Evidence map›Paper›PMID 25900980›Full record

ReviewBlood2015

Regulation of thrombosis and vascular function by protein methionine oxidation.

Sean X Gu, Jeff W Stevens, Steven R Lentz

Open access · bronzeAbstract readReview
In one paragraph

Review in Blood, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

43 citing papers in PubMed, 81 citations in OpenAlex.

  1. Trial
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  3. Trial
  4. Article
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  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Cysteine and methionine oxidation in thrombotic disorders.Current opinion in chemical biology · 2023
    Review
  16. Article
  17. Review
  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

3 authors at 1 institution in 1 country.

Sean X GuDepartment of Internal Medicine, University of Iowa Carver College of Medicine, Iowa City, IA.
Jeff W StevensDepartment of Internal Medicine, University of Iowa Carver College of Medicine, Iowa City, IA.
Steven R LentzDepartment of Internal Medicine, University of Iowa Carver College of Medicine, Iowa City, IA.
University of Iowa · US

Funding

Vascular Protection During HypertensionP01HL062984 · NHLBI · UNIVERSITY OF IOWA · PI FARACI, FRANK M · 2000 to 2015
$22.2M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM007337 · NIGMS · UNIVERSITY OF IOWA · PI GEYER, PAMELA K., LENTZ, STEVEN R · 1985 to 2020
$15.9M
Vascular Mechanisms in Homocysteinemia and AtherosclerosisR01HL063943 · NHLBI · UNIVERSITY OF IOWA · PI LENTZ, STEVEN R · 2000 to 2012
$4.0M
NHLBI NIH HHS HL062984NHLBI NIH HHS HL063943NHLBI NIH HHS P01 HL062984NHLBI NIH HHS R01 HL063943NIGMS NIH HHS GM007337NIGMS NIH HHS T32 GM007337
6 · The paper itself

Abstract

Redox biology is fundamental to both normal cellular homeostasis and pathological states associated with excessive oxidative stress. Reactive oxygen species function not only as signaling molecules but also as redox regulators of protein function. In the vascular system, redox reactions help regulate key physiologic responses such as cell adhesion, vasoconstriction, platelet aggregation, angiogenesis, inflammatory gene expression, and apoptosis. During pathologic states, altered redox balance can cause vascular cell dysfunction and affect the equilibrium between procoagulant and anticoagulant systems, contributing to thrombotic vascular disease. This review focuses on the emerging role of a specific reversible redox reaction, protein methionine oxidation, in vascular disease and thrombosis. A growing number of cardiovascular and hemostatic proteins are recognized to undergo reversible methionine oxidation, in which methionine residues are posttranslationally oxidized to methionine sulfoxide. Protein methionine oxidation can be reversed by the action of stereospecific enzymes known as methionine sulfoxide reductases. Calcium/calmodulin-dependent protein kinase II is a prototypical methionine redox sensor that responds to changes in the intracellular redox state via reversible oxidation of tandem methionine residues in its regulatory domain. Several other proteins with oxidation-sensitive methionine residues, including apolipoprotein A-I, thrombomodulin, and von Willebrand factor, may contribute to vascular disease and thrombosis.

Indexed as

Oxidation-ReductionAnimalsHumansMethionineOxidative StressProteinsReactive Oxygen SpeciesThrombosisVascular DiseasesMethionineProteinsReactive Oxygen Species

Identifiers

PMID25900980
PMCPMC4473114
OpenAlexW2076156854

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.