Evidence map›Paper›PMID 18793332›Full record

ReviewJournal of internal medicine2008

Renin-angiotensin system revisited.

F Fyhrquist, O Saijonmaa

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of internal medicine, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 244 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
244citing papers in PubMed, 3 pooled it
23.4field-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

244 citing papers in PubMed, 3 syntheses or guidelines pooled it, 631 citations in OpenAlex.

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  16. Role of muscle-related genes in sleep bruxism : Understanding the genetic aspect of this behavior.Journal of orofacial orthopedics = Fortschritte der Kieferorthopadie : Organ/official journal Deutsche Gesellschaft fur Kieferorthopadie · 2025
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184 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

F FyhrquistMinerva Institute for Medical Research and Department of Internal Medicine, Helsinki University Central Hospital, Helsinki, Finland. frej.fyhrquist@helsinki.fi
O Saijonmaa
Helsinki University Hospital · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

New components and functions of the renin-angiotensin system (RAS) are still being unravelled. The classical RAS as it looked in the middle 1970s consisted of circulating renin, acting on angiotensinogen to produce angiotensin I, which in turn was converted into angiotensin II (Ang II) by angiotensin-converting enzyme (ACE). Ang II, still considered the main effector of RAS was believed to act only as a circulating hormone via angiotensin receptors, AT1 and AT2. Since then, an expanded view of RAS has gradually emerged. Local tissue RAS systems have been identified in most organs. Recently, evidence for an intracellular RAS has been reported. The new expanded view of RAS therefore covers both endocrine, paracrine and intracrine functions. Other peptides of RAS have been shown to have biological actions; angiotensin 2-8 heptapeptide (Ang III) has actions similar to those of Ang II. Further, the angiotensin 3-8 hexapeptide (Ang IV) exerts its actions via insulin-regulated amino peptidase receptors. Finally, angiotensin 1-7 (Ang 1-7) acts via mas receptors. The discovery of another ACE2 was an important complement to this picture. The recent discovery of renin receptors has made our view of RAS unexpectedly complex and multilayered. The importance of RAS in cardiovascular disease has been demonstrated by the clinical benefits of ACE inhibitors and AT1 receptor blockers. Great expectations are now generated by the introduction of renin inhibitors. Indeed, RAS regulates much more and diverse physiological functions than previously believed.

Indexed as

Angiotensin-Converting Enzyme 2Angiotensin-Converting Enzyme InhibitorsAngiotensin IAngiotensin IIAngiotensin IIIHumansPeptide FragmentsPeptidyl-Dipeptidase AProrenin ReceptorReceptor, Angiotensin, Type 1Receptors, Cell SurfaceRenin-Angiotensin SystemVacuolar Proton-Translocating ATPasesACE2 protein, humanAngiotensin-Converting Enzyme 2Angiotensin-Converting Enzyme InhibitorsAngiotensin Iangiotensin I (1-7)Angiotensin IIangiotensin II, des-Asp(1)-des-Arg(2)-Ile(5)-Angiotensin IIIATP6AP2 protein, humanPeptide FragmentsPeptidyl-Dipeptidase AProrenin ReceptorReceptor, Angiotensin, Type 1Receptors, Cell SurfaceVacuolar Proton-Translocating ATPases

Identifiers

PMID18793332
PMCPMC7166930
OpenAlexW1978998472

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.