Evidence map›Paper›PMID 18267127›Full record

ReviewBiochimica et biophysica acta2008

Redox compartmentalization in eukaryotic cells.

Young-Mi Go, Dean P Jones

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 281 papers.

0numbers the graph read from it
0cells of the map it votes in
281citing papers in PubMed
13.9field-weighted citation impact, top 1% 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

281 citing papers in PubMed, 613 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Use of Human Serum Albumin CysAntioxidants (Basel, Switzerland) · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Navigating the redox landscape: reactive oxygen species in regulation of cell cycle.Redox report : communications in free radical research · 2024
    Review
  18. Article
  19. Structure-activity relationships and pharmacokinetic evaluation of L-cystine diamides as L-cystine crystallization inhibitors for cystinuria.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2024
    Article
  20. Article

221 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

Young-Mi GoEmory Clinical Biomarkers Laboratory and Division of Pulmonary, Allergy and Critical Care Medicine, Department of Medicine, Emory University, Atlanta GA 30322, USA.
Dean P Jones
Emory Clinic · USEmory University · US

Funding

Thioredoxin-2 protection against mitochondrial oxidative toxicityR01ES009047 · NIEHS · EMORY UNIVERSITY · PI JONES, DEAN PAUL · 1998 to 2013
$3.9M
Nuclear and Cytoplasmic Redox in Oxidative StressR01ES011195 · NIEHS · EMORY UNIVERSITY · PI JONES, DEAN PAUL · 2001 to 2011
$3.3M
NIEHS NIH HHS ES009047NIEHS NIH HHS ES011195NIEHS NIH HHS R01 ES009047NIEHS NIH HHS R01 ES011195
6 · The paper itself

Abstract

Diverse functions of eukaryotic cells are optimized by organization of compatible chemistries into distinct compartments defined by the structures of lipid-containing membranes, multiprotein complexes and oligomeric structures of saccharides and nucleic acids. This structural and chemical organization is coordinated, in part, through cysteine residues of proteins which undergo reversible oxidation-reduction and serve as chemical/structural transducing elements. The central thiol/disulfide redox couples, thioredoxin-1, thioredoxin-2, GSH/GSSG and cysteine/cystine (Cys/CySS), are not in equilibrium with each other and are maintained at distinct, non-equilibrium potentials in mitochondria, nuclei, the secretory pathway and the extracellular space. Mitochondria contain the most reducing compartment, have the highest rates of electron transfer and are highly sensitive to oxidation. Nuclei also have more reduced redox potentials but are relatively resistant to oxidation. The secretory pathway contains oxidative systems which introduce disulfides into proteins for export. The cytoplasm contains few metabolic oxidases and this maintains an environment for redox signaling dependent upon NADPH oxidases and NO synthases. Extracellular compartments are maintained at stable oxidizing potentials. Controlled changes in cytoplasmic GSH/GSSG redox potential are associated with functional state, varying with proliferation, differentiation and apoptosis. Variation in extracellular Cys/CySS redox potential is also associated with proliferation, cell adhesion and apoptosis. Thus, cellular redox biology is inseparable from redox compartmentalization. Further elucidation of the redox control networks within compartments will improve the mechanistic understanding of cell functions and their disruption in disease.

Indexed as

Cell CompartmentationAnimalsEndocytosisEukaryotic CellsHumansOrganellesOxidation-Reduction

Identifiers

PMID18267127
PMCPMC2601570
OpenAlexW1995565650

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.