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

Genetic variation of human aspartic proteinases.

Scandinavian journal of clinical and laboratory investigation. Supplementum - 1 Jan 1992

Taggart R T

Abstract excerpt

The human aspartic proteinases include pepsinogen A, pepsinogen C, cathepsin D, cathepsin E and renin. Comparative analysis of the proteinase genes reveals a high degree of similarity with regard to their respective coding sequences and the location of exon-intron junctions. Despite strong conservation of the regions containing the active site aspartyl groups, genetic polymorphisms have been identified for each...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Aspartic Acid Endopeptidases
Share to Base Sequence

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

Share to Cathepsins

Share to Genetic Variation

Share to Molecular Sequence Data

Source

Identifiers

PMID: 1455173

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

Genetic variation of human aspartic proteinases.PMID 1455173Read ↗

Mammalian Glutamyl Aminopeptidase Genes (ENPEP) and Proteins: Comparative Studies of a Major Contributor to Arterial HypertensionSemantic proximity Read ↗

Structural and phylogenetic comparison of napsin genes: the duplication, loss of function and human-specific pseudogenization of napsin B.Semantic proximity Read ↗

Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease.Semantic proximity Read ↗

Genomic structure of human lysosomal glycosylasparaginase.Semantic proximity Read ↗

Dissection of the molecular pathology of aspartylglucosaminuria provides the basis for DNA diagnostics and future therapeutic interventions.Semantic proximity Read ↗

A highly informative polymorphism of the pepsinogen C gene detected by polymerase chain reaction.Semantic proximity Read ↗

A novel aspartoacylase (ASPA) gene mutation in Canavan disease.Semantic proximity Read ↗

Tissue-specific Expression Patterns and Fine Mapping of the Human Kallikrein (KLK) Locus on Proximal 19q13.4Semantic proximity Read ↗

Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase familiesSemantic proximity Read ↗

Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.Semantic proximity Read ↗

Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.Semantic proximity Read ↗

Mutation analysis of the aspartoacylase gene in non-Jewish patients with Canavan disease.Semantic proximity Read ↗

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