Sahin-Tóth M - Search Results

1

Chronic pancreatitis: Multicentre prospective data collection and analysis by the Hungarian Pancreatic Study Group.

Szücs Á, Marjai T, Szentesi A, Farkas N, Párniczky A, Nagy G, Kui B, Takács T, Czakó L, Szepes Z, Németh BC, Vincze Á, Pár G, Szabó I, Sarlós P, Illés A, Gódi S, Izbéki F, Gervain J, Halász A, Farkas G, Leindler L, Kelemen D, Papp R, Szmola R, Varga M, Hamvas J, Novák J, Bod B, Sahin-Tóth M, Hegyi P; Hungarian Pancreatic Study Group. Szücs Á, et al. PLoS One. 2017 Feb 16;12(2):e0171420. doi: 10.1371/journal.pone.0171420. eCollection 2017. PLoS One. 2017. PMID: 28207747 Free PMC 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. 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

Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y.

Szmola R, Sahin-Tóth M. Szmola R, et al. Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11227-32. doi: 10.1073/pnas.0703714104. Epub 2007 Jun 25. Proc Natl Acad Sci U S A. 2007. PMID: 17592142 Free PMC article.

4

Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis.

Rosendahl J, Witt H, Szmola R, Bhatia E, Ozsvári B, Landt O, Schulz HU, Gress TM, Pfützer R, Löhr M, Kovacs P, Blüher M, Stumvoll M, Choudhuri G, Hegyi P, te Morsche RH, Drenth JP, Truninger K, Macek M Jr, Puhl G, Witt U, Schmidt H, Büning C, Ockenga J, Kage A, Groneberg DA, Nickel R, Berg T, Wiedenmann B, Bödeker H, Keim V, Mössner J, Teich N, Sahin-Tóth M. Rosendahl J, et al. Nat Genet. 2008 Jan;40(1):78-82. doi: 10.1038/ng.2007.44. Epub 2007 Dec 2. Nat Genet. 2008. PMID: 18059268 Free PMC article.

5

The guinea pig pancreas secretes a single trypsinogen isoform, which is defective in autoactivation.

Ozsvári B, Hegyi P, Sahin-Tóth M. Ozsvári B, et al. Pancreas. 2008 Aug;37(2):182-8. doi: 10.1097/MPA.0b013e3181663066. Pancreas. 2008. PMID: 18665081 Free PMC article.

6

[Genetic risk factors in chronic pancreatitis].

Sahin-Tóth M, Hegyi P, Tóth M. Sahin-Tóth M, et al. Orv Hetil. 2008 Sep 7;149(36):1683-8. doi: 10.1556/OH.2008.28441. Orv Hetil. 2008. PMID: 18755660 Review. Hungarian.

7

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. Hum Mutat. 2009 Apr;30(4):575-82. doi: 10.1002/humu.20853. Hum Mutat. 2009. PMID: 19191323 Free PMC article.

8

Proteolytic activation of human pancreatitis-associated protein is required for peptidoglycan binding and bacterial aggregation.

Medveczky P, Szmola R, Sahin-Tóth M. Medveczky P, et al. Biochem J. 2009 May 13;420(2):335-43. doi: 10.1042/BJ20090005. Biochem J. 2009. PMID: 19254208 Free PMC article.

9

Pancreatitis-associated chymotrypsinogen C (CTRC) mutant elicits endoplasmic reticulum stress in pancreatic acinar cells.

Szmola R, Sahin-Tóth M. Szmola R, et al. Gut. 2010 Mar;59(3):365-72. doi: 10.1136/gut.2009.198903. Epub 2009 Nov 30. Gut. 2010. PMID: 19951900 Free PMC article.

10

Uncertainties in the classification of human cationic trypsinogen (PRSS1) variants as hereditary pancreatitis-associated mutations.

Szmola R, Sahin-Tóth M. Szmola R, et al. J Med Genet. 2010 May;47(5):348-50. doi: 10.1136/jmg.2009.072751. J Med Genet. 2010. PMID: 20452997 Free PMC article.

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