Evidence map›Paper›PMID 17471184›Full record

ReviewBritish journal of pharmacology2007

Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties.

K Oettl, R E Stauber

Open access · bronzeAbstract readReview
In one paragraph

Review in British journal of pharmacology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
143citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 3% 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

143 citing papers in PubMed, 1 synthesis or guideline pooled it, 346 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Review
  5. Observational
  6. Article
  7. Prognostic Value of Albumin/Globulin Ratio for Mortality in Stage 2 Cardiovascular-Kidney-Metabolic Syndrome: A Nationwide Cohort Analysis (1999-2018).High blood pressure & cardiovascular prevention : the official journal of the Italian Society of Hypertension · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Use of Human Serum Albumin CysAntioxidants (Basel, Switzerland) · 2026
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Declining Serum Albumin With Stable Body Mass Index: A Mortality Indicator in Predialysis Chronic Kidney Disease.Journal of renal nutrition : the official journal of the Council on Renal Nutrition of the National Kidney Foundation · 2025
    Article

83 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 1 institution in 1 country.

K OettlInstitute of Physiological Chemistry, Center of Physiological Medicine, Medical University of Graz, Graz, Austria. karl.oettl@meduni-graz.at
R E Stauber
Medical University of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Binding and transport of a number of endogenous and exogenous compounds is an important function of the main plasma protein, albumin. In vivo and in vitro, albumin may be oxidatively modified in different ways with different agents at different sites. These modifications have various consequences on the physiological functions of albumin. Diabetes mellitus, liver diseases and nephropathy are just a few examples of disorders in which oxidative stress is involved and altered albumin functions have been described. This review is focussed on the consequences of oxidative modification on the binding properties of albumin. These range from no effect to decreased or increased binding affinities depending on the ligand under investigation and the type of modification. Indicators for modification include glycosylation, disulphide formation or the content of carbonyl groups. The redox state of albumin can affect the binding properties in several ways, including altered conformation and consequently altered affinities at binding sites and altered binding when the binding reaction itself is redox sensitive. The physiological or pathophysiological concentrations of different oxidatively modified albumin molecules vary over a wide range and are crucial in assessing the clinical relevance of altered ligand binding properties of a particularly modified albumin species in various disease conditions.

Indexed as

HumansOxidation-ReductionOxidative StressProtein BindingSerum AlbuminSerum Albumin

Identifiers

PMID17471184
PMCPMC2013999
OpenAlexW1977892627

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.