The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Roles of the Mammalian Mitochondrial Fission and Fusion Mediators Fis1, Drp1, and Opa1 in Apoptosis
Open accessAbstract
During apoptosis, the mitochondrial network fragments. Using short hairpin RNAs for RNA interference, we manipulated the expression levels of the proteins hFis1, Drp1, and Opa1 that are involved in mitochondrial fission and fusion in mammalian cells, and we characterized their functions in mitochondrial morphology and apoptosis. Down-regulation of hFis1 powerfully inhibits cell death to an extent significantly greater than down-regulation of Drp1 and at a stage of apoptosis distinct from that induced by Drp1 inhibition. Cells depleted of Opa1 are extremely sensitive to exogenous apoptosis induction, and some die spontaneously by a process that requires hFis1 expression. Wild-type Opa1 may function normally as an antiapoptotic protein, keeping spontaneous apoptosis in check. However, if hFis1 is down-regulated, cells do not require Opa1 to prevent apoptosis, suggesting that Opa1 may be normally counteracting the proapoptotic action of hFis1. We also demonstrate in this study that mitochondrial fragmentation per se does not result in apoptosis. However, we provide further evidence that multiple components of the mitochondrial morphogenesis machinery can positively and negatively regulate apoptosis.
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
“A decrease in mitochondrial fusion caused by reduced levels of Opa1 can also influence the progression of cell-death pathways (Lee et al., 2004; Olichon et al., 2003).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Lee et al., 2004
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
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Movement of Bax from the Cytosol to Mitochondria during Apoptosis
Wolter, K. G., Hsu, Y., Smith, C. L., Nechushtan, A., Xi, X., & Youle, R. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.5.1281 · Cited by 1,809
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cellsPreprint
Paddison, P. J., Caudy, A. A., Bernstein, E., Hannon, G. J., & Conklin, D. S. (2002) · Genes & Development · doi:10.1101/gad.981002 · Cited by 1,571
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330
Desagher, S., Osen‐Sand, A., Nichols, A. C., Eskes, R., Montessuit, S., Lauper, S., Maundrell, K., Antonsson, B. E., & Martinou, J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.891 · Cited by 1,260
Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168
Cited by
Sorted by citations
Items 901–998 of 998
Etiology and pathogenesis of Parkinson’s disease: role of mitochondrial pathology
Brini, M., Ottolini, & Calí, T. (2013) · Research and Reports in Biochemistry · doi:10.2147/rrbc.s28413 · Cited by 3
UV Radiation-Induced Damage at Molecular Level
Mandi, S. S. (2016) · Springer eBooks · doi:10.1007/978-81-322-2767-0_3 · Cited by 3
Structural Organization and Dynamics of Mitochondria in the Cells in Vivo
Kuznetsov, A. V. (2007) · Wiley eBooks · doi:10.1002/9783527621095.ch5 · Cited by 3
Zick, M., & Reichert, A. S. (2011) · Wiley eBooks · doi:10.1002/9781118015759.ch6 · Cited by 3
Braga, P. C., Vitorino, R. M. P., Ferreira, R. M., Marques, M., Oliveira, P. F., Rodrigues, A. S., & Alves, M. G. (2025) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2025.112635 · Cited by 2
Charcot–Marie–Tooth type 2A variants of mitofusin 2 sensitize cells to apoptotic cell death
