Assembly of the oxidative phosphorylation system in humans: What we have learned by studying its defects
Open accessAbstract
Assembly of the oxidative phosphorylation (OXPHOS) system in the mitochondrial inner membrane is an intricate process in which many factors must interact. The OXPHOS system is composed of four respiratory chain complexes, which are responsible for electron transport and generation of the proton gradient in the mitochondrial intermembrane space, and of the ATP synthase that uses this proton gradient to produce ATP. Mitochondrial human disorders are caused by dysfunction of the OXPHOS system, and many of them are associated with altered assembly of one or more components of the OXPHOS system. The study of assembly defects in patients has been useful in unraveling and/or gaining a complete understanding of the processes by which these large multimeric complexes are formed. We review here current knowledge of the biogenesis of OXPHOS complexes based on investigation of the corresponding disorders.
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
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?
Normal respiration requires the coordinated production of subunits for proper assembly into functional complexes.
“Normal respiration requires the coordinated production of subunits for proper assembly into functional complexes [81].”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [81]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Clinical and molecular findings in children with complex I deficiency
Bugiani, M., Invernizzi, F., Alberio, S., Briem, E., Lamantea, E., Carrara, F., Moroni, I., Farina, L., Spada, M., Donati, M. A., et al. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.09.006 · Cited by 264 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 5
- Online Mendelian Inheritance in Man, OMIM. McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University (Baltimore, MD) and National Center for Biotechnology Information, National Library of Medicine (Bethesda, MD). Consulted on January and February 2008. World Wide Web URL: http://www. ncbi.nlm.nih.gov/omim/.
- V.K. Mootha, P. Lepage, K. Miller, J. Bunkenborg, M. Reich, M. Hjerrild, T. Delmonte, A. Villeneuve, R. Sladek, F. Xu, G.A. Mitchell, C. Morin, M. Mann, T.J. Hudson, B. Robinson, J.D. Rioux, E.S. Lander, Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics, Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 605-610.
- J.W. Taanman, S.L. Williams, Assembly of cytochrome c oxidase: what can we learn from patients with cytochrome c oxidase deficiency? Biochem. Soc. Trans. 29 (2001) 446-451.
- S.H. Ackerman, A. Tzagoloff, Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F 1 -ATPase, Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 4986-4990.
- X. Zeng, W. Neupert, A. Tzagoloff. The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase, Mol. Biol. Cell. 18 (2007) 617-626.
Cited by
Sorted by citations
Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network
Scarpulla, R. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.019 · Cited by 1,281 · see citing works
Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein
Richter-Dennerlein, R., Oeljeklaus, S., Lorenzi, I., Ronsör, C., Bareth, B., Schendzielorz, A. B., Wang, C., Warscheid, B., Rehling, P., & Dennerlein, S. (2016) · Cell · doi:10.1016/j.cell.2016.09.003 · Cited by 232 · see citing works
Smits, P., Smeitink, J., & van den Heuvel, L. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2010/737385 · Cited by 202 · see citing works
Orr, A. L., Kim, C., Jimenez-Morales, D., Newton, B. W., Johnson, J. R., Krogan, N. J., Swaney, D. L., & Mahley, R. W. (2019) · Journal of Alzheimer's Disease · doi:10.3233/jad-181184 · Cited by 103 · see citing works
Mitochondrial localization, import, and mitochondrial function of the androgen receptor
Bajpai, P., Koc, E., Sonpavde, G., Singh, R., & Singh, K. K. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006727 · Cited by 99 · see citing works
Sensing the Stress: A Role for the UPRmt and UPRam in the Quality Control of Mitochondria
Callegari, S., & Dennerlein, S. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00031 · Cited by 58 · see citing works
- Authors
- Fernández-Vizarra, E., Tiranti, V., & Zeviani, M.
- Affiliations
- Fondazione IRCCS Istituto Neurologico Carlo Besta (IT)
- Corresponding author
- Zeviani, Massimo
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 1793
- Issue
- 1
- Pages
- 200-211
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2117488437
- Cited by
- 214
- References
- 1
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 5 · 2023: 7 · 2022: 7 · 2021: 10 · 2020: 15 · 2019: 15 · 2018: 11 · 2017: 11 · 2016: 10 · 2015: 12 · 2014: 10 · 2013: 12 · 2012: 25
- FWCI
- 1.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- European Commission
- Fondazione Telethon
- Ministero della Salute
- Fondazione Pierfranco e Luisa Mariani (RF2006)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- oxidative phosphorylation, respiratory chain complexes, ATP synthase, mitochondrial biogenesis, mitochondrial disease, electron transport, proton gradient, human disease
- MeSH terms
- Electron Transport Complex IV, DNA, Mitochondrial, Electron Transport, Humans, Models, Biological, Mutation, Oxidative Phosphorylation, Electron Transport Complex III, Molecular Chaperones, Mitochondrial Diseases, Electron Transport Complex I, Electron Transport Chain Complex Proteins
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
