The DOI matches its Crossref record; 122 of the 122 references it cites were found in a registry or an index.
The thiol pool in human plasma: The central contribution of albumin to redox processes
Open accessAbstract
The plasma compartment has particular features regarding the nature and concentration of low and high molecular weight thiols and oxidized derivatives. Plasma is relatively poor in thiol-based antioxidants; thiols are in lower concentrations than in cells and mostly oxidized. The different thiol-disulfide pairs are not in equilibrium and the steady-state concentrations of total thiols as well as reduced versus oxidized ratios are maintained by kinetic barriers, including the rates of reactions and transport processes. The single thiol of human serum albumin (HSA-SH) is the most abundant plasma thiol. It is an important target for oxidants and electrophiles due to its reactivity with a wide variety of species and its relatively high concentration. A relatively stable sulfenic (HSA-SO3H) acid can be formed in albumin exposed to oxidants. Plasma increases in mixed disulfides (HSA-SSR) or in sulfinic (HSA-SO2H) and sulfonic (HSA-SO3H) acids are associated with different pathologies and may constitute biomarkers of the antioxidant role of the albumin thiol. In this work we provide a critical review of the plasma thiol pool with a focus on human serum albumin.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
All About Albumin: Biochemistry, Genetics, and Medical Applications
Peters, T. (1995) · Thammasat University Digital Collections · Cited by 3,090
Bilirubin Is an Antioxidant of Possible Physiological Importance
Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N., & Ames, B. N. (1987) · Science · doi:10.1126/science.3029864 · Cited by 2,948
Peroxynitrite oxidation of sulfhydryls.
Radi, R., Beckman, J. S., Bush, K. M., & Freeman, B. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,490
Self-citationHomocysteine and Cardiovascular Disease
Refsum, H., Ueland, P. M., Nygård, O., & Vollset, S. E. (1998) · Annual Review of Medicine · doi:10.1146/annurev.med.49.1.31 · Cited by 2,180
Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles
Kratz, F. (2008) · Journal of Controlled Release · doi:10.1016/j.jconrel.2008.05.010 · Cited by 2,151
Crystal structure of human serum albumin at 2.5 Å resolution
Sugio, S., Kashima, A., Mochizuki, S., Noda, M., & Kobayashi, K. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.6.439 · Cited by 1,786
Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726
[41] Measurement of protein thiol groups and glutathione in plasma
Hu, M.-L. (1994) · Methods in Enzymology · doi:10.1016/s0076-6879(94)33044-1 · Cited by 953
Bhattacharya, A. A., Grüne, T., & Curry, S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4158 · Cited by 905
Real-time imaging of the intracellular glutathione redox potential
Gutscher, M., Pauleau, A.-L., Marty, L., Brach, T., Wabnitz, G. H., Samstag, Y., Meyer, A. J., & Dick, T. P. (2008) · Nature Methods · doi:10.1038/nmeth.1212 · Cited by 894
Cited by
N-Acetylcysteine as an antioxidant and disulphide breaking agent: the reasons why
Aldini, G., Altomare, A., Baron, G., Vistoli, G., Carini, M., Borsani, L., & Sergio, F. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1468564 · Cited by 830
Rushworth, G. F., & Megson, I. L. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.09.006 · Cited by 719
Pedre, B., Barayeu, U., Ezeriņa, D., & Dick, T. P. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107916 · Cited by 470
Serum albumin in health and disease: esterase, antioxidant, transporting and signaling properties
Belinskaia, D. A., Voronina, P. A., Shmurak, V. I., Jenkins, R. O., & Goncharov, N. V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910318 · Cited by 416
Molecular interactions at the surface of extracellular vesicles
Buzás, E. I., Tóth, E. Á., Sódar, B. W., & Szabó-Taylor, K. É. (2018) · Seminars in Immunopathology · doi:10.1007/s00281-018-0682-0 · Cited by 375
Metadata
- Authors
- Turell, L., Radi, R., & Alvarez, B.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 65
- Pages
- 244-253
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2085056486
- Cited by
- 708
- References
- 122
- FWCI
- 12.24
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The thiol pool in human plasma: The central contribution of albumin to redox processes. https://app.cochat.ai/papers/10.1016/j.freeradbiomed.2013.05.050
- The paper
- Turell, L., Radi, R., & Alvarez, B. (2013). The thiol pool in human plasma: The central contribution of albumin to redox processes. Free Radical Biology and Medicine. https://doi.org/10.1016/j.freeradbiomed.2013.05.050
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
