Potempa J - Search Results

1

Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases.

Potempa J, Golonka E, Filipek R, Shaw LN. Potempa J, et al. Mol Microbiol. 2005 Aug;57(3):605-10. doi: 10.1111/j.1365-2958.2005.04714.x. Mol Microbiol. 2005. PMID: 16045606 Free article.

2

Porphyromonas gingivalis: a proteinase/gene accounting audit.

Potempa J, Pavloff N, Travis J. Potempa J, et al. Trends Microbiol. 1995 Nov;3(11):430-4. doi: 10.1016/s0966-842x(00)88996-9. Trends Microbiol. 1995. PMID: 8574516 Review.

3

Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis.

Potempa J, Mikolajczyk-Pawlinska J, Brassell D, Nelson D, Thøgersen IB, Enghild JJ, Travis J. Potempa J, et al. J Biol Chem. 1998 Aug 21;273(34):21648-57. doi: 10.1074/jbc.273.34.21648. J Biol Chem. 1998. PMID: 9705298 Free article.

4

Role of bacterial proteinases in matrix destruction and modulation of host responses.

Potempa J, Banbula A, Travis J. Potempa J, et al. Periodontol 2000. 2000 Oct;24:153-92. doi: 10.1034/j.1600-0757.2000.2240108.x. Periodontol 2000. 2000. PMID: 11276866 Review.

5

Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis.

Sztukowska M, Bugno M, Potempa J, Travis J, Kurtz DM Jr. Sztukowska M, et al. Among authors: potempa j. Mol Microbiol. 2002 Apr;44(2):479-88. doi: 10.1046/j.1365-2958.2002.02892.x. Mol Microbiol. 2002. PMID: 11972784 Free article.

6

New method for typing Staphylococcus aureus strains: multiple-locus variable-number tandem repeat analysis of polymorphism and genetic relationships of clinical isolates.

Sabat A, Krzyszton-Russjan J, Strzalka W, Filipek R, Kosowska K, Hryniewicz W, Travis J, Potempa J. Sabat A, et al. Among authors: potempa j. J Clin Microbiol. 2003 Apr;41(4):1801-4. doi: 10.1128/JCM.41.4.1801-1804.2003. J Clin Microbiol. 2003. PMID: 12682193 Free PMC article.

7

The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease.

Filipek R, Rzychon M, Oleksy A, Gruca M, Dubin A, Potempa J, Bochtler M. Filipek R, et al. Among authors: potempa j. J Biol Chem. 2003 Oct 17;278(42):40959-66. doi: 10.1074/jbc.M302926200. Epub 2003 Jul 21. J Biol Chem. 2003. PMID: 12874290 Free article.

8

Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases.

Rzychon M, Sabat A, Kosowska K, Potempa J, Dubin A. Rzychon M, et al. Among authors: potempa j. Mol Microbiol. 2003 Aug;49(4):1051-66. doi: 10.1046/j.1365-2958.2003.03613.x. Mol Microbiol. 2003. PMID: 12890028 Free article.

9

Staphostatins resemble lipocalins, not cystatins in fold.

Rzychon M, Filipek R, Sabat A, Kosowska K, Dubin A, Potempa J, Bochtler M. Rzychon M, et al. Among authors: potempa j. Protein Sci. 2003 Oct;12(10):2252-6. doi: 10.1110/ps.03247703. Protein Sci. 2003. PMID: 14500882 Free PMC article.

10

A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus.

Dubin G, Krajewski M, Popowicz G, Stec-Niemczyk J, Bochtler M, Potempa J, Dubin A, Holak TA. Dubin G, et al. Among authors: potempa j. Biochemistry. 2003 Nov 25;42(46):13449-56. doi: 10.1021/bi035310j. Biochemistry. 2003. PMID: 14621990

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