Dash C - Search Results

1

Aspartic peptidase inhibitors: implications in drug development.

Dash C, Kulkarni A, Dunn B, Rao M. Dash C, et al. Crit Rev Biochem Mol Biol. 2003;38(2):89-119. doi: 10.1080/713609213. Crit Rev Biochem Mol Biol. 2003. PMID: 12749695 Review.

2

Fabrication, characterization, and enzymatic activity of encapsulated fungal protease--fatty lipid biocomposite films.

Gole A, Dash C, Mandale AB, Rao M, Sastry M. Gole A, et al. Among authors: dash c. Anal Chem. 2000 Sep 15;72(18):4301-9. doi: 10.1021/ac000099s. Anal Chem. 2000. PMID: 11008764

3

Interactions of a novel inhibitor from an extremophilic Bacillus sp. with HIV-1 protease: implications for the mechanism of inactivation.

Dash C, Rao M. Dash C, et al. J Biol Chem. 2001 Jan 26;276(4):2487-93. doi: 10.1074/jbc.M005662200. Epub 2000 Oct 20. J Biol Chem. 2001. PMID: 11042202 Free article.

4

Novel bifunctional inhibitor of xylanase and aspartic protease: implications for inhibition of fungal growth.

Dash C, Ahmad A, Nath D, Rao M. Dash C, et al. Antimicrob Agents Chemother. 2001 Jul;45(7):2008-17. doi: 10.1128/AAC.45.7.2008-2017.2001. Antimicrob Agents Chemother. 2001. PMID: 11408216 Free PMC article.

5

Structural and mechanistic insight into the inhibition of aspartic proteases by a slow-tight binding inhibitor from an extremophilic Bacillus sp.: correlation of the kinetic parameters with the inhibitor induced conformational changes.

Dash C, Phadtare S, Deshpande V, Rao M. Dash C, et al. Biochemistry. 2001 Sep 25;40(38):11525-32. doi: 10.1021/bi010594y. Biochemistry. 2001. PMID: 11560501

6

On the preparation, characterization, and enzymatic activity of fungal protease-gold colloid bioconjugates.

Gole A, Dash C, Soman C, Sainkar SR, Rao M, Sastry M. Gole A, et al. Among authors: dash c. Bioconjug Chem. 2001 Sep-Oct;12(5):684-90. doi: 10.1021/bc0001241. Bioconjug Chem. 2001. PMID: 11562186

7

Slow-tight binding inhibition of xylanase by an aspartic protease inhibitor: kinetic parameters and conformational changes that determine the affinity and selectivity of the bifunctional nature of the inhibitor.

Dash C, Vathipadiekal V, George SP, Rao M. Dash C, et al. J Biol Chem. 2002 May 17;277(20):17978-86. doi: 10.1074/jbc.M111250200. Epub 2002 Feb 13. J Biol Chem. 2002. PMID: 11844793 Free article.

The first report of slow-tight inhibition of xylanase by a bifunctional inhibitor alkalo-thermophilic Bacillus inhibitor (ATBI), from an extremophilic Bacillus sp. is described. ATBI inhibits aspartic protease (Dash, C., and Rao, M. (2001) J. Biol. Chem., 276, 2487- …

The first report of slow-tight inhibition of xylanase by a bifunctional inhibitor alkalo-thermophilic Bacillus inhibitor (ATBI), from an ext …

8

Improved performance of preordered fungal protease-stearic acid biocomposites: enhanced catalytic activity, reusability, and temporal stability.

Phadtare S, Dash C, Gole A, Vinod VP, Rao M, Sastry M. Phadtare S, et al. Among authors: dash c. Biotechnol Prog. 2002 Jul-Aug;18(4):700-5. doi: 10.1021/bp025538i. Biotechnol Prog. 2002. PMID: 12153301

9

Slow tight binding inhibition of proteinase K by a proteinaceous inhibitor: conformational alterations responsible for conferring irreversibility to the enzyme-inhibitor complex.

Pandhare J, Dash C, Rao M, Deshpande V. Pandhare J, et al. Among authors: dash c. J Biol Chem. 2003 Dec 5;278(49):48735-44. doi: 10.1074/jbc.M308976200. Epub 2003 Sep 24. J Biol Chem. 2003. PMID: 14507912 Free article.

10

Illustration of HIV-1 protease folding through a molten-globule-like intermediate using an experimental model that implicates alpha-crystallin and calcium ions.

Dash C, Sastry M, Rao M. Dash C, et al. Biochemistry. 2005 Mar 15;44(10):3725-34. doi: 10.1021/bi048378n. Biochemistry. 2005. PMID: 15751949

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