about
Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseasesHereditary pancreatitis caused by mutation-induced misfolding of human cationic trypsinogen: a novel disease mechanismChymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme YBiochemical models of hereditary pancreatitisProspective, Multicentre, Nationwide Clinical Data from 600 Cases of Acute PancreatitisChronic pancreatitis: Multicentre prospective data collection and analysis by the Hungarian Pancreatic Study Group.A novel mutation in PNLIP causes pancreatic triglyceride lipase deficiency through protein misfolding.Human mesotrypsin exhibits restricted S1' subsite specificity with a strong preference for small polar side chainsGenetic Risk in Chronic Pancreatitis: The Trypsin-Dependent Pathway.High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4' acidic residues.Complete analysis of the human mesotrypsinogen gene (PRSS3) in patients with chronic pancreatitis.Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.The pathobiochemistry of hereditary pancreatitis: studies on recombinant human cationic trypsinogen.Autoantibodies against the exocrine pancreas in autoimmune pancreatitis: gene and protein expression profiling and immunoassays identify pancreatic enzymes as a major target of the inflammatory process.Alcohol disrupts levels and function of the cystic fibrosis transmembrane conductance regulator to promote development of pancreatitis.Gene conversion between cationic trypsinogen (PRSS1) and the pseudogene trypsinogen 6 (PRSS3P2) in patients with chronic pancreatitis.Tyrosine sulfation of human trypsin steers S2' subsite selectivity towards basic amino acids.Chymotrypsin C (caldecrin) is associated with enamel developmentMesotrypsin Signature Mutation in a Chymotrypsin C (CTRC) Variant Associated with Chronic Pancreatitis.Variants in pancreatic carboxypeptidase genes CPA2 and CPB1 are not associated with chronic pancreatitis.Overlapping Specificity of Duplicated Human Pancreatic Elastase 3 Isoforms and Archetypal Porcine Elastase 1 Provides Clues to Evolution of Digestive Enzymes.Serine protease inhibitor Kazal type 1 (SPINK1) drives proliferation and anoikis resistance in a subset of ovarian cancersA Common CCK-B Receptor Intronic Variant in Pancreatic Adenocarcinoma in a Hungarian Cohort.Pathogenic cellular role of the p.L104P human cationic trypsinogen variant in chronic pancreatitisFunctional effects of 13 rare PRSS1 variants presumed to cause chronic pancreatitis.Tighter Control by Chymotrypsin C (CTRC) Explains Lack of Association between Human Anionic Trypsinogen and Hereditary Pancreatitis.Minigene analysis of intronic variants in common SPINK1 haplotypes associated with chronic pancreatitis.A common African polymorphism abolishes tyrosine sulfation of human anionic trypsinogen (PRSS2).The guinea pig pancreas secretes a single trypsinogen isoform, which is defective in autoactivation.Signal peptide variants that impair secretion of pancreatic secretory trypsin inhibitor (SPINK1) cause autosomal dominant hereditary pancreatitisGenetic Analysis of Human Chymotrypsin-Like Elastases 3A and 3B (CELA3A and CELA3B) to Assess the Role of Complex Formation between Proelastases and