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

The Arg92Cys colipase polymorphism impairs function and secretion by increasing protein misfolding.

Journal of lipid research - 1 Feb 2013

Xiao Xunjun, Ferguson Michael R, Magee Kelsey E, Hale Pamela D, Wang Yan, Lowe Mark E

Abstract excerpt

Colipase is essential for efficient fat digestion. An arginine-to-cysteine polymorphism at position 92 of colipase (Arg92Cys) associates with an increased risk for developing type-2 diabetes through an undefined mechanism. To test our hypothesis that the extra cysteine increases colipase misfolding, thereby altering its intracellular trafficking and function, we expressed Cys92 colipase in HEK293T cells. Less...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cysteine
Share to Dietary Fats

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to HEK293 Cells

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 23204298
DOI: 10.1194/jlr.M034066
PMCID: PMC3837459

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

The Arg92Cys colipase polymorphism impairs function and secretion by increasing protein misfolding.PMID 23204298Read ↗

Missense PNLIP mutations impeding pancreatic lipase secretion cause protein misfolding and endoplasmic reticulum stress.Semantic proximity Read ↗

Diabetes and pancreatic exocrine dysfunction due to mutations in the carboxyl ester lipase gene-maturity onset diabetes of the young (CEL-MODY): a protein misfolding disease.Semantic proximity Read ↗

A Carboxyl Ester Lipase (CEL) Mutant Causes Chronic Pancreatitis by Forming Intracellular Aggregates That Activate Apoptosis.Semantic proximity Read ↗

Single nucleotide polymorphisms in CEL-HYB1 increase risk for chronic pancreatitis through proteotoxic misfolding.Semantic proximity Read ↗

The position of single-base deletions in the VNTR sequence of the carboxyl ester lipase (CEL) gene determines proteotoxicity.Semantic proximity Read ↗

The role of the carboxyl ester lipase (CEL) gene in pancreatic disease.Semantic proximity Read ↗

Novel p.G250A Mutation Associated with Chronic Pancreatitis Highlights Misfolding-Prone Region in Carboxypeptidase A1 (CPA1).Semantic proximity Read ↗

Genetic variability of procolipase associates with altered insulin secretion in non-diabetic Caucasians.Semantic proximity Read ↗

Structure-function relationships in naturally occurring mutants of pancreatic lipase.Semantic proximity Read ↗

Structural requirements for the stability and microsomal transport activity of the human glucose 6-phosphate transporter.Semantic proximity Read ↗

The position of single-base deletions in the VNTR sequence of the carboxyl ester lipase ( <i>CEL</i> ) gene determines pathogenicitySemantic proximity Read ↗

Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.Semantic proximity Read ↗

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