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

Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region.

The Journal of biological chemistry - 23 Feb 2001

Eyries M, Michaud A, Deinum J, Agrapart M, Chomilier J, Kramers C, Soubrier F

Abstract excerpt

Angiotensin-converting enzyme (ACE), an enzyme that plays a major role in vasoactive peptide metabolism, is a type 1 ectoprotein, which is released from the plasma membrane by a proteolytic cleavage occurring in the stalk sequence adjacent to the membrane anchor. In this study, we have discovered the molecular mechanism underlying the marked increase of plasma ACE levels observed in three unrelated individuals....

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 Dipeptides

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

Share to Hydroxamic Acids

Share to Netherlands

Share to Peptidyl-Dipeptidase A

Share to Protein Structure, Tertiary

Share to Solubility

Share to Tetradecanoylphorbol Acetate

Source

Identifiers

PMID: 11076943
DOI: 10.1074/jbc.M007706200

Genes

ACE

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

Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region.PMID 11076943Read ↗

Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease.Semantic proximity Read ↗

An angiotensin I-converting enzyme mutation (Y465D) causes a dramatic increase in blood ACE via accelerated ACE shedding.Semantic proximity Read ↗

Angiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACE.Semantic proximity Read ↗

Defining the boundaries of the testis angiotensin I-converting enzyme ectodomain.Semantic proximity Read ↗

A Novel Splice-Site Mutation in Angiotensin I-Converting Enzyme (ACE) Gene, c.3691+1G>A (IVS25+1G>A), Causes a Dramatic Increase in Circulating ACE through Deletion of the Transmembrane AnchorSemantic proximity Read ↗

The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity.Semantic proximity Read ↗

Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints.Semantic proximity Read ↗

Fine epitope mapping of monoclonal antibodies 9B9 and 3G8 to the N domain of angiotensin-converting enzyme (CD143) defines a region involved in regulating angiotensin-converting enzyme dimerization and shedding.Semantic proximity Read ↗

A novel angiotensin I-converting enzyme mutation (S333W) impairs N-domain enzymatic cleavage of the anti-fibrotic peptide, AcSDKP.Semantic proximity Read ↗

Proteolytic release of membrane proteins: studies on a membrane-protein-solubilizing activity in CHO cells.Semantic proximity Read ↗

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.Semantic proximity Read ↗

Phenotyping Angiotensin-Converting Enzyme in Blood: A Necessary Approach for Precision Medicine.Semantic proximity Read ↗

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