Evidence map›Paper›PMID 29702251›Full record

ReviewNitric oxide : biology and chemistry2018

Structure/function of the soluble guanylyl cyclase catalytic domain.

Kenneth C Childers, Elsa D Garcin

Open access · hybridAbstract readReview
In one paragraph

Review in Nitric oxide : biology and chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. The discovery of hidden guanylate cyclases (GCs) in theComputational and structural biotechnology journal · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Memory Enhancers for Alzheimer's Dementia: Focus on cGMP.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Kenneth C ChildersUniversity of Maryland Baltimore County, Department of Chemistry and Biochemistry, Baltimore, USA.
Elsa D GarcinUniversity of Maryland Baltimore County, Department of Chemistry and Biochemistry, Baltimore, USA. Electronic address: egarcin@umbc.edu.
University of Maryland, Baltimore County · US

Funding

Graduate Training at The Chemistry Biology InterfaceT32GM066706 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SELEY-RADTKE, KATHERINE L, SMITH, AARON T · 2004 to 2023
$3.3M
Identifying Long-range Interaction NetworKs (LINKs) in soluble guanylate cyclase to regulate intraocular pressure: implications for new glaucoma therapies.R21EY026663 · NEI · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI GARCIN, ELSA D · 2017 to 2018
$363k
NEI NIH HHS R21 EY026663NIGMS NIH HHS T32 GM066706
6 · The paper itself

Abstract

Soluble guanylyl cyclase (GC-1) is the primary receptor of nitric oxide (NO) in smooth muscle cells and maintains vascular function by inducing vasorelaxation in nearby blood vessels. GC-1 converts guanosine 5'-triphosphate (GTP) into cyclic guanosine 3',5'-monophosphate (cGMP), which acts as a second messenger to improve blood flow. While much work has been done to characterize this pathway, we lack a mechanistic understanding of how NO binding to the heme domain leads to a large increase in activity at the C-terminal catalytic domain. Recent structural evidence and activity measurements from multiple groups have revealed a low-activity cyclase domain that requires additional GC-1 domains to promote a catalytically-competent conformation. How the catalytic domain structurally transitions into the active conformation requires further characterization. This review focuses on structure/function studies of the GC-1 catalytic domain and recent advances various groups have made in understanding how catalytic activity is regulated including small molecules interactions, Cys-S-NO modifications and potential interactions with the NO-sensor domain and other proteins.

Indexed as

Catalytic DomainAnimalsBiocatalysisHumansNitric OxideProtein ConformationSoluble Guanylyl CyclaseStructure-Activity RelationshipNitric OxideSoluble Guanylyl CyclaseActivation mechanismAdenylyl cyclaseCatalytic domainNitric oxideS-nitrosationSoluble guanylyl cyclase

Identifiers

PMID29702251
PMCPMC6005667
OpenAlexW2799987636

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.