Evidence map›Paper›PMID 32014997›Full record

ArticleThe Journal of biological chemistry2020

Inactivation of mesotrypsin by chymotrypsin C prevents trypsin inhibitor degradation.

Vanda Toldi, András Szabó, Miklós Sahin-Tóth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 37% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Proteases in intestinal health and disease.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Mouse model suggests limited role for human mesotrypsin in pancreatitis.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2021
    Article
  8. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Vanda ToldiDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
András SzabóDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary; Department of Molecular and Cell Biology, Center for Exocrine Disorders, Boston University, Henry M. Goldman School of Dental Medicine, Boston, Massachusetts 02118. Electronic address: andrasszabo@med.unideb.hu.
Miklós Sahin-TóthDepartment of Molecular and Cell Biology, Center for Exocrine Disorders, Boston University, Henry M. Goldman School of Dental Medicine, Boston, Massachusetts 02118; Department of Surgery, University of California Los Angeles, Los Angeles, California 90095. Electronic address: msahintoth@mednet.ucla.edu.
Boston University · USUniversity of Debrecen · HU

Funding

Chymotrypsin in pancreatitisR01DK082412 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SAHIN-TOTH, MIKLOS · 2009 to 2024
$5.8M
Molecular Pathomechanism of Hereditary PancreatitisR01DK058088 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SAHIN-TOTH, MIKLOS · 2001 to 2019
$5.3M
NIDDK NIH HHS R01 DK058088NIDDK NIH HHS R01 DK082412
6 · The paper itself

Abstract

Mesotrypsin is an unusual human trypsin isoform with inhibitor resistance and the ability to degrade trypsin inhibitors. Degradation of the protective serine protease inhibitor Kazal type 1 (SPINK1) by mesotrypsin in the pancreas may contribute to the pathogenesis of pancreatitis. Here we tested the hypothesis that the regulatory digestive protease chymotrypsin C (CTRC) mitigates the harmful effects of mesotrypsin by cleaving the autolysis loop. As human trypsins are post-translationally sulfated in the autolysis loop, we also assessed the effect of this modification. We found that mesotrypsin cleaved in the autolysis loop by CTRC exhibited catalytic impairment on short peptides due to a 10-fold increase in

Indexed as

ProteolysisBiocatalysisCaseinsChymotrypsinHEK293 CellsHumansKineticsMutationTrypsinTrypsin Inhibitor, Kazal PancreaticTrypsin InhibitorsCaseinsChymotrypsinchymotrypsin CPRSS3 protein, humanSPINK1 protein, humanTrypsinTrypsin Inhibitor, Kazal PancreaticTrypsin Inhibitorschymotrypsin Cmesotrypsinpancreasproteaseprotease inhibitortrypsintrypsinogen

Identifiers

PMID32014997
PMCPMC7076226
OpenAlexW3005304294

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.