Janata J - Search Results

1

Cleavage site selection within a folded substrate by the ATP-dependent lon protease.

Ondrovicová G, Liu T, Singh K, Tian B, Li H, Gakh O, Perecko D, Janata J, Granot Z, Orly J, Kutejová E, Suzuki CK. Ondrovicová G, et al. Among authors: janata j. J Biol Chem. 2005 Jul 1;280(26):25103-10. doi: 10.1074/jbc.M502796200. Epub 2005 May 3. J Biol Chem. 2005. PMID: 15870080 Free article.

2

Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis.

Bauer J, Ondrovičová G, Najmanová L, Pevala V, Kameník Z, Koštan J, Janata J, Kutejová E. Bauer J, et al. Among authors: janata j. Acta Crystallogr D Biol Crystallogr. 2014 Apr;70(Pt 4):943-57. doi: 10.1107/S139900471303397X. Epub 2014 Mar 19. Acta Crystallogr D Biol Crystallogr. 2014. PMID: 24699640

3

Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element.

Janata J, Holá K, Kubala M, Gakh O, Parkhomenko N, Matusková A, Kutejová E, Amler E. Janata J, et al. Biochem Biophys Res Commun. 2004 Mar 26;316(1):211-7. doi: 10.1016/j.bbrc.2004.02.025. Biochem Biophys Res Commun. 2004. PMID: 15003532

4

A computational study of the glycine-rich loop of mitochondrial processing peptidase.

Kučera T, Otyepka M, Matušková A, Samad A, Kutejová E, Janata J. Kučera T, et al. Among authors: janata j. PLoS One. 2013 Sep 13;8(9):e74518. doi: 10.1371/journal.pone.0074518. eCollection 2013. PLoS One. 2013. PMID: 24058582 Free PMC article.

5

Substrate binding changes conformation of the alpha-, but not the beta-subunit of mitochondrial processing peptidase.

Gakh O, Obsil T, Adamec J, Spizek J, Amler E, Janata J, Kalousek F. Gakh O, et al. Among authors: janata j. Arch Biochem Biophys. 2001 Jan 15;385(2):392-6. doi: 10.1006/abbi.2000.2167. Arch Biochem Biophys. 2001. PMID: 11368022

6

Glycine-rich loop of mitochondrial processing peptidase alpha-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20.

Dvoráková-Holá K, Matusková A, Kubala M, Otyepka M, Kucera T, Vecer J, Herman P, Parkhomenko N, Kutejova E, Janata J. Dvoráková-Holá K, et al. Among authors: janata j. J Mol Biol. 2010 Mar 12;396(5):1197-210. doi: 10.1016/j.jmb.2009.12.054. Epub 2010 Jan 4. J Mol Biol. 2010. PMID: 20053354

7

Adaptation of an L-proline adenylation domain to use 4-propyl-L-proline in the evolution of lincosamide biosynthesis.

Kadlčík S, Kučera T, Chalupská D, Gažák R, Koběrská M, Ulanová D, Kopecký J, Kutejová E, Najmanová L, Janata J. Kadlčík S, et al. Among authors: janata j. PLoS One. 2013 Dec 27;8(12):e84902. doi: 10.1371/journal.pone.0084902. eCollection 2013. PLoS One. 2013. PMID: 24386435 Free PMC article.

8

Reductive evolution of the mitochondrial processing peptidases of the unicellular parasites trichomonas vaginalis and giardia intestinalis.

Smíd O, Matusková A, Harris SR, Kucera T, Novotný M, Horváthová L, Hrdý I, Kutejová E, Hirt RP, Embley TM, Janata J, Tachezy J. Smíd O, et al. Among authors: janata j. PLoS Pathog. 2008 Dec;4(12):e1000243. doi: 10.1371/journal.ppat.1000243. Epub 2008 Dec 19. PLoS Pathog. 2008. PMID: 19096520 Free PMC article.

9

Lincomycin biosynthesis involves a tyrosine hydroxylating heme protein of an unusual enzyme family.

Novotna J, Olsovska J, Novak P, Mojzes P, Chaloupkova R, Kamenik Z, Spizek J, Kutejova E, Mareckova M, Tichy P, Damborsky J, Janata J. Novotna J, et al. Among authors: janata j. PLoS One. 2013 Dec 4;8(12):e79974. doi: 10.1371/journal.pone.0079974. eCollection 2013. PLoS One. 2013. PMID: 24324587 Free PMC article.

10

Characterization of N-demethyllincosamide methyltransferases LmbJ and CcbJ.

Najmanová L, Kutejová E, Kadlec J, Polan M, Olšovská J, Benada O, Novotná J, Kameník Z, Halada P, Bauer J, Janata J. Najmanová L, et al. Among authors: janata j. Chembiochem. 2013 Nov 25;14(17):2259-62. doi: 10.1002/cbic.201300389. Epub 2013 Oct 25. Chembiochem. 2013. PMID: 24166757

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