The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells
Open accessAbstract
Recognition of injured mitochondria for degradation by macroautophagy is essential for cellular health, but the mechanisms remain poorly understood. Cardiolipin is an inner mitochondrial membrane phospholipid. We found that rotenone, staurosporine, 6-hydroxydopamine and other pro-mitophagy stimuli caused externalization of cardiolipin to the mitochondrial surface in primary cortical neurons and SH-SY5Y cells. RNAi knockdown of cardiolipin synthase or of phospholipid scramblase-3, which transports cardiolipin to the outer mitochondrial membrane, decreased the delivery of mitochondria to autophagosomes. Furthermore, we found that the autophagy protein microtubule-associated-protein-1 light chain 3 (LC3), which mediates both autophagosome formation and cargo recognition, contains cardiolipin-binding sites important for the engulfment of mitochondria by the autophagic system. Mutation of LC3 residues predicted as cardiolipin-interaction sites by computational modelling inhibited its participation in mitophagy. These data indicate that redistribution of cardiolipin serves as an 'eat-me' signal for the elimination of damaged mitochondria from neuronal cells.
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?
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“changes in LC3-II amounts are tissue- and cell context-dependent.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). (2016) · cites this paper as [145]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“In the absence of lysosomal protease inhibitors, starvation results in a modest increase (HEK 293 cells) or even a decrease (HeLa cells) in the amount of LC3-II. The use of inhibitors reveals that this apparent decrease is due to lysosome-dependent degradation.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). (2016) · cites this paper as [145]
Experimental — accuracy not yet measuredIn the citing paper
“Cardiolipin — a phospholipid that is normally segregated to the inner mitochondrial membrane and is essential to the maintenance of mitochondrial architecture and function — when herniated outside a damaged mitochondrial membrane, stimulates mitophagy, a process that eliminates dysfunctional mitochondria and promotes the formation of new mitochondria (79).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [79]
In the citing paper
“It should also be mentioned that the translocation of cardiolipin from the inner to outer mitochondrial membrane is another event that can trigger mitophagy [144].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [144]
In the citing paper
“LC3 proteins are involved in autophagosome formation, with participation of GABARAP subfamily members in later stages of autophagosome formation [201].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [201]
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
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Trott, O., & Olson, A. J. (2010) · Journal of Computational Chemistry · doi:10.1002/jcc.21334 · Cited by 38,412
Molecular dynamics with coupling to an external bath
Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 31,057
A smooth particle mesh Ewald method
Essmann, U., Perera, L., Berkowitz, M., Darden, T., Lee, H.-C., & Pedersen, L. (1995) · The Journal of Chemical Physics · doi:10.1063/1.470117 · Cited by 21,378
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
WebLogo: A Sequence Logo Generator: Figure 1Preprint
Crooks, G. E., Hon, G. C., Chandonia, J., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,418
The MARTINI Force Field: Coarse Grained Model for Biomolecular Simulations
Marrink, . J., Risselada, H. J., Yefimov, S., Tieleman, D. P., & de Vries, A. H. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp071097f · Cited by 5,641
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003
Boeckmann, B. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg095 · Cited by 3,911
Evans, D. J., & Holian, B. L. (1985) · The Journal of Chemical Physics · doi:10.1063/1.449071 · Cited by 3,644
Flagged first, then by citations
Cited by
Sorted by citations
Items 901–999 of 999
Mitochondrial dysfunction–ferroptosis crosstalk drives renal fibrosis in chronic kidney disease
Zeng, L., Zhu, L., Xu, H., Li, Y., & Hu, K. (2026) · Renal Failure · doi:10.1080/0886022x.2026.2659414 · Cited by 2
The ubiquitin‐proteasome system and autophagy as guardians of the cellular proteome
Đikić, I. (2026) · FEBS Letters · doi:10.1002/1873-3468.70371 · Cited by 4
Chowdhury, R. M. (2022) · National Journal of Maxillofacial Surgery · doi:10.4103/njms.njms_123_20
The dual role of mitophagy in cancer and its targeting for effective anticancer therapy
Mishra, S. R., Mishra, P., Dhiman, R., & Bhutia, S. K. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00002-8 · Cited by 2
Phosphorylation Events in Selective Mitophagy: Possible Biochemical Markers?
