Evidence map›Paper›PMID 33067882›Full record

ArticleThe FEBS journal2021

Angiotensin-converting enzyme open for business: structural insights into the subdomain dynamics.

Gyles E Cozier, Lizelle Lubbe, Edward D Sturrock, K Ravi Acharya

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Multitarget Amaranth Peptides: ACE Inhibition, ACE2 Modulation, and Bioavailability Assessment.Plant foods for human nutrition (Dordrecht, Netherlands) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Epitope mapping of novel monoclonal antibodies to human angiotensin I-converting enzyme.Protein science : a publication of the Protein Society · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Gyles E CozierDepartment of Biology and Biochemistry, University of Bath, Bath, UK.ORCID 0000-0003-2851-0902
Lizelle LubbeDepartment of Integrative Biomedical Sciences, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Cape Town, South Africa.ORCID 0000-0001-9905-1438
Edward D SturrockDepartment of Integrative Biomedical Sciences, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Cape Town, South Africa.ORCID 0000-0003-2032-7636
K Ravi AcharyaDepartment of Biology and Biochemistry, University of Bath, Bath, UK.ORCID 0000-0002-3009-4058
University of Bath · GBUniversity of Cape Town · ZA

Funding

Medical Research Council MR/M026647/1
6 · The paper itself

Abstract

Angiotensin-1-converting enzyme (ACE) is a key enzyme in the renin-angiotensin-aldosterone and kinin systems where it cleaves angiotensin I and bradykinin peptides, respectively. However, ACE also participates in numerous other physiological functions, can hydrolyse many peptide substrates and has various exo- and endopeptidase activities. ACE achieves this complexity by containing two homologous catalytic domains (N- and C-domains), which exhibit different substrate specificities. Here, we present the first open conformation structures of ACE N-domain and a unique closed C-domain structure (2.0 Å) where the C terminus of a symmetry-related molecule is observed inserted into the active-site cavity and binding to the zinc ion. The open native N-domain structure (1.85 Å) enables comparison with ACE2, a homologue previously observed in open and closed states. An open S

Indexed as

Protein ConformationAngiotensin-Converting Enzyme InhibitorsBinding SitesCatalytic DomainCrystallography, X-RayDatabases, ProteinHumansPeptidyl-Dipeptidase AProtein BindingSubstrate SpecificityAngiotensin-Converting Enzyme InhibitorsPeptidyl-Dipeptidase Aangiotensin-1-converting enzymedomain dynamicsenzyme mechanismenzyme structuremetalloproteaseX-ray crystallography

Identifiers

PMID33067882
PMCPMC8048788
OpenAlexW3093283395

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.