Evidence map›Paper›PMID 23257181›Full record

ReviewPharmacological reviews2013

A modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzyme.

Kenneth E Bernstein, Frank S Ong, Wendell-Lamar B Blackwell, Kandarp H Shah, Jorge F Giani, Romer A Gonzalez-Villalobos, Xiao Z Shen, Sebastien Fuchs, Rhian M Touyz

Erratum issuedOpen access · bronzeAbstract readHistorical ArticleReview
In one paragraph

Review in Pharmacological reviews, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 147 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed, 4 pooled it
16.0field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 4 syntheses or guidelines pooled it, 318 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Pooled it
  5. Angiotensin-related genetic determinants of cardiovascular disease in patients undergoing hemodialysis.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2019
    Trial
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Multitarget Amaranth Peptides: ACE Inhibition, ACE2 Modulation, and Bioavailability Assessment.Plant foods for human nutrition (Dordrecht, Netherlands) · 2026
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Small Molecule Protease Inhibitors as Model Peptidomimetics.Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  18. Redirecting the Peptide Cleavage Causes Protease Inactivation.Angewandte Chemie (International ed. in English) · 2025
    Article
  19. Review
  20. Review

87 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Kenneth E BernsteinCedars-Sinai Medical Center, 8700 Beverly Boulevard, Davis 2021, Los Angeles, CA 90048, USA. kbernst@cshs.org
Frank S Ong
Wendell-Lamar B Blackwell
Kandarp H Shah
Jorge F Giani
Romer A Gonzalez-Villalobos
Xiao Z Shen
Sebastien Fuchs
Rhian M Touyz
Cedars-Sinai Medical Center · US

Funding

Training Program in Endocrinology, Diabetes, and MetabolismT32DK007770 · NIDDK · CEDARS-SINAI MEDICAL CENTER · PI MELMED, SHLOMO · 1999 to 2022
$3.4M
RAS and InjuryR01HL110353 · NHLBI · CEDARS-SINAI MEDICAL CENTER · PI BERNSTEIN, KENNETH E · 2011 to 2015
$2.2M
Intrarenal Angiotensin II generation during Angiotensin II-induced hypertensionR00DK083455 · NIDDK · CEDARS-SINAI MEDICAL CENTER · PI GONZALEZ-VILLALOBOS, ROMER ANDRES · 2011 to 2013
$720k
NHLBI NIH HHS R01 HL110353NHLBI NIH HHS R01HL110353NIDDK NIH HHS R00 DK083455NIDDK NIH HHS R00DK083455NIDDK NIH HHS T32 DK007770NIDDK NIH HHS T32DK007770PHS HHS F32H105036
6 · The paper itself

Abstract

Angiotensin-converting enzyme (ACE) is a zinc-dependent peptidase responsible for converting angiotensin I into the vasoconstrictor angiotensin II. However, ACE is a relatively nonspecific peptidase that is capable of cleaving a wide range of substrates. Because of this, ACE and its peptide substrates and products affect many physiologic processes, including blood pressure control, hematopoiesis, reproduction, renal development, renal function, and the immune response. The defining feature of ACE is that it is composed of two homologous and independently catalytic domains, the result of an ancient gene duplication, and ACE-like genes are widely distributed in nature. The two ACE catalytic domains contribute to the wide substrate diversity of ACE and, by extension, the physiologic impact of the enzyme. Several studies suggest that the two catalytic domains have different biologic functions. Recently, the X-ray crystal structure of ACE has elucidated some of the structural differences between the two ACE domains. This is important now that ACE domain-specific inhibitors have been synthesized and characterized. Once widely available, these reagents will undoubtedly be powerful tools for probing the physiologic actions of each ACE domain. In turn, this knowledge should allow clinicians to envision new therapies for diseases not currently treated with ACE inhibitors.

Indexed as

Angiotensin-Converting Enzyme InhibitorsAnimalsHistory, 20th CenturyHumansPeptidyl-Dipeptidase APolymorphism, GeneticProtein Structure, TertiaryReninAngiotensin-Converting Enzyme InhibitorsPeptidyl-Dipeptidase ARenin

Identifiers

PMID23257181
PMCPMC3565918
OpenAlexW2126949664

What OpenQuestion holds

Textmetadata
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.