The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Cyclophilin D Modulates Mitochondrial F0F1-ATP Synthase by Interacting with the Lateral Stalk of the Complex
Open accessAbstract
Blue native gel electrophoresis purification and immunoprecipitation of F(0)F(1)-ATP synthase from bovine heart mitochondria revealed that cyclophilin (CyP) D associates to the complex. Treatment of intact mitochondria with the membrane-permeable bifunctional reagent dimethyl 3,3-dithiobis-propionimidate (DTBP) cross-linked CyPD with the lateral stalk of ATP synthase, whereas no interactions with F(1) sector subunits, the ATP synthase natural inhibitor protein IF1, and the ATP/ADP carrier were observed. The ATP synthase-CyPD interactions have functional consequences on enzyme catalysis and are modulated by phosphate (increased CyPD binding and decreased enzyme activity) and cyclosporin (Cs) A (decreased CyPD binding and increased enzyme activity). Treatment of MgATP submitochondrial particles or intact mitochondria with CsA displaced CyPD from membranes and activated both hydrolysis and synthesis of ATP sustained by the enzyme. No effect of CsA was detected in CyPD-null mitochondria, which displayed a higher specific activity of the ATP synthase than wild-type mitochondria. Modulation by CyPD binding appears to be independent of IF1, whose association to ATP synthase was not affected by CsA treatment. These findings demonstrate that CyPD association to the lateral stalk of ATP synthase modulates the activity of the complex.
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
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Wittig, I., Braun, H.-P., & Schägger, H. (2006) · Nature Protocols · doi:10.1038/nprot.2006.62 · Cited by 1,708
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., & Schmid, F. X. (1989) · Nature · doi:10.1038/337476a0 · Cited by 1,407
Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D
Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808
Self-citationThe ATP synthase is involved in generating mitochondrial cristae morphology
Paumard, P., Vaillier, J., Coulary, B., Schaeffer, J., Soubannier, V., Mueller, D. M., Brèthes, D., di Rago, J.-P., & Velours, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.221 · Cited by 808
Effects of the new anti-lymphocytic peptide cyclosporin A in animals.
Borel, J. F., Feurer, C., Magnée, C., & Stähelin, H. (1977) · PubMed Central · Cited by 707
Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
Strauss, M., Hofhaus, G., Schröder, R. R., & Kühlbrandt, W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.35 · Cited by 676
The mitochondrial permeability transition from in vitro artifact to disease target
Bernardi, P., Krauskopf, A., Basso, E., Petronilli, V., Blalchy‐Dyson, E., Di Lisa, F., & Forte, M. A. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05213.x · Cited by 627
Self-citationWang, P., & Heitman, J. (2005) · Genome biology · doi:10.1186/gb-2005-6-7-226 · Cited by 617
Cited by
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition
Bonora, M., Bononi, A., De Marchi, E., Giorgi, C., Lebiedzinska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., et al. (2013) · Cell Cycle · doi:10.4161/cc.23599 · Cited by 458
Normalization of NAD + Redox Balance as a Therapy for Heart Failure
Lee, C. F., Chavez, J. D., Garcia-Menendez, L., Choi, Y., Roe, N. D., Chiao, Y. A., Edgar, J. S., Goo, Y. A., Goodlett, D. R., Bruce, J. E., et al. (2016) · Circulation · doi:10.1161/circulationaha.116.022495 · Cited by 336
Bonora, M., Wieckowski, M. R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., & Pinton, P. (2015) · Oncogene · doi:10.1038/onc.2014.96 · Cited by 330
Ong, S.-B., Samangouei, P., Kalkhoran, S. B., & Hausenloy, D. J. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.11.005 · Cited by 323
Metadata
- Authors
- Giorgio, V., Bisetto, E., Soriano, M. E., Dabbeni-Sala, F., Basso, E., Petronilli, V., Forte, M. A., Bernardi, P., & Lippe, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-12
- Volume
- 284
- Issue
- 49
- Pages
- 33982-33988
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2066200217
- Cited by
- 305
- References
- 40
- FWCI
- 3.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
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: Cyclophilin D Modulates Mitochondrial F0F1-ATP Synthase by Interacting with the Lateral Stalk of the Complex. https://app.cochat.ai/papers/10.1074/jbc.m109.020115
- The paper
- Giorgio, V., Bisetto, E., Soriano, M. E., Dabbeni-Sala, F., Basso, E., Petronilli, V., Forte, M. A., Bernardi, P., & Lippe, G. (2009). Cyclophilin D Modulates Mitochondrial F0F1-ATP Synthase by Interacting with the Lateral Stalk of the Complex. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m109.020115
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.
