Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and Biophysical Insights into SPINK1 Bound to Human Cationic Trypsin.

International journal of molecular sciences - 23 Mar 2022

Nagel Felix, Palm Gottfried J, Geist Norman, McDonnell Thomas C R, Susemihl Anne, Girbardt Britta, Mayerle Julia, Lerch Markus M, Lammers Michael, Delcea Mihaela

Abstract excerpt

(1) The serine protease inhibitor Kazal type 1 (SPINK1) inhibits trypsin activity in zymogen granules of pancreatic acinar cells. Several mutations in the SPINK1 gene are associated with acute recurrent pancreatitis (ARP) and chronic pancreatitis (CP). The most common variant is SPINK1 p.N34S. Although this mutation was identified two decades ago, the mechanism of action has remained elusive. (2) SPINK1 and human...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli
Share to Genetic Predisposition to Disease

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Pancreatitis, Chronic

Share to Trypsin

Share to Trypsin Inhibitor, Kazal Pancreatic

Source

Open in PubMed Open full text

Identifiers

PMID: 35408828
DOI: 10.3390/ijms23073468
PMCID: PMC8998336

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Biophysical Insights into SPINK1 Bound to Human Cationic Trypsin.PMID 35408828Read ↗

Defective binding of SPINK1 variants is an uncommon mechanism for impaired trypsin inhibition in chronic pancreatitisSemantic proximity Read ↗

Inhibition of mouse trypsin isoforms by SPINK1 and effect of human pancreatitis-associated mutations.Semantic proximity Read ↗

The N34S mutation of SPINK1 may impact the kinetics of trypsinogen activation to cause early trypsin release in the pancreasSemantic proximity Read ↗

Mutations in the gene encoding the serine protease inhibitor, Kazal type 1 are associated with chronic pancreatitis.Semantic proximity Read ↗

Phenotypic variability of the homozygous IVS3+2T>C mutation in the serine protease inhibitor Kazal type 1 (SPINK1) gene in patients with chronic pancreatitis.Semantic proximity Read ↗

Pathogenic cellular role of the p.L104P human cationic trypsinogen variant in chronic pancreatitis.Semantic proximity Read ↗

Serine protease inhibitor Kazal type 1 mutations and pancreatitis.Semantic proximity Read ↗

Genetics and clinical implications of SPINK1 in the pancreatitis continuum and pancreatic cancer.Semantic proximity Read ↗

Mutations of the serine protease inhibitor, Kazal type 1 gene, in patients with idiopathic chronic pancreatitisSemantic proximity Read ↗

Is the SPINK1 variant p.N34S overrepresented in patients with acute pancreatitis?Semantic proximity Read ↗

Serine Protease Inhibitor Kazal Type I (SPINK1) Mutation: A Risk Factor for Early-onset Chronic Pancreatitis?Semantic proximity Read ↗

Two novel severe mutations in the pancreatic secretory trypsin inhibitor gene (SPINK1) cause familial and/or hereditary pancreatitis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.