Evidence map›Paper›PMID 33571505›Full record

ArticleBiochemical pharmacology2021

Higher susceptibility to heme oxidation and lower protein stability of the rare α

Iraida Sharina, Karina Lezgyieva, Yekaterina Krutsenko, Emil Martin

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical pharmacology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. ML355 Modulates Platelet Activation and Prevents ABT-737 Induced Apoptosis in Platelets.The Journal of pharmacology and experimental therapeutics · 2022
    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

4 authors.

Iraida SharinaUniversity of Texas Health Science Center, McGovern Medical School, Department of Internal Medicine, Division of Cardiology, United States.
Karina LezgyievaSchool of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Yekaterina KrutsenkoSchool of Science and Technology, Nazarbayev University, Astana, Kazakhstan.
Emil MartinUniversity of Texas Health Science Center, McGovern Medical School, Department of Internal Medicine, Division of Cardiology, United States. Electronic address: emil.martin@uth.tmc.edu.

Funding

Regulation of sGC vascular function by the Activator of G-protein Signaling 3R01HL139838 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MARTIN, EMIL · 2018 to 2021
$1.5M
NHLBI NIH HHS R01 HL139838
6 · The paper itself

Abstract

NO sensitive soluble guanylyl cyclase (sGC) plays a key role in mediating physiological functions of NO. Genetic alterations of the GUCY1A3 gene, coding for the α1 subunit of sGC, are associated with several cardiovascular dysfunctions. A rare sGC variant with Cys517 → Tyr substitution in the α1subunit, has been associated with moyamoya disease and achalasia. In this report we characterize the properties of this rare sGC variant. Purified α

Indexed as

AnimalsChlorocebus aethiopsCOS CellsDose-Response Relationship, DrugGenetic VariationHemeHumansMoyamoya DiseaseOxadiazolesOxazinesOxidation-ReductionProtein StabilityProtein Structure, SecondarySf9 CellsSoluble Guanylyl CyclaseGUCY1A1 protein, humanHemeNS 2028OxadiazolesOxazinesSoluble Guanylyl CyclasecGMPNitric oxideOxidative stressProtein stabilitySoluble guanylyl cyclase

Identifiers

PMID33571505
PMCPMC8052303

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.