Evidence map›Paper›PMID 21375693›Full record

ReviewThe FEBS journal2011

Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase.

Kunio S Misono, John S Philo, Tsutomu Arakawa, Craig M Ogata, Yue Qiu, Haruo Ogawa, Howard S Young

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 94 citations in OpenAlex.

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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

7 authors at 5 institutions in 3 countries.

Kunio S MisonoUniversity of Nevada School of Medicine, Reno, NV 89557, USA. kmisono@unr.edu
John S Philo
Tsutomu Arakawa
Craig M Ogata
Yue Qiu
Haruo Ogawa
Howard S Young
Alliance Protein Laboratories (United States) · USUniversity of Nevada, Reno · USArgonne National Laboratory · USThe University of Tokyo · JPUniversity of Alberta · CA

Funding

NATRIURETIC PEPTIDE RECEPTOR--STRUCTURE AND SIGNALINGR01HL054329 · NHLBI · UNIVERSITY OF NEVADA RENO · PI MISONO, KUNIO S · 1996 to 2005
$1.5M
CIHRNHLBI NIH HHS HL54329NHLBI NIH HHS R01 HL054329
6 · The paper itself

Abstract

Atrial natriuretic peptide (ANP) and the homologous B-type natriuretic peptide are cardiac hormones that dilate blood vessels and stimulate natriuresis and diuresis, thereby lowering blood pressure and blood volume. ANP and B-type natriuretic peptide counterbalance the actions of the renin-angiotensin-aldosterone and neurohormonal systems, and play a central role in cardiovascular regulation. These activities are mediated by natriuretic peptide receptor-A (NPRA), a single transmembrane segment, guanylyl cyclase (GC)-linked receptor that occurs as a homodimer. Here, we present an overview of the structure, possible chloride-mediated regulation and signaling mechanism of NPRA and other receptor GCs. Earlier, we determined the crystal structures of the NPRA extracellular domain with and without bound ANP. Their structural comparison has revealed a novel ANP-induced rotation mechanism occurring in the juxtamembrane region that apparently triggers transmembrane signal transduction. More recently, the crystal structures of the dimerized catalytic domain of green algae GC Cyg12 and that of cyanobacterium GC Cya2 have been reported. These structures closely resemble that of the adenylyl cyclase catalytic domain, consisting of a C1 and C2 subdomain heterodimer. Adenylyl cyclase is activated by binding of G(s)α to C2 and the ensuing 7° rotation of C1 around an axis parallel to the central cleft, thereby inducing the heterodimer to adopt a catalytically active conformation. We speculate that, in NPRA, the ANP-induced rotation of the juxtamembrane domains, transmitted across the transmembrane helices, may induce a similar rotation in each of the dimerized GC catalytic domains, leading to the stimulation of the GC catalytic activity.

Indexed as

Molecular StructureSignal TransductionAmino Acid SequenceAnimalsGuanylate CyclaseMolecular Sequence DataNatriuretic PeptidesProtein ConformationRatsReceptors, Atrial Natriuretic FactorSequence Homology, Amino AcidGuanylate CyclaseNatriuretic PeptidesReceptors, Atrial Natriuretic Factor

Identifiers

PMID21375693
PMCPMC3097287
OpenAlexW1573211116

What OpenQuestion holds

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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.