Evidence map›Paper›PMID 20513478›Full record

ReviewMethods in enzymology2010

Measurement and identification of S-glutathiolated proteins.

Bradford G Hill, Kota V Ramana, Jian Cai, Aruni Bhatnagar, Satish K Srivastava

Abstract readReview
In one paragraph

Review in Methods in enzymology, 2010. 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
–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

25 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Redox RegulationAntioxidants & redox signaling · 2020
    Review
  9. Article
  10. NaAutism research : official journal of the International Society for Autism Research · 2018
    Article
  11. Suppression of External NADPH Dehydrogenase-NDB1 inInternational journal of molecular sciences · 2018
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Dysfunctional mitochondrial bioenergetics and oxidative stress in Akita(+/Ins2)-derived β-cells.American journal of physiology. Endocrinology and metabolism · 2013
    Article
  19. S-glutathionylation in monocyte and macrophage (dys)function.International journal of molecular sciences · 2013
    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

5 authors.

Bradford G HillDiabetes and Obesity Center, University of Louisville, Louisville, Kentucky, USA.
Kota V Ramana
Jian Cai
Aruni Bhatnagar
Satish K Srivastava

Funding

Tumor Necrosis Factor Modulation of CPCsP01HL078825 · NHLBI · UNIVERSITY OF LOUISVILLE · PI BOLLI, ROBERTO · 2005 to 2021
$37.6M
STEM CELLS AND DIABETIC CARDIOMYOPATHY PROJ 2 2009P20RR024489 · NCRR · UNIVERSITY OF LOUISVILLE · PI BHATNAGAR, ARUNI · 2008 to 2011
$10.0M
TOXICITY OF 4-HYDROXYALKENALS IN HEARTR01HL055477 · NHLBI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI BHATNAGAR, ARUNI · 1997 to 2015
$4.4M
Role of Aldose Reductase in Diabetic ComplicationsR37DK036118 · NIDDK · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI SRIVASTAVA, SATISH K · 2003 to 2013
$4.1M
CARDIAC METABOLISM OF ENALSR01HL059378 · NHLBI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI BHATNAGAR, ARUNI · 1998 to 2011
$3.3M
Aldose Reductase: A Regulator of Inflammatory SignalsR01GM071036 · NIGMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI RAMANA, KOTA VENKATA · 2005 to 2011
$1.8M
ALDOSE REDUCTASE AND DIABETIC COMPLICATIONSR01DK036118 · NIDDK · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI SRIVASTAVA, SATISH K · 1987 to 2002
$626k
Structural Biology /Structural Genomics of TraffickingZ01DK036118 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI HURLEY, JAMES H · 1994 to 2006
–
Intramural NIH HHS Z01 DK036118NCRR NIH HHS P20 RR024489NCRR NIH HHS RR-024489NHLBI NIH HHS HL-55477NHLBI NIH HHS HL-59378NHLBI NIH HHS HL-78825NHLBI NIH HHS P01 HL078825NHLBI NIH HHS R01 HL055477NHLBI NIH HHS R01 HL059378NIDDK NIH HHS R01 DK036118NIDDK NIH HHS R37 DK036118NIGMS NIH HHS GM71036NIGMS NIH HHS R01 GM071036
6 · The paper itself

Abstract

Protein thiol modifications occur under both physiological and pathological conditions and can regulate protein function, redox signaling, and cell viability. The thiolation of proteins by glutathione (GSH) appears to be a particularly important mode of posttranslational modification that is increased under conditions of oxidative or nitrosative stress. Modification of proteins by glutathiolation has been shown to affect the structure and function of several susceptible proteins and protect them from subsequent oxidative injury. In many cases, the glutathiolated proteins are low in abundance, and dethiolation occurs readily. Therefore, sensitive, reliable, and reproducible methods are required for measuring both the total levels of protein glutathiolation and for identifying glutathiolated proteins under given conditions. These methods necessitate the preservation or the controlled removal of the GSH adducts during sample preparation for the accurate measurement of total S-glutathiolation and for the identification of protein-GSH adducts. In this chapter, we briefly review and provide protocols for chemical, mass spectrometric, immunological, and radioactive tagging techniques, for measuring protein S-glutathiolation in cells and tissues.

Indexed as

Clinical Laboratory TechniquesAnimalsCellsGlutathioneHumansOxidation-ReductionProtein Processing, Post-TranslationalProteinsSpectrometry, Mass, Electrospray IonizationStaining and LabelingSulfhydryl CompoundsSulfonic AcidsTissue ExtractsGlutathioneProteinsSulfhydryl CompoundsSulfonic AcidsTissue Extracts

Identifiers

PMID20513478
PMCPMC3142817

What OpenQuestion holds

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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.