Zhang, W., Wu, H., Liu, L., Zhu, Y., & Chen, Q. (2013) · Current Pathobiology Reports · doi:10.1007/s40139-013-0033-8 · Cited by 2
Wu, M., Chen, L., Chen, L., & Wang, Y. (2021) · PubMed Central · doi:10.11817/j.issn.1672-7347.2021.200583 · Cited by 2
Mitochondrial biogenesis and mitophagy
Tan, S., Kennedy, B. K., & Wong, E. S. P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821562-3.00037-x · Cited by 2
Pharmacological agents affecting mitophagy and inflammation
Borisov, E. E., Bezsonov, E. E., Lyukmanov, D., Poggio, P., Moschetta, D., & Valerio, V. (2022) · Vessel Plus · doi:10.20517/2574-1209.2022.20 · Cited by 3
Autophagy and Huntington's disease
Croce, K. R., Jasutkar, H. G., & Yamamoto, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95672-7.00018-2 · Cited by 2
Werner, A. (2018) · doi:10.53846/goediss-6798 · Cited by 1
Sagar, S., Faizan, M. I., Chaudhary, N., Gheware, A., Sharma, K., Azmi, I., Singh, V. P., Kharya, G., Mabalirajan, U., Agrawal, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.27.470183 · Cited by 2
Mitochondrial Function and Dysfunction in White Adipocytes and Therapeutic Implications
Wang, F., Huynh, P. M., & An, Y. (2024) · Comprehensive physiology · doi:10.1002/cphy.c230009 · Cited by 10
Imbalanced mitochondrial dynamics in human and mouse PD brainsPreprint
Brown, H. J., Fan, R. Z., Bell, R., Salehe, S. S., Gil, C. M., Lai, Y., & Tieu, K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.27.635175 · Cited by 2
Ma, W., Ma, J., Zhang, K., Zheng, X., Wang, P., Feng, L., Ming, S., Zhuang, X., Zhou, J., Gao, C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.29.656919 · Cited by 2
Asiago, J. M., Doyle, T. B., Mishra, V. R., Jacquet, A. D. R., & Rochet, J. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622888-00325 · Cited by 1
Beebe, S. J. (2021) · Series in bioengineering · doi:10.1007/978-981-10-5113-5_8 · Cited by 1
Tateishi, H., Chinen, T., Fukuda, R., Radwan, M. O., Shimagaki, K., Koga, R., Masuda, T., Okamoto, Y., Sakamoto, A., Misumi, S., et al. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14401 · Cited by 1
Mitophagy: an emerging therapeutic target in mitochondrial diseases
Pinho, B. R., Duchen, M. R., & Oliveira, J. M. A. (2026) · Biochemical Journal · doi:10.1042/bcj20260161 · Cited by 1
Egress-enhancing mutation reveals the inefficiency of non-enveloped virus cell exit
Rodriguez-Irizarry, V. J., Maples, R. W., & Pfeiffer, J. K. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003245 · Cited by 1
Martins, W. K., Tsubone, T. M., Sanches, C. E. N., Rocha, C. D. S., Navarro, R. S., Stolf, B. S., Diniz, S. N., Itri, R., & Baptista, M. S. (2025) · Cell Biology International · doi:10.1002/cbin.70073 · Cited by 1
Li, G., Li, T., Deng, Y., Deng, X., Chen, C., Yu, B., & Zhang, K. (2025) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2025.08.002 · Cited by 1
The B-lymphoblastoid model in Barth syndrome
Chan, J. Z., Tomczewski, M. V., Berdeklis, A. N., & Duncan, R. E. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2025.159691 · Cited by 1
Zou, J., Jian, J., Ge, D., Zhou, B., & Zhang, J. (2025) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70586 · Cited by 1
Zhao, J., Wang, Q., Cao, Y., Shan, H., & Xu, S. (2025) · Hereditas · doi:10.1186/s41065-025-00544-y · Cited by 1
Bringer, M.-A., Manceau, S., Azzaz, J. A., Buteau, B., Proukhnitzky, L., Aumeunier, A., Bermúdez‐Humarán, L. G., Chain, F., Daniel, C., Jacquin, É., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-025-02616-y · Cited by 1
Yang, J. F., Zou, Y., & Zhao, X. (2026) · Reviews in the Neurosciences · doi:10.1515/revneuro-2025-0115 · Cited by 1
Lipid alterations in hereditary peripheral neuropathies: common mechanisms in disease heterogeneity?