Joaquim, M., Bulimaga, M.-B., Mohn, M. A., Plouzennec, S., Osinski, L., Altin, S., Mahabir, E., Chevrollier, A., & Escobar‐Henriques, M. (2025) · Journal of Cell Science · doi:10.1242/jcs.263691 · Cited by 2
Regulation of mitochondrial biogenesis and energy metabolism in the heart
She, P., 莫非, Zhu, P., & Zhong, T. P. (2026) · Chinese Medical Journal · doi:10.1097/cm9.0000000000004011 · Cited by 2
Abd-El-Raouf, R., Harrison-Gleason, J., Kim, J., Wai, C. M., Yerlioglu, K. L., Ananías-Sáez, C., Ksiazek, A., Poomkudy, J. T., Araínga, M., Bose, D., et al. (2026) · JCI Insight · doi:10.1172/jci.insight.198810 · Cited by 2
Domingo, J. S., Lassueur, S., Galindo, A. N., Álvarez-Illera, P., Romero-Sanz, S., Caldero-Escudero, E., de la Fuente, S., Dayon, L., & Wiederkehr, A. (2023) · Journal of Cell Science · doi:10.1242/jcs.260049 · Cited by 3
Lin, Y., Zhao, W., Cai, J.-P., Shi, Q., & Lin, J. (2023) · International Journal of Pharmacology · doi:10.3923/ijp.2023.339.348 · Cited by 2
Häussler, S., Ghaffari, M. H., Seibt, K. D., Sadri, H., Alaedin, M., Huber, K., Frahm, J., Dänicke, S., & Sauerwein, H. (2023) · Journal of Dairy Science · doi:10.3168/jds.2023-23556 · Cited by 3
Live-cell imaging study of mitochondrial morphology in mammalian cells exposed to X-rays
Noguchi, M., Kanari, Y., Yokoya, A., Narita, A., & Fujii, K. (2015) · Radiation Protection Dosimetry · doi:10.1093/rpd/ncv157 · Cited by 2
Mitochondrial Biology in Parkinson's Disease
Lee, Y. (2009) · Interdisciplinary Bio Central · doi:10.4051/ibce.2009.2.0011 · Cited by 2
The Mitochondrial Pathway: Focus on Shape Changes
Campello, S., & Scorrano, L. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-381-7_6 · Cited by 2
Dying oligodendrocytes persist without mitochondriaPreprint
Bame, X., Gilani, S. Z., Kamen, Y., & Hill, R. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.19.699752 · Cited by 3
Mitochondrial Dysfunction and Cell Death: Mechanisms and Implications in Pathology
Lee, J. (2025) · Biochemistry · doi:10.5772/intechopen.1010111 · Cited by 1
Wei, C., Yuan, X., Liu, X., Feng, J., Song, M., Liu, X., Zhou, J., & Liu, J. (2025) · Interdisciplinary medicine · doi:10.1002/inmd.20240033 · Cited by 2
The interplay between circadian rhythm components and apoptosis in health and disease
Khezri, M. R., Panah, S. M., Ghasemnejad‐Berenji, M., Ghasemnejad‐Berenji, H., Mehrzadi, S., Fard, A. A., Rezabakhsh, A., & Rahnama, M. (2026) · Human Cell · doi:10.1007/s13577-026-01351-x · Cited by 1
Killingsworth, Z. K., Chaudhary, M., Mares, J. A., Ellery, H., Rowe, C. J., Stewart, I. J., Walker, P. F., & Burmeister, D. M. (2026) · Biomolecules · doi:10.3390/biom16020279 · Cited by 1
Mitochondrial dynamics and cancer: mechanisms and targeted therapy
Wang, A., Ye, X., Zhao, Y., & Zhang, C. (2026) · Cell Biology and Toxicology · doi:10.1007/s10565-026-10174-3 · Cited by 1
Programmed Cardiomyocyte Death in Heart Disease
Dorn, G. W., & Kitsis, R. N. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381510-1.00031-4 · Cited by 1
Role of the Mitochondrial Fission Protein Drp1 in Synaptic Damage and Neurodegeneration
Nakamura, T., Cho, D., & Lipton, S. A. (2011) · Springer eBooks · doi:10.1007/978-94-007-1291-1_8 · Cited by 1
Studi, D., Milano-Bicocca, D., Gaglio, D., & Chiaradonna, F. (2009) · Cited by 1
Mitophagy in sarcopenic muscle and practical recommendations for exercise training
Sanchez, A. M. J., & Solsona, R. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822146-4.00011-9 · Cited by 2
Mitochondrial decline and chronic conditions of older adults
