Kukor Z - Search Results

1

Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases.

Kukor Z, Tóth M, Sahin-Tóth M. Kukor Z, et al. Eur J Biochem. 2003 May;270(9):2047-58. doi: 10.1046/j.1432-1033.2003.03581.x. Eur J Biochem. 2003. PMID: 12709065 Free article.

2

Human mesotrypsin is a unique digestive protease specialized for the degradation of trypsin inhibitors.

Szmola R, Kukor Z, Sahin-Tóth M. Szmola R, et al. Among authors: kukor z. J Biol Chem. 2003 Dec 5;278(49):48580-9. doi: 10.1074/jbc.M310301200. Epub 2003 Sep 24. J Biol Chem. 2003. PMID: 14507909 Free PMC article.

3

Expression of human cationic trypsinogen with an authentic N terminus using intein-mediated splicing in aminopeptidase P deficient Escherichia coli.

Király O, Guan L, Szepessy E, Tóth M, Kukor Z, Sahin-Tóth M. Király O, et al. Among authors: kukor z. Protein Expr Purif. 2006 Jul;48(1):104-11. doi: 10.1016/j.pep.2006.01.023. Epub 2006 Feb 21. Protein Expr Purif. 2006. PMID: 16542853 Free PMC article.

4

Human cationic trypsinogen is sulfated on Tyr154.

Sahin-Tóth M, Kukor Z, Nemoda Z. Sahin-Tóth M, et al. Among authors: kukor z. FEBS J. 2006 Nov;273(22):5044-50. doi: 10.1111/j.1742-4658.2006.05501.x. FEBS J. 2006. PMID: 17087724 Free PMC article.

5

Hereditary pancreatitis caused by mutation-induced misfolding of human cationic trypsinogen: a novel disease mechanism.

Kereszturi E, Szmola R, Kukor Z, Simon P, Weiss FU, Lerch MM, Sahin-Tóth M. Kereszturi E, et al. Among authors: kukor z. Hum Mutat. 2009 Apr;30(4):575-82. doi: 10.1002/humu.20853. Hum Mutat. 2009. PMID: 19191323 Free PMC article.

6

Human cationic trypsinogen. Arg(117) is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation.

Kukor Z, Tóth M, Pál G, Sahin-Tóth M. Kukor Z, et al. J Biol Chem. 2002 Feb 22;277(8):6111-7. doi: 10.1074/jbc.M110959200. Epub 2001 Dec 17. J Biol Chem. 2002. PMID: 11748242 Free article.

7

Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis.

Kukor Z, Mayerle J, Krüger B, Tóth M, Steed PM, Halangk W, Lerch MM, Sahin-Tóth M. Kukor Z, et al. J Biol Chem. 2002 Jun 14;277(24):21389-96. doi: 10.1074/jbc.M200878200. Epub 2002 Apr 3. J Biol Chem. 2002. PMID: 11932257 Free article.

8

Evolution of trypsinogen activation peptides.

Chen JM, Kukor Z, Le Maréchal C, Tóth M, Tsakiris L, Raguénès O, Férec C, Sahin-Tóth M. Chen JM, et al. Among authors: kukor z. Mol Biol Evol. 2003 Nov;20(11):1767-77. doi: 10.1093/molbev/msg183. Epub 2003 Jun 27. Mol Biol Evol. 2003. PMID: 12832630

9

Interaction between trypsinogen isoforms in genetically determined pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased transactivation of anionic trypsinogen (PRSS2).

Teich N, Le Maréchal C, Kukor Z, Caca K, Witzigmann H, Chen JM, Tóth M, Mössner J, Keim V, Férec C, Sahin-Tóth M. Teich N, et al. Among authors: kukor z. Hum Mutat. 2004 Jan;23(1):22-31. doi: 10.1002/humu.10285. Hum Mutat. 2004. PMID: 14695529

10

A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitis.

Witt H, Sahin-Tóth M, Landt O, Chen JM, Kähne T, Drenth JP, Kukor Z, Szepessy E, Halangk W, Dahm S, Rohde K, Schulz HU, Le Maréchal C, Akar N, Ammann RW, Truninger K, Bargetzi M, Bhatia E, Castellani C, Cavestro GM, Cerny M, Destro-Bisol G, Spedini G, Eiberg H, Jansen JB, Koudova M, Rausova E, Macek M Jr, Malats N, Real FX, Menzel HJ, Moral P, Galavotti R, Pignatti PF, Rickards O, Spicak J, Zarnescu NO, Böck W, Gress TM, Friess H, Ockenga J, Schmidt H, Pfützer R, Löhr M, Simon P, Weiss FU, Lerch MM, Teich N, Keim V, Berg T, Wiedenmann B, Luck W, Groneberg DA, Becker M, Keil T, Kage A, Bernardova J, Braun M, Güldner C, Halangk J, Rosendahl J, Witt U, Treiber M, Nickel R, Férec C. Witt H, et al. Among authors: kukor z. Nat Genet. 2006 Jun;38(6):668-73. doi: 10.1038/ng1797. Epub 2006 May 14. Nat Genet. 2006. PMID: 16699518 Free PMC article.

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