Kuipers, K., Vanherle, S., Poelmans, K., Wolfs, E., Bogie, J. F. J., & Vangansewinkel, T. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00932-6 · Cited by 1
The role of selective autophagy in cardiovascular diseases: mechanisms and therapeutic potential
Zeng, T., Zhang, Z., Qian, C., Li, X., & Li, S. (2026) · The Journal of Cardiovascular Aging · doi:10.20517/jca.2025.46 · Cited by 1
Wang, X., Lin, B., Xu, X., Bao, Z., Ren, R., Lin, P., Luo, G., Yu, Y., & Liang, Y. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07964-y · Cited by 1
HADHA in cardiovascular disease: From mitochondrial dysfunction to therapeutic targets
Qi, Y., Guo, S., Cai, X., Liu, C., Dong, Y., Chen, X., Chen, Y., & Zhu, W. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103106 · Cited by 1
Yang, H., Zhang, C., Pan, J., Xing, J., Bin, S., Han, F., Wang, M., Shui, G., & Yang, W. (2026) · New Phytologist · doi:10.1111/nph.71139 · Cited by 1
Liu, J., Li, F., Zeng, Q., Hu, W., Yang, L., Luo, S., Lv, F., Li, D., & Deng, Y. (2026) · Drug Design Development and Therapy · doi:10.2147/dddt.s610273 · Cited by 1
Ikegami, A., Watanabe‐Takahashi, M., Shimasaki, K., Okuda, Y., Choda, M., Waku, T., Maru, Y., Deguchi, A., Nishino, Y., Miyazawa, A., et al. (2026) · The FASEB Journal · doi:10.1096/fj.202504723r · Cited by 1
Lipid Codes and Lipid‐Binding Proteins as Central Regulators of Autophagy
Kumar, A., & Ghosh, D. K. (2026) · BioFactors · doi:10.1002/biof.70124 · Cited by 1
Zhan, Z., Liu, X., Li, Z. H., Qiao, X., Li, S., Gong, Y., Yang, L., Gao, Y., Xia, X., Bai, K., et al. (2026) · Science Advances · doi:10.1126/sciadv.aef1896 · Cited by 1
Extracellular Mitochondria Mediate Endothelial Injury After Traumatic Brain Injury
Tang, L., Liu, Y., Pang, K., Li, Y., Zhang, Y., Lu, X., Zhang, X., Zhao, P., Zhou, Z., Zhang, H., et al. (2026) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.126.323502 · Cited by 1
Nirala, N., Kuwar, O. K., Rana, D., & Dhingra, M. S. (2026) · Acta Diabetologica · doi:10.1007/s00592-026-02749-7 · Cited by 1
Mitochondrial Damage and Mitophagy in Ischemia/Reperfusion-Induced Liver Injury
Go, K. L., Lee, S., Behrns, K. E., & Js, K. (2017) · Springer eBooks · doi:10.1007/978-3-319-58106-4_9 · Cited by 1
Lautrup, S., Anisimov, A. S., Lagartos-Donate, M. J., & Fang, E. F. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91617-2.00010-9 · Cited by 2
Santos, R. S., Franco, M. S. F., Ravagnani, F. G., Chaves‐Filho, A. B., Miyamoto, S., Baptista, M. S., Shchepinov, M. S., & Yoshinaga, M. Y. (2023) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2023.100005 · Cited by 1
Recent advances in organelle-specific autophagy in melanoma
Qi, J., Zhang, Q., Wang, L. Y., Wen, X., He, G., & Jiang, X. L. (2024) · ONCOLOGIE · doi:10.1515/oncologie-2024-0228 · Cited by 1
Role of Mitochondria in the Regulation of Kidney Function and Metabolism in Type 2 Diabetes
Han, X., Shi, Y., Diamond-Stanic, M. K., & Sharma, K. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811752-1.00012-2 · Cited by 1
Mitochondria as Signaling Platforms
Yoboue, E. D., Manon, S., & Camougrand, N. M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811752-1.00002-x · Cited by 1
Bagshaw, O. R. M., Atkinson, J., Fajardo, V. A., LeBlanc, P. J., & Stuart, J. A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819621-2.00020-6 · Cited by 1
Examining Autophagy and Mitophagy as Inducible Mechanisms of Cellular Remodelling
Bloemberg, D. (2017) · UWSpace (University of Waterloo) · Cited by 1
Huntingtin aggregation at interfaces associated with membranes and organelles
Adegbuyiro, A. (2021) · doi:10.33915/etd.8315 · Cited by 1
Roy, M., Nandy, S., Marchesan, E., Banerjee, C., Mondal, R., Caicci, F., Ziviani, E., & Chakraborty, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.10.561633 · Cited by 1
Vykoukal, J., Chen, Y., Hong, M. J., Zuo, M., Krishna, H., Katayama, H., Irajizad, E., Wu, R., Léon-Letelier, R. A., Dennison, J. B., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.04.587899 · Cited by 1
Interaction Between Mitochondria and Autophagy
Gegg, M. E. (2015) · Current topics in neurotoxicity · doi:10.1007/978-3-319-13939-5_3