Marzetti, E., Landi, F., Martini, F., Leeuwenburgh, C., & Calvani, R. (2017) · Oxford University Press eBooks · doi:10.1093/med/9780198701590.003.0046 · Cited by 1
Differentiating Compromised Mitochondria of Lung Cancer Cells from Mitochondria in Healthy Cells
Sharma, B., Shafaee, Z., Twelker, K., Bhatia, N. D., Agriantonis, G., Dave, J., Mestre, J., Ghanta, H., Arora, S., & Whittington, J. (2024) · Journal of Biomedical Research & Environmental Sciences · doi:10.37871/jbres1900 · Cited by 1
Castillo‐Galán, S., Grünenwald, F., Hidalgo, Y., Cárdenas, C., Cádiz, M. I., Alcayaga‐Miranda, F., Khoury, M., & Cuenca, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104686 · Cited by 1
Mitochondrial Control of Apoptosis and Cancer
Dakubo, G. D. (2010) · Springer eBooks · doi:10.1007/978-3-642-11416-8_3 · Cited by 1
Lou, D., & Guan, Z. (2021) · Springer eBooks · doi:10.1007/978-981-16-1498-9_17 · Cited by 1
Bax, Bak and Bid: Key Mediators of Apoptosis
Dempsey, C. E., Roberts, D. L., & Dive, C. (2006) · doi:10.1002/9783527619665.ch12 · Cited by 1
CDK5 and Mitochondrial Cell Death Pathways
Meuer, K., Bähr, M., & Weishaupt, J. H. (2008) · Springer eBooks · doi:10.1007/978-0-387-78887-6_7 · Cited by 1
Brow, S. (2015) · Open Access Victoria University of Wellington | Te Herenga Waka (Figshare) · doi:10.26686/wgtn.17013455 · Cited by 1
Functional analysis of mammalian m-AAA proteases
Ehses, S. (2008) · Kölner Universitäts PublikationsServer (Universität zu Köln) · Cited by 1
Cell death: initiation, propagation and clearance
Krysko, D. V. (2006) · Ghent University Academic Bibliography (Ghent University) · Cited by 1
E3 ubiquitin ligase MARCHF5 controls BAK apoptotic activity independently of BH3-only proteinsPreprint
Huang, A. S., Chin, H. S., Reljić, B., Djajawi, T. M., Tan, I. K. L., Stroud, D. A., Huang, D. C. S., van Delft, M. F., & Dewson, G. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.04.474880 · Cited by 1
Ma, H., Hou, T., Wu, J., Zhao, J., Cao, H., Masula, M., & Wang, J. (2023) · Research Square · doi:10.21203/rs.3.rs-3129123/v1 · Cited by 1
ROCK1 activates mitochondrial fission leading to oxidative stress and muscle atrophyPreprint
Si, M., Yu, R., Lin, H., Li, F., Jung, S. Y., Thomas, S. S., Danesh, F. S., Wang, Y., Peng, H., & Hu, Z. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.22.563469 · Cited by 1
O’Reilly, C. L., Davidyan, A., Cizio, K., Doidge, S. M., Bubak, M. P., Borowik, A., Lewis, T. L., & Miller, B. F. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.10.627796 · Cited by 1
Regulation des mitochondrialen Zerfalls innerhalb der neuronalen Apoptose
Meuer, K. (2007) · doi:10.53846/goediss-206 · Cited by 1
Neumann, D. (2010) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-383
Division of the single mitochondrion in "Trypanosoma brucei" and its impact on the cell cycle
Chanez, A. (2006) · reroDoc Digital Library
Dinámica mitocondrial y sus implicaciones en la desregulación metabólica y en la neurodegeneración
Antonio Zorzano, A., Segalés, J., Hernández‐Álvarez, M. I., & Sorianello, E. M. (2012) · Monografías de la Real Academia Nacional de Farmacia
CHARACTERIZATION OF MITOCHONDRIAL MEMBRANE PROTEINS AS NOVEL COMPONENTS IN MITOCHONDRIAL DYNAMICS
Liu, T. (2014) · Figshare
Characterization of SLP-2 function in T lymphocytes
Christie, D. A. (2012) · Scholarship@Western (Western University)
Mitochondrial form and function in pancreatic β-cells and brown adipocytes
Wikström, J. D. (2010) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Mitochondria in the Aging Heart
