhtiyarova M. Dunn BM, et al. Among authors: scarborough pe. Adv Exp Med Biol. 1998;436:133-8. doi: 10.1007/978-1-4615-5373-1_18. Adv Exp Med Biol. 1998. PMID: 9561210 Review. No abstract available.

9

Sensitive, soluble chromogenic substrates for HIV-1 proteinase.

Richards AD, Phylip LH, Farmerie WG, Scarborough PE, Alvarez A, Dunn BM, Hirel PH, Konvalinka J, Strop P, Pavlickova L, et al. Richards AD, et al. Among authors: scarborough pe. J Biol Chem. 1990 May 15;265(14):7733-6. J Biol Chem. 1990. PMID: 2186027 Free article.

10

Substrate cleavage by HIV-1 proteinase.

Jupp RA, Richards AD, Phylip LH, Kay J, Konvalinka J, Strop P, Kostka V, Scarborough PE, Farmerie WG, Dunn BM. Jupp RA, et al. Among authors: scarborough pe. Adv Exp Med Biol. 1991;306:461-7. doi: 10.1007/978-1-4684-6012-4_59. Adv Exp Med Biol. 1991. PMID: 1812743 No abstract available.

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