Procarboxypeptidases in Chronic Pancreatitis.CFTR: A New Horizon in the Pathomechanism and Treatment of Pancreatitis.Zymogen activation confers thermodynamic stability on a key peptide bond and protects human cationic trypsin from degradation.Human cationic trypsinogen (PRSS1) variants and chronic pancreatitis.Chymotrypsin C (caldecrin) stimulates autoactivation of human cationic trypsinogen.Expression of human cationic trypsinogen with an authentic N terminus using intein-mediated splicing in aminopeptidase P deficient Escherichia coli.Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.SPINK1 Promoter Variants in Chronic Pancreatitis.Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.Genetic risk in chronic pancreatitis: the misfolding-dependent pathway
P50
Q24300351-C51000FA-4B74-4D30-97C3-EAE8D3876E80Q24650338-D61DE4B0-B378-49BA-8455-0969DA810DD2Q24675338-6A0AB95A-91FE-4EBC-9538-19F972297586Q24675973-CEB7C713-23FA-4A0F-B00C-00873CD31342Q31140215-2924CFA0-CB53-4239-B72D-F1BF35DEEC65Q31162496-793B1653-6E73-4AE8-9E55-8CD43096C452Q31814814-FBD48E07-9C01-4BC5-ACFF-1CE92948A8C0Q33246025-5E369C3D-1DB0-4A1C-987F-AA07346DB351Q33843764-0310F668-F3F5-4E91-8E1D-8712E3999974Q33880616-68F7511E-F125-4380-B7C7-D3B7D2C7D123Q33970803-B3A9DF82-7176-49F3-9A07-67EE95F73A5BQ34503091-A0E06CA7-214F-46B6-9CDD-165DE11446FDQ34743067-BA19DD82-7135-4A29-9556-0EC003D45E61Q34996503-4648ED08-6F88-4E8A-A696-83F4F8C2CF5AQ35159183-92E702D0-DCAA-456A-9C3B-8A492C6ED08BQ35181335-94FF12F6-2215-4DFA-8737-88ED29E49631Q35204469-3A6AD216-6EE2-43A9-88DE-16D03389778BQ35212921-909173A3-3272-461E-BD68-D6A1B70D4AA7Q35837145-E1A6D3F3-6243-4286-86E2-F019CB3938D3Q36174524-DF2EC647-7E23-48AF-B52E-E584A4EE8FBDQ36243521-2DFBE8D1-1F5A-4A93-8F72-8604F3B858D5Q36546449-E6ED445F-4579-4AA1-B5EA-71BAB9250142Q36664946-84A1C7AC-834D-46B9-AD31-0811043B6A0EQ36775826-104D74EF-F1DA-48BD-BF1F-BE8DA323A69BQ36927073-8C63A3D8-88FD-4218-AEC3-53415CB1EA5CQ37065823-A0CCE443-8C13-49BF-8DA9-B69C8BEFEB53Q37181595-E16CAD16-649F-4903-B7F5-BD5E1080BAC0Q37236772-AD50CBE5-4DF4-4941-BE36-F2B000EE1D05Q37255493-A602DD61-391B-4D01-924B-903EDD2BA6D4Q37395316-700C6487-9AE3-4BD7-B49E-F7C65BF98914Q37534966-32A39680-A20F-41CB-8E43-8AA10363346BQ37583400-175BE7CB-24DA-44AC-9BD0-1ECC1DB1147DQ37596314-5A6008F2-BC19-42C1-8B65-DC589A284DD2Q37629167-7107B25F-460F-480C-B584-0FE9FC23A744Q38290039-17340CD5-542B-4476-8315-426D98428A72Q38605810-8B61F74A-6618-4B24-AC50-D42058A00BA8Q38760758-522A126D-BA20-49B9-A6B2-C3A5DA79ED95Q38837070-5AD55999-7773-4B41-9EBC-209965DDF2B7Q38963298-59D73CD5-FCCD-468F-A4F0-C2DA6C240836Q39398523-651B4ED5-9475-4E0F-8EDA-D9D3E535ECF3
P50
description
biokémikus (?)
@hu
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Miklós Sahin-Tóth
@de
Miklós Sahin-Tóth
@en
Miklós Sahin-Tóth
@es
Miklós Sahin-Tóth
@nl
Miklós Sahin-Tóth
@sl
Miklós Sahin-Tóth
@tr
Sahin-Tóth Miklós
@hu
type
label
Miklós Sahin-Tóth
@de
Miklós Sahin-Tóth
@en
Miklós Sahin-Tóth
@es
Miklós Sahin-Tóth
@nl
Miklós Sahin-Tóth
@sl
Miklós Sahin-Tóth
@tr
Sahin-Tóth Miklós
@hu
prefLabel
Miklós Sahin-Tóth
@de
Miklós Sahin-Tóth
@en
Miklós Sahin-Tóth
@es
Miklós Sahin-Tóth
@nl
Miklós Sahin-Tóth
@sl
Miklós Sahin-Tóth
@tr
Sahin-Tóth Miklós
@hu
P106
P21
P31
P496
0000-0003-4513-9922