Reynolds, C. A. (2015) · Human Biology
A Get‐Together to Tear It Apart
McLelland, G., & Fon, E. A. (2015) · Wiley eBooks · doi:10.1002/9781119017127.ch12
Functional characterization of murine 1-acylglycerol-3-phosphate O-acyltransferase 4 (AGPAT4)
Bradley, R. (2015) · UWSpace (University of Waterloo)
Computational Studies of Lipid Oxidation and Signaling
Mohammadyani, D. (2016) · D-Scholarship@Pitt (University of Pittsburgh)
Self-citationLipid Phosphate Phosphatases (LPPs) And Its Role In Mitochondrial Function
Miriyala, S. (2016) · MOJ Anatomy & Physiology · doi:10.15406/mojap.2016.02.00033
Grevengoed, T. J. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/g7gj-eb34
Mechanisms of communication from mitochondria to lysosomes
Fernández-Mosquera, L. (2017) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6214
Tan, S. (2017) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/72655
Humphries, K. M. (2017) · The Atrium (University of Guelph)
Bradley, R. M. (2018) · UWSpace (University of Waterloo)
A Study on Molecular Mechanism of Novel Mitophagy Regulators
박성우 (2015) · Seoul National University Open Repository (Seoul National University)
Mechanisms and Roles of Mitophagy
Vigié, P., Bhatia‐Kiššová, I., & Camougrand, N. M. (2017) · Wiley eBooks · doi:10.1002/9780470015902.a0027587
Molecular Mechanisms Underlying the Role of Mitophagy in Neurodegeneration
Ahlawat, A., Kaira, M., Walia, V., & Garg, M. (2020) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-7998-1317-0.ch003
Serramito-Gómez, I. (2019) · Gredos (University of Salamanca) · doi:10.14201/gredos.143539
Structural and Post-Transcriptional Regulation of Autophagy in Saccharomyces cerevisiae
Gatica, D. (2019) · Deep Blue (University of Michigan)
Characterization of Mitochondrial Calcium Uniporter in Barth Syndrome Models
Hartmann, M. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8100
The mitochondrial network in Parkinson's disease
Aufschnaiter, A., Kohler, V., & Büttner, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815950-7.00008-4
Praharaj, P. P., Behera, B. P., Mishra, S. R., Patra, S., Mahapatra, K. K., Panigrahi, D. P., Bhol, C. S., & Bhutia, S. K. (2020) · Springer eBooks · doi:10.1007/978-981-15-6930-2_7
Regulation of intracellular traffic by TBK1 and its relevance to ALS
Villarroel‐Campos, D. (2020) · UCL Discovery (University College London)
Лямзаев, К. Г., Кнорре, Д. А., & Черняк, Б. В. (2020) · Biochemistry (Moscow) · doi:10.31857/s0320972520120027
Mitochondrial response to axonal injury
Kedra, J. (2020) · TUScholarShare (Temple University)
Mitochondrial-localized Phosphatidylethanolamine in Mitochondrial Dynamics and Autophagy
Chan, E. Y. L. (2014) · TSpace (University of Toronto)
Walczak, M., Meister, T. R., Zhu, Y., & Yeh, E. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.24.445495
Mitochondria-associated membranes in the maintenance of cell homeostasis
Camougrand, N. M., & Manon, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821562-3.00043-5
Ge, Y., Boopathy, S., Nguyen, T. H., Lugo, C. M., & Chao, L. H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.01.458556
Prospective Advances in Exercise-Induced Autophagy on Health
Liang, J., Kirberger, M., & Chen, N. (2021) · Springer eBooks · doi:10.1007/978-981-16-4525-9_11
Mitochondrial Dysfunction and Mitophagy: Physiological Implications in Cardiovascular Health
Gustafsson, Å. B. (2021) · Advances in biochemistry in health and disease · doi:10.1007/978-3-030-78799-8_11
Characterization and identification of novel regulators of the synthesis of phospholipids
Ye, C. (2014) · Human Biology
Huang, Y., Feng, Y., Zhang, Q., Li, L., Zhang, J., Huang, Y., Lv, Y., Jia, J., Zhang, D., Luo, G., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-1014224/v1
The Role of Autophagy and Mitophagy in Huntington’s Disease
Eswaran, A., Lim, C. S. Y., Chye, S. M., Ling, A. P. K., & Koh, R. Y. (2021) · ASM Science Journal · doi:10.32802/asmscj.2021.911
Role of mitophagy in muscle growth and metabolism
Peker, N. (2017) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/72691
Chu, C. T. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809324-5.03651-8