Marı́n-Garcı́a, J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4599-9_13
Schwann cells and mesenchymal stem cells as promoter of peripheral nerve regeneration
Mantovani, M. C. (2011) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Mechanism of action of autosomal recessive juvenile parkinsonism gene mutations
Sandebring, A. (2010) · Figshare
Rothenberg, K. G., Siedlak, S. L., Lee, H., Zhu, X., Perry, G. L., & Smith, M. A. (2011) · Future Neurology · doi:10.2217/fnl.10.81
Kong, B. (2015) · uO Research (University of Ottawa) · doi:10.20381/ruor-6589
Stagge, F. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4871
Functional characterization of prohibitins by conditional inactivation in the mouse
Merkwirth, C. (2008) · Kölner Universitäts PublikationsServer (Universität zu Köln)
High-throughput siRNA Screen Identifies MTX2 as a Novel Mediator of Mitochondrial Morphology
Gaetz, M. (2014) · uO Research (University of Ottawa) · doi:10.20381/ruor-4048
Mitochondrial Structure, Composition, and Dynamics
Marín-García, J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4599-9_3 · Cited by 1
Action of resveratrol analogs and hyperthermia in cancer chemoprevention and chemotherapyY
Butler, R. (2011) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t34t6j1z
Genetic and Chemical Genetic Analysis of the Cell Cycle
Yu, L. X. (2009) · TSpace (University of Toronto)
Raschke, I. (2009) · Kölner Universitäts PublikationsServer (Universität zu Köln)
Guillet, V., & REYNIER, P. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique)
Mitochondrial involvement in neuronal cell death
Gray, J. J. (2014) · Digital Commons - DU (University of Denver)
Functional and Morphological Impact of ER Stress on
Renard, P., Raes, M. J., & Arnould, T. (2013)
Wang, P. T. C. (2015) · cIRcle (University of British Columbia) · doi:10.14288/1.0166455
Lecome-backde la mitochondrie dans l’apoptose chez la drosophile
Clavier, A., Rincheval‐Arnold, A., Mignotte, B., & Guénal, I. (2016) · médecine/sciences · doi:10.1051/medsci/20163205014
Mitochondrial Dynamics and Its Implications in Metabolic Dysregulation and Neurodegeneration
Antonio Zorzano, A., Segalés, J., Hernández‐Álvarez, M. I., & Sorianello, E. M. (2012) · Oxidative stress and disease · doi:10.1201/b12308-21
The Emerging Role of Mitochondrial Dynamics in Cardiovascular Disease
Marín-García, J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404599-6.00015-9
Programmed Cell Death and Its Role in Neurological Disease
Bredesen, D. E., Rao, R. V., & Mehlen, P. (2007) · Elsevier eBooks · doi:10.1016/b978-012369509-3.50010-x
Role of Autophagy in Cancer Therapy
Gargini, R., & Izquierdo, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801033-4.00005-9
Mitofusin 1 and Mitofusin 2 Function in the Context of Brain Development
Hamze, C. (2011) · Library and Archives Canada (Government of Canada) · doi:10.20381/ruor-4991
Nahirny, A. (2011) · TSpace (University of Toronto)
Peroxins: A Proliferation Romance amongst Supposition and Disposition
Brocard, C., & Hartig, A. (2007)
Wilkins, J. M. (2013) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/44044
Peñagarikano, O. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aal3703
Insights Into Mitochondrial Genetic and Morphologic Dynamics Gained by Stochastic Simulation
Rajasimha, H. K. (2007)
Defective Dynamics Of Mitochondria In Amyotrophic Lateral Sclerosis And Huntington's Disease
Song, W. (2012) · Journal of International Crisis and Risk Communication Research
Identifying novel genes involved in amino acid sensing
