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Items: 1 to 20 of 129

1.

Zymogen activation confers thermodynamic stability on a key peptide bond and protects human cationic trypsin from degradation.

Szabó A, Radisky ES, Sahin-Tóth M.

J Biol Chem. 2014 Feb 21;289(8):4753-61. doi: 10.1074/jbc.M113.538884. Epub 2014 Jan 8.

2.

Determinants of chymotrypsin C cleavage specificity in the calcium-binding loop of human cationic trypsinogen.

Szabó A, Sahin-Tóth M.

FEBS J. 2012 Dec;279(23):4283-92. doi: 10.1111/febs.12018. Epub 2012 Oct 30.

3.

Autoactivation of mouse trypsinogens is regulated by chymotrypsin C via cleavage of the autolysis loop.

Németh BC, Wartmann T, Halangk W, Sahin-Tóth M.

J Biol Chem. 2013 Aug 16;288(33):24049-62. doi: 10.1074/jbc.M113.478800. Epub 2013 Jun 27.

4.

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

Szmola R, Sahin-Tóth M.

Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11227-32. Epub 2007 Jun 25.

5.

Tighter Control by Chymotrypsin C (CTRC) Explains Lack of Association between Human Anionic Trypsinogen and Hereditary Pancreatitis.

Jancsó Z, Sahin-Tóth M.

J Biol Chem. 2016 Apr 18. pii: jbc.M116.725374. [Epub ahead of print]

6.

Mesotrypsin Signature Mutation in a Chymotrypsin C (CTRC) Variant Associated with Chronic Pancreatitis.

Szabó A, Ludwig M, Hegyi E, Szépeová R, Witt H, Sahin-Tóth M.

J Biol Chem. 2015 Jul 10;290(28):17282-92. doi: 10.1074/jbc.M114.618439. Epub 2015 May 26.

PMID:
26013824
7.

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.

J Biol Chem. 2002 Feb 22;277(8):6111-7. Epub 2001 Dec 17.

8.
9.

Chymotrypsin C (caldecrin) stimulates autoactivation of human cationic trypsinogen.

Nemoda Z, Sahin-Tóth M.

J Biol Chem. 2006 Apr 28;281(17):11879-86. Epub 2006 Feb 27.

10.

Increased activation of hereditary pancreatitis-associated human cationic trypsinogen mutants in presence of chymotrypsin C.

Szabó A, Sahin-Tóth M.

J Biol Chem. 2012 Jun 8;287(24):20701-10. doi: 10.1074/jbc.M112.360065. Epub 2012 Apr 26.

11.
12.

A novel A121T mutation in human cationic trypsinogen associated with hereditary pancreatitis: functional data indicating a loss-of-function mutation influencing the R122 trypsin cleavage site.

Felderbauer P, Schnekenburger J, Lebert R, Bulut K, Parry M, Meister T, Schick V, Schmitz F, Domschke W, Schmidt WE.

J Med Genet. 2008 Aug;45(8):507-12. doi: 10.1136/jmg.2007.056481. Epub 2008 May 29.

PMID:
18511571
13.

Properties of the His57-Asp102 dyad of rat trypsin D189S in the zymogen, activated enzyme, and alpha1-proteinase inhibitor complexed forms.

Kaslik G, Westler WM, Gráf L, Markley JL.

Arch Biochem Biophys. 1999 Feb 15;362(2):254-64.

PMID:
9989934
14.

Ostrich trypsinogen: purification, kinetic properties and characterization of the pancreatic enzyme.

Bodley MD, Naudé RJ, Oelofsen W, Pátthy A.

Int J Biochem Cell Biol. 1995 Jul;27(7):719-28.

PMID:
7648428
15.

Mesotrypsin: a new inhibitor-resistant protease from a zymogen in human pancreatic tissue and fluid.

Rinderknecht H, Renner IG, Abramson SB, Carmack C.

Gastroenterology. 1984 Apr;86(4):681-92.

PMID:
6698368
16.

Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation.

Batra J, Szabó A, Caulfield TR, Soares AS, Sahin-Tóth M, Radisky ES.

J Biol Chem. 2013 Apr 5;288(14):9848-59. doi: 10.1074/jbc.M113.457382. Epub 2013 Feb 19.

17.

Limited proteolyses in pancreatic chymotrypsinogens and trypsinogens.

Rovery M.

Biochimie. 1988 Sep;70(9):1131-5. Review.

PMID:
3147704
18.

Kinetic analysis of ligand-induced autocatalytic reactions.

Liu JH, Wang ZX.

Biochem J. 2004 May 1;379(Pt 3):697-702.

19.

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.

Hum Mutat. 2004 Jan;23(1):22-31.

PMID:
14695529
20.

Chronic pancreatitis associated with an activation peptide mutation that facilitates trypsin activation.

Teich N, Ockenga J, Hoffmeister A, Manns M, Mössner J, Keim V.

Gastroenterology. 2000 Aug;119(2):461-5.

PMID:
10930381
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