Evidence map›Paper›PMID 18242196›Full record

ArticleFree radical biology & medicine2008

Oxidative modification of cytochrome c by singlet oxygen.

Junhwan Kim, Myriam E Rodriguez, Ming Guo, Malcolm E Kenney, Nancy L Oleinick, Vernon E Anderson

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2008. 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
3.8field-weighted citation impact, top 7% 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, 64 citations in OpenAlex.

  1. Singlet Oxygen in Photodynamic Therapy.Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Chemoptogenetic damage to mitochondria causes rapid telomere dysfunction.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Laminin targeting of a peripheral nerve-highlighting peptide enables degenerated nerve visualization.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Review
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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

6 authors at 1 institution in 1 country.

Junhwan KimDepartment of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106-4935, USA.
Myriam E Rodriguez
Ming Guo
Malcolm E Kenney
Nancy L Oleinick
Vernon E Anderson
Case Western Reserve University · US

Funding

SULFHYDRYL STATUS IN THE AGING HEART: ROLE OF GLUTAREDOXINP01AG015885 · NIA · CASE WESTERN RESERVE UNIVERSITY · PI LESNEFSKY, EDWARD J · 1998 to 2008
$8.1M
SYNTHESIS OF PHTHALOCYANINES FOR TUMOR PHOTOTHERAPYP01CA048735 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI OLEINICK, NANCY L · 1990 to 2002
$3.3M
PHOTOTHERAPY OF PROSTATE CANCER--PRO AND ANTI APOPTOSISR01CA083917 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI OLEINICK, NANCY L · 2000 to 2006
$2.3M
The Maternal/Fetal InteractionR01AI055739 · NIAID · MONTANA STATE UNIVERSITY - BOZEMAN · PI SCHMIDT, EDWARD E · 2005 to 2009
$1.7M
Cardiolipin in Photodynamic TherapyR01CA106491 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI OLEINICK, NANCY L · 2005 to 2008
$972k
NCI NIH HHS P01 CA048735NCI NIH HHS P01 CA48735NCI NIH HHS R01 CA083917NCI NIH HHS R01 CA106491NIAID NIH HHS P01 AI55739NIAID NIH HHS R01 AI055739NIA NIH HHS P01 AG015885
6 · The paper itself

Abstract

Singlet oxygen ((1)O(2)) is a reactive oxygen species that may be generated in biological systems. Photodynamic therapy generates (1)O(2) by photoexcitation of sensitizers resulting in intracellular oxidative stress and induction of apoptosis. (1)O(2) oxidizes amino acid side chains of proteins and inactivates enzymes when generated in vitro. Among proteogenic amino acids, His, Tyr, Met, Cys, and Trp are known to be oxidized by (1)O(2) at physiological pH. However, there is a lack of direct evidence of oxidation of proteins by (1)O(2). Because (1)O(2) is difficult to detect in cells, identifying oxidized cellular products uniquely derived from (1)O(2) could serve as a marker of its presence. In the present study, (1)O(2) reactions with model peptides analyzed by tandem mass spectrometry provide insight into the mass of prominent adducts formed with the reactive amino acids. Analysis by MALDI-TOF and tandem mass spectrometry of peptides of cytochrome c exposed to (1)O(2) generated by photoexcitation of the phthalocyanine Pc 4 showed unique oxidation products, which might be used as markers of the presence of (1)O(2) in the mitochondrial intermembrane space. Differences in the elemental composition of the oxidized amino acid residues observed with cytochrome c and the model peptides suggest that the protein environment can affect the oxidation pathway.

Indexed as

AnimalsApoptosisCytochromes cHistidineHorsesHydrogen-Ion ConcentrationMethionineMitochondriaModels, BiologicalModels, ChemicalMyocardiumOxygenPhotochemotherapyReactive Oxygen SpeciesTryptophanCytochromes cHistidineMethionineOxygenReactive Oxygen SpeciesTryptophan

Identifiers

PMID18242196
PMCPMC2424268
OpenAlexW2042778264

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.