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

Application of proteomic technology in identifying pancreatic secretory trypsin inhibitor variants in urine of patients with pancreatitis.

Clinical chemistry - 1 Jan 2006

Valmu Leena, Paju Annukka, Lempinen Marko, Kemppainen Esko, Stenman Ulf-Håkan

Abstract excerpt

BACKGROUND: Although the analysis of genetic variability has traditionally been performed with molecular genetic techniques, the development of proteomic technology has raised the possibility of analyzing genetic variants at the protein level. This method provides additional information about posttranslational modifications and differences in expression. We used mass spectrometry to characterize 3 variants of the...

Read the complete abstract on PubMed

Topics

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

Share to Adolescent
Share to Amino Acid Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carrier Proteins

Share to Pancreatitis, Chronic

Share to Proteomics

Share to Sensitivity and Specificity

Share to Spectrometry, Mass, Electrospray Ionization

Share to Trypsin Inhibitor, Kazal Pancreatic

Source

Identifiers

PMID: 16254194
DOI: 10.1373/clinchem.2005.056861

Genes

SPINK1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Application of proteomic technology in identifying pancreatic secretory trypsin inhibitor variants in urine of patients with pancreatitis.PMID 16254194Read ↗

An immunocapture-LC-MS-based assay for serum SPINK1 allows simultaneous quantification and detection of SPINK1 variants.Semantic proximity Read ↗

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

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

Do genetic variants in the SPINK1 gene affect the level of serum PSTI?Semantic proximity Read ↗

Mutations in serine protease inhibitor Kazal type 1 are strongly associated with chronic pancreatitis.Semantic proximity Read ↗

Presence of SPINK-1 variant alters the course of chronic pancreatitis.Semantic proximity Read ↗

Pancreatic secretory trypsin inhibitor (SPINK1) gene mutations in patients with acute pancreatitis.Semantic proximity Read ↗

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

Human cationic trypsinogen but not serine peptidase inhibitor, Kazal type 1 variants increase the risk of type 1 autoimmune 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 ↗

The SPINK1 N34S variant is associated with acute pancreatitis.Semantic proximity Read ↗

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

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