References
- Beyer G, Habtezion A, Werner J, Lerch MM, Mayerle J. Chronic pancreatitis. Lancet. 2020;396(10249):499–512. doi:10.1016/S0140-6736(20)31318-0
- Angelopoulos N, Dervenis C, Goula A, et al. Endocrine pancreatic insufficiency in chronic pancreatitis. Pancreatology. 2005;5(2–3):122–131. doi:10.1159/000085264
- Capurso G, Traini M, Piciucchi M, Signoretti M, Arcidiacono PG. Exocrine pancreatic insufficiency: prevalence, diagnosis, and management. Clin Exp Gastroenterol. 2019;12:129–139. doi:10.2147/CEG.S168266
- Weiss FU, Laemmerhirt F, Lerch MM. Etiology and risk factors of acute and chronic pancreatitis. Visc Med. 2019;35(2):73–81. doi:10.1159/000499138
- Hirota M, Ohmuraya M, Baba H. The role of trypsin, trypsin inhibitor, and trypsin receptor in the onset and aggravation of pancreatitis. J Gastroenterol. 2006;41(9):832–836. doi:10.1007/s00535-006-1874-2
- Nagel F, Palm GJ, Geist N, et al. Structural and biophysical insights into SPINK1 bound to human cationic trypsin. Int J Mol Sci. 2022;23(7):3468. doi:10.3390/ijms23073468
- Hegyi E, Sahin-Tóth M. Genetic risk in chronic pancreatitis: the trypsin-dependent pathway. Dig Dis Sci. 2017;62(7):1692–1701. doi:10.1007/s10620-017-4601-3
- Whitcomb DC, Gorry MC, Preston RA, et al. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. Nat Genet. 1996;14(2):141–145. doi:10.1038/ng1096-141
- Teich N, Bauer N, Mössner J, Keim V. Mutational screening of patients with nonalcoholic chronic pancreatitis: identification of further trypsinogen variants. Am J Gastroenterol. 2002;97(2):341–346. doi:10.1111/j.1572-0241.2002.05467.x
- Gorry MC, Gabbaizedeh D, Furey W, et al. Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis. Gastroenterology. 1997;113(4):1063–1068. doi:10.1053/gast.1997.v113.pm9322498
- Witt H, Luck W, Becker M. A signal peptide cleavage site mutation in the cationic trypsinogen gene is strongly associated with chronic pancreatitis. Gastroenterology. 1999;117(1):7–10. doi:10.1016/s0016-5085(99)70543-3
- Kukor Z, Tóth M, Pál G, Sahin-Tóth M. Human cationic trypsinogen: Arg (117) is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation. J Biol Chem. 2002;277(8):6111–6117. doi:10.1074/jbc.M110959200
- Witt H, Sahin-Tóth M, Landt O, et al. A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitis. Nat Genet. 2006;38(6):668–673. doi:10.1038/ng1797
- Jancsó Z, Sahin-Tóth M. Tighter control by chymotrypsin C (CTRC) explains lack of association between human anionic trypsinogen and hereditary Pancreatitis*♦. J Biol Chem. 2016;291(25):12897–12905. doi:10.1074/jbc.M116.725374
- Weiss FU, Skube ME, Lerch MM. Chronic pancreatitis: an update on genetic risk factors. Curr Opin Gastroenterol. 2018;34(5):322–329. doi:10.1097/MOG.0000000000000461
- Kukor Z, Tóth M, Sahin-Tóth M. Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases. Eur J Biochem. 2003;270(9):2047–2058. doi:10.1046/j.1432-1033.2003.03581.x
- Guy O, Lombardo D, Bartelt DC, Amic J, Figarella C. Two human trypsinogens. purification, molecular properties, and N-terminal sequences. Biochemistry. 1978;17(9):1669–1675. doi:10.1021/bi00602a014
- Rinderknecht H, Renner IG, Carmack C. Trypsinogen variants in pancreatic juice of healthy volunteers, chronic alcoholics, and patients with pancreatitis and cancer of the pancreas. Gut. 1979;20(10):886–891. doi:10.1136/gut.20.10.886
- Rinderknecht H, Stace NH, Renner IG. Effects of chronic alcohol abuse on exocrine pancreatic secretion in man. Dig Dis Sci. 1985;30(1):65–71. doi:10.1007/BF01318373
