The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
The Biology of Mitochondrial Uncoupling Proteins
Abstract
Uncoupling proteins (UCPs) are mitochondrial transporters present in the inner membrane of mitochondria. They are found in all mammals and in plants. They belong to the family of anion mitochondrial carriers including adenine nucleotide transporters. The term “uncoupling protein” was originally used for UCP1, which is uniquely present in mitochondria of brown adipocytes, the thermogenic cells that maintain body temperature in small rodents. In these cells, UCP1 acts as a proton carrier activated by free fatty acids and creates a shunt between complexes of the respiratory chain and ATP synthase. Activation of UCP1 enhances respiration, and the uncoupling process results in a futile cycle and dissipation of oxidation energy as heat. UCP2 is ubiquitous and highly expressed in the lymphoid system, macrophages, and pancreatic islets. UCP3 is mainly expressed in skeletal muscles. In comparison to the established uncoupling and thermogenic activities of UCP1, UCP2 and UCP3 appear to be involved in the limitation of free radical levels in cells rather than in physiological uncoupling and thermogenesis. Moreover, UCP2 is a regulator of insulin secretion and UCP3 is involved in fatty acid metabolism.
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
Thermogenic mechanisms in brown fat.
Nicholls, D. G., & Locke, R. M. (1984) · Physiological Reviews · doi:10.1152/physrev.1984.64.1.1 · Cited by 1,602
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382
Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese
Enerbäck, S., Jacobsson, A., Simpson, E. M., Guerra, C., Yamashita, H., Harper, M.-E., & Kozak, L. P. (1997) · Nature · doi:10.1038/387090a0 · Cited by 1,379
Mitochondria, oxygen free radicals, disease and ageing
Raha, S., & Robinson, B. H. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01674-1 · Cited by 1,066 · cited 1×
“Respiration is associated with production of reactive oxygen species (ROS) because the oxygen molecule is capable of accepting an additional electron to create the superoxide ion, a more reactive form of oxygen (34).”
BackgroundEnergy metabolism in uncoupling protein 3 gene knockout mice
Vidal-Puig, A. J., Grujic, D., Zhang, C.-Y., Hagen, T., Boss, O., Ido, Y., Szczepanik, A., Wade, J., Mootha, V., Cortright, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910179199 · Cited by 677
Transport function and regulation of mitochondrial uncoupling proteins 2 and 3
Jabůrek, M., Vařecha, M., Gimeno, R. E., Dembski, M., Ježek, P., Zhang, M., Burn, P., Tartaglia, L. A., & Garlid, K. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26003 · Cited by 321
Skeletal muscle respiratory uncoupling prevents diet-induced obesity and insulin resistance in mice
Li, B., Nolte, L. A., Ju, J.-S., Ho Han, D., Coleman, T., Holloszy, J. O., & Semenkovich, C. F. (2000) · Nature Medicine · doi:10.1038/80450 · Cited by 291
Mitochondrial proton leak and the uncoupling protein 1 homologues
Stuart, J. A., Cadenas, S., Jekabsons, M. B., Roussel, D., & Brand, M. D. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00243-7 · Cited by 169
Couplan, E., del Mar Gonzalez-Barroso, M., Alves-Guerra, M. C., Ricquier, D., Goubern, M., & Bouillaud, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202535200 · Cited by 161
Self-citationDiehl, A. M., & Hoek, J. B. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005452624640 · Cited by 95
Cited by
den Besten, G., Bleeker, A., Gerding, A., van Eunen, K., Havinga, R., van Dijk, T. H., Oosterveer, M. H., Jonker, J. W., Groen, A. K., Reijngoud, D.-J., et al. (2015) · Diabetes · doi:10.2337/db14-1213 · Cited by 1,125
Oxidative Stress and the Pathogenesis of Alzheimer's Disease
Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855
Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells
Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715
Thermogenic Mechanisms and Their Hormonal Regulation
Silva, J. E. (2006) · Physiological Reviews · doi:10.1152/physrev.00009.2005 · Cited by 687
Is Alzheimer’s disease a type 3 diabetes? A critical appraisal
Kandimalla, R., Thirumala, V., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.018 · Cited by 621
Metadata
- Authors
- Rousset, S., Alves-Guerra, M.-C., Mozo, J., Miroux, B., Cassard-Doulcier, A.-M., Bouillaud, F., & Ricquier, D.
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2004-02-01
- Volume
- 53
- Issue
- suppl_1
- Pages
- S130-S135
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2104645520
- Cited by
- 553
- References
- 11
- FWCI
- 11.92
- Type
- journal article
- Language
- en
- Open access
- closed
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 Biology of Mitochondrial Uncoupling Proteins. https://app.cochat.ai/papers/10.2337/diabetes.53.2007.s130
- The paper
- Rousset, S., Alves-Guerra, M.-C., Mozo, J., Miroux, B., Cassard-Doulcier, A.-M., Bouillaud, F., & Ricquier, D. (2004). The Biology of Mitochondrial Uncoupling Proteins. Diabetes. https://doi.org/10.2337/diabetes.53.2007.s130
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.
