Human cationic trypsinogen is sulfated on Tyr154.

scientific article published on November 2006

Human cationic trypsinogen is sulfated on Tyr154. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1111/J.1742-4658.2006.05501.X
P932PMC publication ID2645268
P698PubMed publication ID17087724
P5875ResearchGate publication ID6708872

P50authorMiklós Sahin-TóthQ38318675
Zsófia NemodaQ38318655
P2093author name stringZoltán Kukor
P2860cites workHuman cationic trypsinogen. Role of Asn-21 in zymogen activation and implications in hereditary pancreatitisQ41734787
Comparative in vitro studies on native and recombinant human cationic trypsins. Cathepsin B is a possible pathological activator of trypsinogen in pancreatitis.Q43581652
Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogenQ46911281
Reduced body weight and increased postimplantation fetal death in tyrosylprotein sulfotransferase-1-deficient mice.Q47187809
A quantitative assay for tyrosine sulfation and tyrosine phosphorylation in peptidesQ53034792
A novel exocrine protein associated with pancreas transplantation in humansQ68169588
Determination and occurrence of tyrosine O-sulfate in proteinsQ70397477
Sulphation of tyrosine residues—a widespread modification of proteinsQ72674597
Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseasesQ24300351
Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2Q24313018
Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteinsQ24317447
Mutations of human cationic trypsinogen (PRSS1) and chronic pancreatitisQ24658116
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151Q27733151
Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegansQ28115054
The Biology and Enzymology of Protein Tyrosine O-SulfationQ28202302
A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitisQ30815377
Characterization of human exocrine pancreatic proteins by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis.Q34274288
Targeted disruption of tyrosylprotein sulfotransferase-2, an enzyme that catalyzes post-translational protein tyrosine O-sulfation, causes male infertilityQ35098792
Chymotrypsin C (caldecrin) stimulates autoactivation of human cationic trypsinogenQ38290039
P433issue22
P407language of work or nameEnglishQ1860
P304page(s)5044-5050
P577publication date2006-11-01
P1433published inFEBS JournalQ1388041
P1476titleHuman cationic trypsinogen is sulfated on Tyr154.
P478volume273

Reverse relations

cites work (P2860)
Q37236772A common African polymorphism abolishes tyrosine sulfation of human anionic trypsinogen (PRSS2).
Q50127788Distinguishing Sulfotyrosine Containing Peptides from their Phosphotyrosine Counterparts Using Mass Spectrometry
Q37693897Human trypsinogens in the pancreas and in cancer
Q89517074Inactivation of mesotrypsin by chymotrypsin C prevents trypsin inhibitor degradation
Q40036264Mass spectrometric detection of tyrosine sulfation in human pancreatic trypsinogens, but not in tumor-associated trypsinogen
Q35534772Protein surface charge of trypsinogen changes its activation pattern
Q33970780Sequence analysis of the human tyrosylprotein sulfotransferase-2 gene in subjects with chronic pancreatitis
Q34635652Systematic analysis of the in situ crosstalk of tyrosine modifications reveals no additional natural selection on multiply modified residues.
Q37065823Tighter Control by Chymotrypsin C (CTRC) Explains Lack of Association between Human Anionic Trypsinogen and Hereditary Pancreatitis
Q57286529Trypsinogen isoforms in the ferret pancreas
Q35204469Tyrosine sulfation of human trypsin steers S2' subsite selectivity towards basic amino acids.

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