Self-citationDiehl, J. A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.725967101.793538077
Mitochondria-Associated Inflammasome Activation and Its Impact on Aging and Age-Related Diseases
Kauppinen, A. (2019) · Springer eBooks · doi:10.1007/978-3-319-99375-1_107
Michaelis, J. B. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.69732
Nodweddu effaith signalu ghrelin-GHS-R ar awtoffagi niwronaidd
Roberts, L. D. (2022) · Cronfa (Swansea University) · doi:10.23889/suthesis.62285
Prognostic value of plasma interleukin 6 levels in severe traumatic brain injury
Jamsheed, A., Sidiq, S., Lone, A. Q., & Amin, Z. (2023) · Asian Journal of Medical Sciences · doi:10.3126/ajms.v14i8.52505
Lipids in membrane formation for autophagosomes and autophagy induction
Praharaj, P. P., & Bhutia, S. K. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-90142-0.00010-4
ATG8 family protein, cargo selection, and autophagy
Mishra, A., & Dhiman, R. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-90142-0.00006-2
Matamoros, A., Muñoz, M., Quiñones, M. M., Gonzalez-Ibañez, A. M., Gómez-Lillo, G., Malleda, A., Escalona, E., Castro, A. F., Ruíz, L. M., & Elorza, Á. A. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4862202
Synthetic activators of autophagy
Guseva, E. A., Pavlova, J. A., Dontsova, O. А., & Владимирович, С. П. (2024) · Biochemistry (Moscow) · doi:10.31857/10.31857/s0320972524010027
Causes and Consequences of Perturbations of the Mitochondrial Genome
King, D. E., Copeland, W. C., Wallace, K. B., & Meyer, J. N. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00128-5
Cardioprotection through mitophagy
Miyamoto, S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00009-0
Kassir, M. F., & Öğretmen, B. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00005-3
Ktistakis, N. T. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00001-6
Metadata
- Authors
- Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., Qiang Wang, K. Z., Zhu, J., Klein-Seetharaman, J., Balasubramanian, K., Amoscato, A. A., Borisenko, G., Huang, Z., Gusdon, A. M., Cheikhi, A., Steer, E. K., Wang, R., Baty, C., Watkins, S., Bahar, I., Bayır, H., & Kagan, V. E.
- Affiliations
- University of Pittsburgh (US)
- Corresponding author
- Chu, Charleen T.
- Tyurina, Yulia Y.
- Bayır, Hülya
- Kagan, Valerian E.
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2013-09-15
- Volume
- 15
- Issue
- 10
- Pages
- 1197-1205
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC3806088
- OpenAlex
- W2135592618
- Cited by
- 1,083
- References
- 66
- Citations by year
- 2026: 75 · 2025: 96 · 2024: 102 · 2023: 87 · 2022: 83 · 2021: 105 · 2020: 104 · 2019: 82 · 2018: 73 · 2017: 85 · 2016: 60 · 2015: 65 · 2014: 59 · 2013: 6
- FWCI
- 46.15
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (U19AIO68021)
- National Institute on Aging (AG026389, F32AG030821, R01AG026389)
- National Heart, Lung, and Blood Institute (HL-70755, R01HL070755, R01HL094488)
- National Institute of General Medical Sciences (P20GM103554, P41GM103712)
- National Institute of Allergy and Infectious Diseases (U19AI068021)
- National Institute of Neurological Disorders and Stroke (NS065789, NS076511, R01NS061817, R01NS065789, NS061817, R56NS065789, R37NS061817, R01NS076511)
- National Institute of Environmental Health Sciences (R21ES021068, ES 020693, R01ES020693)
- National Institute for Occupational Safety and Health (R01 OH008282, OH008282)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R21HD057587)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- cardiolipin, mitophagy, mitochondrial outer membrane, LC3, cardiolipin synthase, autophagy, neurons, mitochondrial damage, autophagosome formation, rotenone, staurosporine, 6-hydroxydopamine
- MeSH terms
- Amino Acid Sequence, Animals, Autophagy, Biological Transport, Cardiolipins, Cells, Cultured, HeLa Cells, Humans, Mitochondria, Models, Molecular, Molecular Sequence Data, Neurons, Rotenone, Uncoupling Agents, Signal Transduction, Oxidopamine, Rats, Sprague-Dawley, Protein Structure, Tertiary, Cell Line, Tumor, Mitochondrial Membranes, Rats, Gene Knockdown Techniques, Mitophagy
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
