Evidence map›Paper›PMID 26906466›Full record

ReviewAntioxidants & redox signaling2017

Thiol-Based Redox Modulation of Soluble Guanylyl Cyclase, the Nitric Oxide Receptor.

Annie Beuve

Open access · hybridAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
4.3field-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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.

  1. Pooled it
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  18. Nitric Oxide Mediated Degradation of CYP2A6 via the Ubiquitin-Proteasome Pathway in Human Hepatoma Cells.Drug metabolism and disposition: the biological fate of chemicals · 2020
    Article
  19. Article
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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

1 author at 1 institution in 1 country.

Annie BeuveDepartment of Pharmacology, Physiology and Neuroscience, New Jersey Medical School-Rutgers , Newark, New Jersey.
Rutgers, The State University of New Jersey · US

Funding

Regulation of Soluble Guanylyl Cyclase, the NO-ReceptorR01GM067640 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI BEUVE, ANNIE V · 2003 to 2021
$5.8M
NO signaling by a Soluble Guanylyl Cyclase-Thioredoxin transnitrosation complexR01GM112415 · NIGMS · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI BEUVE, ANNIE V · 2015 to 2023
$3.5M
NIGMS NIH HHS R01 GM067640NIGMS NIH HHS R01 GM112415
6 · The paper itself

Abstract

significanceSoluble guanylyl cyclase (sGC), which produces the second messenger cyclic guanosine 3', 5'-monophosphate (cGMP), is at the crossroads of nitric oxide (NO) signaling: sGC catalytic activity is both stimulated by NO binding to the heme and inhibited by NO modification of its cysteine (Cys) thiols (S-nitrosation). Modulation of sGC activity by thiol oxidation makes sGC a therapeutic target for pathologies originating from oxidative or nitrosative stress. sGC has an unusually high percentage of Cys for a cytosolic protein, the majority solvent exposed and therefore accessible modulatory targets for biological and pathophysiological signaling. Recent Advances: Thiol oxidation of sGC contributes to the development of cardiovascular diseases by decreasing NO-dependent cGMP production and thereby vascular reactivity. This thiol-based resistance to NO (e.g., increase in peripheral resistance) is observed in hypertension and hyperaldosteronism. CRITICAL ISSUES: Some roles of specific Cys thiols have been identified in vitro. So far, it has not been possible to pinpoint the roles of specific Cys of sGC in vivo and to investigate the molecular mechanisms in an animal model. FUTURE DIRECTIONS: The role of Cys as redox sensors, intermediates of activation, and mediators of change in sGC conformation, activity, and dimerization remains largely unexplored. To understand modulation of sGC activity, it is critical to investigate the roles of specific oxidative thiol modifications that are formed during these processes. Where the redox state of sGC thiols contribute to pathologies (vascular resistance and sGC desensitization by NO donors), it becomes crucial to design therapeutic strategies to restore sGC to its normal, physiological thiol redox state. Antioxid. Redox Signal. 26, 137-149.

Indexed as

Oxidation-ReductionAnimalsCardiovascular DiseasesCatalysisCysteineHemeHumansNitric OxideNitrosationProtein BindingSoluble Guanylyl CyclaseSolventsStructure-Activity RelationshipSulfhydryl CompoundsCysteineHemeNitric OxideSoluble Guanylyl CyclaseSolventsSulfhydryl Compoundsguanylyl cyclasenitric oxideoxidative stressreactive cysteineS-nitrosationS-nitrosylation

Identifiers

PMID26906466
PMCPMC5240013
OpenAlexW2283092967

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.