Evidence map›Paper›PMID 11416199›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration.

S Marcondes, I V Turko, F Murad

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 78 citations in OpenAlex.

  1. Trial
  2. Review
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  4. Article
  5. Review
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  8. Article
  9. Article
  10. Review
  11. Regulation of Ketone Body Metabolism and the Role of PPARα.International journal of molecular sciences · 2016
    Review
  12. Article
  13. Ketone body metabolism and cardiovascular disease.American journal of physiology. Heart and circulatory physiology · 2013
    Review
  14. Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.American journal of physiology. Endocrinology and metabolism · 2013
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Mechanisms of disease: the oxidative stress theory of diabetic neuropathy.Reviews in endocrine & metabolic disorders · 2008
    Review
  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.

S MarcondesDepartment of Integrative Biology and Pharmacology and Institute of Molecular Medicine, University of Texas Medical School, Houston, TX 77030, USA.
I V Turko
F Murad
Texas Medical Center · US

Funding

ROLE OF PROTEIN NITRATION AND NITRIC OXIDER01HL064221 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MURAD, FERID · 2000 to 2003
$1.2M
NHLBI NIH HHS HL64221NHLBI NIH HHS R01 HL064221
6 · The paper itself

Abstract

The tyrosine nitration of proteins has been observed in diverse inflammatory conditions and has been linked to the presence of reactive nitrogen species. From many in vitro experiments, it is apparent that tyrosine nitration may alter the function of proteins. A limited number of experiments under in vivo conditions also demonstrate that protein nitration is associated with altered cellular processes. To understand the association of protein nitration with the pathogenic mechanism of the disease, it is essential to identify specific protein targets of nitration with in vivo or intact tissue models. Using anti-nitrotyrosine antibodies, we demonstrated the accumulation of nitrotyrosine in a 52-kDa protein in rat kidney after lipopolysaccharide treatment. The 52-kDa protein was purified and identified with partial sequence as succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC ). Western blot analysis revealed that the nitration of this mitochondrial enzyme increased in the kidneys and hearts of lipopolysaccharide-treated rats, whereas its catalytic activity decreased. These data suggest that tyrosine nitration may be a mechanism for the inhibition of SCOT activity in inflammatory conditions. SCOT is a key enzyme for ketone body utilization. Thus, tyrosine nitration of the enzyme with sepsis or inflammation may explain the altered metabolism of ketone bodies present in these disorders.

Indexed as

Amino Acid SequenceAnimalsBrainCoenzyme A-TransferasesEndotoxinsEscherichia coliKidneyLipopolysaccharidesMaleMitochondriaMitochondria, HeartRatsRats, WistarThiobarbituric Acid Reactive SubstancesTyrosine3-ketoacid CoA-transferase3-nitrotyrosineCoenzyme A-TransferasesEndotoxinsLipopolysaccharidesThiobarbituric Acid Reactive SubstancesTyrosine

Identifiers

PMID11416199
PMCPMC34637
OpenAlexW2020105615

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.