- Wan J, Haddock A, Edenfield B, Ji B, Bi Y. Transgenic expression of human PRSS2 exacerbates pancreatitis in mice. Gut. 2020;69(11):2051–2052. doi:10.1136/gutjnl-2019-320399
- Susemihl A, Nagel F, Grabarczyk P, Schmidt CA, Delcea M. Easy expression and purification of fluorescent N-terminal BCL11B CCHC zinc finger domain. Molecules. 2021;26:24. doi:10.3390/molecules26247576
- Kabsch W. XDS. Acta Crystallogr Sect D. 2010;66(2):125–132. doi:10.1107/S0907444909047337
- McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ. Phaser crystallographic software. J Appl Crystallogr. 2007;40(4):658–674. doi:10.1107/S0021889807021206
- Liebschner D, Afonine PV, Baker ML, et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr Sect D. 2019;75(10):861–877. doi:10.1107/S2059798319011471
- Emsley P, Lohkamp B, Scott WG, Cowtan K. Features and development of Coot. Acta Crystallogr Sect D Biol Crystallogr. 2010;66(4):486–501. doi:10.1107/S0907444910007493
- Phillips JC, Braun R, Wang W, et al. Scalable molecular dynamics with NAMD. J Comput Chem. 2005;26(16):1781–1802. doi:10.1002/jcc.20289
- Huang J, MacKerell AD Jr. CHARMM36 all-atom additive protein force field: validation based on comparison to NMR data. J Comput Chem. 2013;34(25):2135–2145. doi:10.1002/jcc.23354
- Jo S, Kim T, Iyer VG, Im W. CHARMM-GUI: a web-based graphical user interface for CHARMM. J Comput Chem. 2008;29(11):1859–1865. doi:10.1002/jcc.20945
- Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graph. 1996;14(1):33–38. doi:10.1016/0263-7855(96)00018-5
- Hopkins CW, Le Grand S, Walker RC, Roitberg AE. Long-time-step molecular dynamics through hydrogen mass repartitioning. J Chem Theory Comput. 2015;11(4):1864–1874. doi:10.1021/ct5010406
- Schechter I, Berger A. On the size of the active site in proteases. I Papain. Biochem Biophys Res Commun. 1967;27(2):157–162. doi:10.1016/S0006-291X(67)80055-X
- Blevins RA, Tulinsky A. The refinement and the structure of the dimer of alpha-chymotrypsin at 1.67-A resolution. J Biol Chem. 1985;260(7):4264–4275. doi:10.2210/pdb5cha/pdb
- Scheele G, Bartelt D, Bieger W. Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis. Gastroenterology. 1981;80(3):461–473. doi:10.1016/0016-5085(81)90007-X
- Katona G, Berglund GI, Hajdu J, Gráf L, Szilágyi L. Crystal structure reveals basis for the inhibitor resistance of human brain trypsin11. J Mol Biol. 2002;315(5):1209–1218. doi:10.1006/jmbi.2001.5305
- Szabó A, Toldi V, Gazda LD, Demcsák A, Tőzsér J, Sahin-Tóth M. Defective binding of SPINK1 variants is an uncommon mechanism for impaired trypsin inhibition in chronic pancreatitis. J Biol Chem. 2021;296:100343. doi:10.1016/j.jbc.2021.100343
- Zakharova E, Horvath MP, Goldenberg DP. Structure of a serine protease poised to resynthesize a peptide bond. Proc Natl Acad Sci USA. 2009;106(27):11034–11039. doi:10.1073/pnas.0902463106
- Goncz KK, Behrsing R, Rothman SS. The protein content and morphogenesis of zymogen granules. Cell Tissue Res. 1995;280(3):519–530. doi:10.1007/BF00318356
- Kambhampati S, Park W, Habtezion A. Pharmacologic therapy for acute pancreatitis. World J Gastroenterol. 2014;20(45):16868–16880. doi:10.3748/wjg.v20.i45.16868
- Leppäniemi A, Tolonen M, Tarasconi A, et al. 2019 WSES guidelines for the management of severe acute pancreatitis. World J Emerg Surg. 2019;14(1):27. doi:10.1186/s13017-019-0247-0
- Pezzilli R. Pharmacotherapy for acute pancreatitis. Expert Opin Pharmacother. 2009;10(18):2999–3014. doi:10.1517/14656560903382630
- Baker NA, Sept D, Joseph S, Holst MJ, McCammon JA. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci. 2001;98(18):10037–10041. doi:10.1073/pnas.181342398