Evidence map›Paper›PMID 18443752›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2008

New insights into the role of angiotensin-converting enzyme obtained from the analysis of genetically modified mice.

Xiao Z Shen, Hong D Xiao, Ping Li, Chentao X Lin, Sandrine Billet, Derick Okwan-Duodu, Jon W Adams, Ellen A Bernstein, Yi Xu, Sebastien Fuchs and 1 more

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Will the real angiotensin converting enzyme please stand up?Journal of molecular medicine (Berlin, Germany) · 2012
    Article
  3. Emergence and evolution of the renin-angiotensin-aldosterone system.Journal of molecular medicine (Berlin, Germany) · 2012
    Review
  4. Article
  5. 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

11 authors at 1 institution in 1 country.

Xiao Z ShenDepartment of Pathology, Emory University, 101 Woodruff Circle, Atlanta, GA 30322, USA.
Hong D Xiao
Ping Li
Chentao X Lin
Sandrine Billet
Derick Okwan-Duodu
Jon W Adams
Ellen A Bernstein
Yi Xu
Sebastien Fuchs
Kenneth E Bernstein
Emory University · US

Funding

TESTIS ACE--FUNCTION AND DEVELOPMENTAL EXPRESSIONR01DK051445 · NIDDK · EMORY UNIVERSITY · PI BERNSTEIN, KENNETH E · 1996 to 2008
$2.5M
RENIN/ANGIOTENSIN SYSTEM AND INJURYR01DK039777 · NIDDK · EMORY UNIVERSITY · PI BERNSTEIN, KENNETH E · 1988 to 2010
$1.3M
Importance of the Two Catalytic Sites of ACE in Bleomycin-Induced Lung InjuryK99HL088000 · NHLBI · EMORY UNIVERSITY · PI FUCHS, SEBASTIEN · 2007 to 2008
$177k
NHLBI NIH HHS K99 HL 088000NHLBI NIH HHS K99 HL088000NIDDK NIH HHS R01 DK 039777NIDDK NIH HHS R01 DK039777NIDDK NIH HHS R01 DK 051445NIDDK NIH HHS R01 DK051445
6 · The paper itself

Abstract

Angiotensin-converting enzyme (ACE) has been well-recognized for its role in blood pressure regulation. ACE is made by many tissues, though it is most abundantly expressed on the luminal surface of vascular endothelium. ACE knockout mice show a profound phenotype with low blood pressure, but also with hemopoietic and developmental defects, which complicates understanding the biological functions of ACE in individual tissue types. Using a promoter-swapping strategy, several mouse lines with unique ACE tissue expression patterns were studied. These include mice with ACE expression in the liver (ACE 3/3), the heart (ACE 8/8), and macrophages (ACE 10/10). We also investigated mice with a selective inactivation of either the N- or C-terminal ACE catalytic domain. Our studies indicate that ACE plays a role in many other physiologic processes beyond simple blood pressure control.

Indexed as

AnimalsCatalytic DomainMacrophagesMiceMice, KnockoutMutationOrgan SpecificityPeptidyl-Dipeptidase APeptidyl-Dipeptidase A

Identifiers

PMID18443752
PMCPMC6167991
OpenAlexW2166572906

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.