Evidence map›Paper›PMID 24458023›Full record

ReviewAmerican journal of physiology. Gastrointestinal and liver physiology2014

Human cationic trypsinogen (PRSS1) variants and chronic pancreatitis.

Balázs Csaba Németh, Miklós Sahin-Tóth

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Gastrointestinal and liver physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Pathologically relevant trypsinogen activation in pancreatitis.American journal of physiology. Gastrointestinal and liver physiology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Roles ofJournal of Zhejiang University. Science. B · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Misfolding PRSS1 variant p.Ala61Val in a case of suspected intrauterine pancreatitis.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Mouse model of PRSS1 p.R122H-related hereditary pancreatitis highlights context-dependent effect of autolysis-site mutation.Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] · 2023
    Article
  16. Chronic pancreatitis caused by a HomozygousJournal of pediatric genetics · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Balázs Csaba NémethDepartment of Molecular and Cell Biology, Henry M. Goldman School of Dental Medicine, Boston University, Boston, Massachusetts.
Miklós Sahin-Tóth
Boston University · US

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
Pancreatic elastasesR01DK095753 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SAHIN-TOTH, MIKLOS · 2013 to 2016
$1.4M
NIDDK NIH HHS R01 DK058088NIDDK NIH HHS R01DK058088NIDDK NIH HHS R01 DK082412NIDDK NIH HHS R01DK082412NIDDK NIH HHS R01 DK095753NIDDK NIH HHS R01DK095753
6 · The paper itself

Abstract

Variations in the serine protease 1 (PRSS1) gene encoding human cationic trypsinogen have been conclusively associated with autosomal dominant hereditary pancreatitis and sporadic nonalcoholic chronic pancreatitis. Most high-penetrance PRSS1 variants increase intrapancreatic trypsin activity by stimulating trypsinogen autoactivation and/or by inhibiting chymotrypsin C-dependent trypsinogen degradation. Alternatively, some PRSS1 variants can cause trypsinogen misfolding, which results in intracellular retention and degradation with consequent endoplasmic reticulum stress. However, not all PRSS1 variants are pathogenic, and clinical relevance of rare variants is often difficult to ascertain. Here we review the PRSS1 variants published since 1996 and discuss their functional properties and role in chronic pancreatitis.

Indexed as

AnimalsHumansModels, AnimalPancreatitis, ChronicPolymorphism, GeneticTrypsinPRSS1 protein, humanTrypsin

Identifiers

PMID24458023
PMCPMC3949028
OpenAlexW2119054539

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.