The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
A mitochondrial specific stress response in mammalian cells
Open accessAbstract
Cells respond to a wide variety of stresses through the transcriptional activation of genes that harbour stress elements within their promoters. While many of these elements are shared by genes encoding proteins representative of all subcellular compartments, cells can also respond to stresses that are specific to individual organelles, such as the endoplasmic reticulum un folded protein response. Here we report on the discovery and characterization of a mitochondrial stress response in mammalian cells. We find that the accumulation of unfolded protein within the mitochondrial matrix results in the transcriptional upregulation of nuclear genes encoding mitochondrial stress proteins such as chaperonin 60, chaperonin 10, mtDnaJ and ClpP, but not those encoding stress proteins of the endoplasmic reticulum. Analysis of the chaperonin 60/10 bidirectional promoter identified a CHOP element as the mitochondrial stress response element. Dominant-negative mutant forms of CHOP and overexpression of CHOP revealed that this transcription factor, in association with C/EBPbeta, regulates expression of mitochondrial stress genes in response to the accumulation of unfolded proteins.
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
“Under stress conditions, when the degradation pathways are insufficient to repair the consequences of the alteration in mitochondrial translation [52] or the accumulation of oxidatively damaged or misfolded proteins, a retrograde signal is activated which coordinates nuclear gene expression. This mitochondria-to- nucleus response is named mitochondrial unfolding protein response (UPRmt) [53].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [53]
In the citing paper
“Under stress conditions, UPRmt occurs in an attempt to maintain mitochondrial proteostasis by upregulating the expression of mitochondrial chaperones and m-AAA proteases (e.g., chaperonin 10, chaperonin 60, and CLPP) (69).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [69]
In the citing paper
“a known protein degraded by LONP1 and an established model for studying mitochondrial proteostasis imbalance38–40”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [38]
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
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., & Pease, L. R. (1989) · Gene · doi:10.1016/0378-1119(89)90358-2 · Cited by 7,414
Efficient selection for high-expression transfectants with a novel eukaryotic vector
Niwa, H., Yamamura, K., & Miyazaki, J. (1991) · Gene · doi:10.1016/0378-1119(91)90434-d · Cited by 5,149
Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,131
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
Molecular chaperones in cellular protein folding
Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,584
Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,344
IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
Calfon, M. A., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., Clark, S. G., & Ron, D. (2002) · Nature · doi:10.1038/415092a · Cited by 2,907
Andrews, N. C., & Faller, D. V. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.9.2499 · Cited by 2,337
Flagged first, then by citations
Cited by
Sorted by citations
Items 701–800 of 999
Single-cell RNA sequencing analysis of T helper cell differentiation and heterogeneity
Jaroušek, R., Mikulová, A., Daďová, P., Tauš, P., Kurucová, T., Plevová, K., Tichý, B., & Kubala, L. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119321 · Cited by 12
Huang, L., Dong, H., Chuang, I., Liu, M.-S., & Yang, R. (2012) · Shock · doi:10.1097/shk.0b013e3182734ff9 · Cited by 11
Savu, D., Petcu, I., Temelie, M., Mustăciosu, C. C., & Moisoi, N. (2014) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2014.11.005 · Cited by 12
Cytotoxic activity to acute myeloid leukemia cells by Antp-TPR hybrid peptide targeting Hsp90
Horibe, T., Kawamoto, M., Kohno, M., & