The DOI matches its Crossref record; 73 of the 74 references it cites were found in a registry or an index.
Mitochondrial proton leak and the uncoupling protein 1 homologues
Open accessAbstract
Mitochondrial proton leak is the largest single contributor to the standard metabolic rate (SMR) of a rat, accounting for about 20% of SMR. Yet the mechanisms by which proton leak occurs are incompletely understood. The available evidence suggests that both phospholipids and proteins in the mitochondrial inner membrane are important determinants of proton conductance. The uncoupling protein 1 homologues (e.g. UCP2, UCP3) may play a role in mediating proton leak, but it is unlikely they account for all of the observed proton conductance. Experimental data regarding the functions of these proteins include important ambiguities and contradictions which must be addressed before their function can be confirmed. The physiological role of the proton leak, and of the uncoupling protein 1 homologues, remains similarly unclear.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“However, the single-electron transfers are tightly controlled and quickly coupled with the second electron transfer (107, 293, 294).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [294]
In the citing paper
“However, it is now widely accepted that, in brown adipose tissue (BAT), UCP1 does function in this way.”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [300]
In the citing paper
“However, this overexpression is clearly not physiologic (300).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [300]
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
Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia
Fleury, C., Neverova, M., Collins, S., Raimbault, S., Champigny, O., Lévi-Meyrueis, C., Bouillaud, F., Seldin, M. F., Surwit, R. S., Ricquier, D., et al. (1997) · Nature Genetics · doi:10.1038/ng0397-269 · Cited by 1,630
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
Boss, O., Samec, S., Paoloni‐Giacobino, A., Rossier, C., Dulloo, A. G., Seydoux, J., Muzzin, P., & Giacobino, J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00384-0 · Cited by 1,041
Uncoupling: new approaches to an old problem of bioenergetics
Skulachev, V. P. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(97)00091-1 · Cited by 893
Phospholipid vesicle formation and transmembrane protein incorporation using octyl glucoside
Mimms, L. T., Zampighi, G. A., Nozaki, Y., Tanford, C., & Reynolds, J. A. (1981) · Biochemistry · doi:10.1021/bi00507a028 · Cited by 679
Energy 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
Synthetic Amphiphilic Peptide Models for Protein Ion Channels
Lear, J. D., Wasserman, Z. R., & DeGrado, W. F. (1988) · Science · doi:10.1126/science.2453923 · Cited by 607
Mice overexpressing human uncoupling protein-3 in skeletal muscle are hyperphagic and lean
Clapham, J. C., Arch, J. R. S., Chapman, H., Haynes, A., Lister, C., Moore, G. B. T., Piercy, V., Carter, S. A., Lehner, I., Smith, S. A., et al. (2000) · Nature · doi:10.1038/35019082 · Cited by 604
Self-citationPaula, S., Volkov, A. G., Van Hoek, A. N., Haines, T. H., & Deamer, D. W. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79575-9 · Cited by 578
Reactive oxygen species, mitochondria, apoptosis and aging
Papa, S., & Skulachev, V. P. (1997) · Springer eBooks · doi:10.1007/978-1-4615-6111-8_47 · Cited by 467
Research works printed but not linked: 5
- B. Cannon, A. Matthias, V. Golozoubova, K.B.E. Ohlson, U. Andersson, A. Jacobsson, J. Nedergaard, Unifying and distinguishing features of brown and white adipose tissues: UCP1 versus other UCPs, in: G. Ailhaud, B. Guy-Grands (Eds.), Progress in Obesity Research, John Libbey and Company, 1999, pp. 13–26.
- Ricquier, 2000, The UCP family: where are we?, Int. J. Obes., 24, S10
- Stuart, 2000, An uncoupling artifact can accompany uncoupling protein-1 expression in yeast mitochondria, Int. J. Obes., 24, S187
- Cadenas, 2000, Human uncoupling protein-3 overexpression increases mitochondrial proton leak, Int. J. Obes., 24, S187
- M.B. Jekabsons, B.A. Horwitz, Nucleotide effects on liver and muscle mitochondrial nonphosphorylating respiration and membrane potential, Biochim. Biophys. Acta, in press.
Cited by
Sorted by citations
Brown Adipose Tissue: Function and Physiological Significance
CANNON, B., & NEDERGAARD, J. (2004) · Physiological Reviews · doi:10.1152/physrev.00015.2003 · Cited by 6,433
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
Self-citationSivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742
The mitochondrial uncoupling-protein homologues
Krauss, S., Zhang, C., & Lowell, B. B. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1592 · Cited by 670
Mitochondrial uncoupling, ROS generation and cardioprotection
Cadenas, S. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.019 · Cited by 591
Self-citation
Metadata
- Authors
- Stuart, J. A., Cadenas, S., Jekabsons, M. B., Roussel, D., & Brand, M. D.
- Affiliations
- University of Cambridge (GB)
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Brand, M.D
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2001-03
- Volume
- 1504
- Issue
- 1
- Pages
- 144-158
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2051826214
- Cited by
- 169
- References
- 74
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 7 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 2 · 2015: 4 · 2014: 2 · 2013: 5 · 2012: 5
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- mitochondrial proton leak, UCP2, UCP3, inner mitochondrial membrane, proton conductance, standard metabolic rate, mitochondrial membrane phospholipids, mitochondrial membrane proteins
- MeSH terms
- Uncoupling Protein 2, Uncoupling Protein 3, Uncoupling Protein 1, Amino Acid Sequence, Animals, Basal Metabolism, Carrier Proteins, Diffusion, Humans, Intracellular Membranes, Ion Channels, Membrane Proteins, Mitochondria, Molecular Sequence Data, Proteins, Protons, RNA, Messenger, Sequence Alignment, Sequence Homology, Models, Animal, Mitochondrial Proteins, Membrane Transport Proteins, Animals, Genetically Modified
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