Dayhoff-Brannigan, M. (2014)
Mitochondrial Remodeling During Hyperosmotic Stress
Zulys, M. (2009) · TSpace (University of Toronto)
Zhang, Y., Tryon, L. D., & Hood, D. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802936-7.00007-6
Potential application of alternative oxidase (AOX) in neurodegenerative diseases
Zhuang, Y. (2018) · Työväentutkimus Vuosikirja
Kanazashi, Y., Takara, N., Iwami, K., Ohta, Y., & Umeda, N. (2018) · Japanese Journal of Applied Physics · doi:10.7567/jjap.57.046601
Close, A.-F. (2017) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r33f4m242
A Critical Therapeutic Target to Inhibit Apoptosis in Relevant Heart Failure: An Overview
Nepala, A., Yasmeenb, S., Akhtarc, F., Kojua, N., Aina, Q. U., Teng-Li, C., Xiu-Xiua, Z., Qinga, L., & Ding-Dinga, C. (2018) · American Journal of Advanced Drug Delivery · doi:10.21767/2321-547x.1000027
Clegg, H. V. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/dcpq-a148
Disease Modelling and Precision Medicine Using Canadian Cardiomyocytes
Liang, W., Alqarawi, W., & Davis, D. R. (2019) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2019.10.036
Miyamoto, T., Uosaki, H., Mizunoe, Y., Goto, S., Yamanaka, D., Masuda, M., Yoneyama, Y., Nakamura, H., Hattori, N., Takeuchi, Y., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.22.166165
Letter to the Editor - New Pharmacotherapy for Heart Failure with Reduced Ejection Fraction
Ioannou, A., Metaxa, S., Simon, S., Mandal, A. K. J., & Missouris, C. G. (2020) · Expert Review of Cardiovascular Therapy · doi:10.1080/14779072.2020.1799562
Stephan, T. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8278
A Review on the Mechanisms of Mitochondrial Dynamics and the Relationship with Neurodegeneration
Zhu, Y. (2020) · International Symposium on Artificial Intelligence for Medicine Sciences (ISAIMS) · doi:10.1145/3429889.3429941
Mitochondrien als Kraftwerk der β-Zelle
Baltrusch, S., Reinhardt, F., & Tiedge, M. (2015) · Der Diabetologe · doi:10.1007/s11428-014-1278-5
Mitra, K. (2009) · Wiley eBooks · doi:10.1002/9780470747919.ch9
Surana, U., & Koh, C.-G. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733748588.793552560
Metadata
- Authors
- Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Venue
- Molecular Biology of the Cell
- Published
- 2004-11
- Volume
- 15
- Issue
- 11
- Pages
- 5001-5011
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC524759
- OpenAlex
- W1970248089
- Cited by
- 1,042
- References
- 49
- Citations by year
- 2026: 15 · 2025: 20 · 2024: 41 · 2023: 39 · 2022: 43 · 2021: 50 · 2020: 52 · 2019: 36 · 2018: 54 · 2017: 40 · 2016: 72 · 2015: 55 · 2014: 47 · 2013: 50 · 2012: 74
- FWCI
- 14.83
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- AJOU Open Repository (Ajou University) (submittedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute
- National Institute of Neurological Disorders and Stroke
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- apoptosis, mitochondrial fission, mitochondrial fusion, Fis1, Drp1, OPA1, mitochondrial morphology, mitochondrial fragmentation, anti-apoptotic proteins, spontaneous apoptosis, mitochondrial morphogenesis
- MeSH terms
- HeLa Cells, Humans, Immunohistochemistry, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Poly(ADP-ribose) Polymerases, RNA, Subcellular Fractions, Time Factors, Immunoblotting, Down-Regulation, Apoptosis, Microscopy, Confocal, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins, RNA Interference
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