Evidence map›Paper›PMID 23198874›Full record

ReviewAntioxidants & redox signaling2013

Molecular controls of the oxygenation and redox reactions of hemoglobin.

Celia Bonaventura, Robert Henkens, Abdu I Alayash, Sambuddha Banerjee, Alvin L Crumbliss

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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  9. Article
  10. Review
  11. Journal of the American Chemical Society · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. βCysteine 93 in human hemoglobin: a gateway to oxidative stability in health and disease.Laboratory investigation; a journal of technical methods and pathology · 2021
    Review
  18. Article
  19. Review
  20. Nitrite and nitrate chemical biology and signalling.British journal of pharmacology · 2019
    Review
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

5 authors.

Celia BonaventuraNicholas School of the Environment, Duke University Marine Laboratory, Beaufort, NC 28516, USA. bona@duke.edu
Robert Henkens
Abdu I Alayash
Sambuddha Banerjee
Alvin L Crumbliss

Funding

Recombinant HbAp Production for In Vivo Toxicity StudiesP01HL110900 · NHLBI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI FRIEDMAN, JOEL M · 2012 to 2016
$10.6M
NHLBI NIH HHS P01 HL110900
6 · The paper itself

Abstract

significanceThe broad classes of O(2)-binding proteins known as hemoglobins (Hbs) carry out oxygenation and redox functions that allow organisms with significantly different physiological demands to exist in a wide range of environments. This is aided by allosteric controls that modulate the protein's redox reactions as well as its O(2)-binding functions. RECENT ADVANCES: The controls of Hb's redox reactions can differ appreciably from the molecular controls for Hb oxygenation and come into play in elegant mechanisms for dealing with nitrosative stress, in the malarial resistance conferred by sickle cell Hb, and in the as-yet unsuccessful designs for safe and effective blood substitutes. CRITICAL ISSUES: An important basic principle in consideration of Hb's redox reactions is the distinction between kinetic and thermodynamic reaction control. Clarification of these modes of control is critical to gaining an increased understanding of Hb-mediated oxidative processes and oxidative toxicity in vivo. FUTURE DIRECTIONS: This review addresses emerging concepts and some unresolved questions regarding the interplay between the oxygenation and oxidation reactions of structurally diverse Hbs, both within red blood cells and under acellular conditions. Developing methods that control Hb-mediated oxidative toxicity will be critical to the future development of Hb-based blood substitutes.

Indexed as

Oxygen ConsumptionAnimalsBlood SubstitutesHemoglobinsHumansOxidation-ReductionOxygenProtein BindingBlood SubstitutesHemoglobinsOxygen

Identifiers

PMID23198874
PMCPMC4047995

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.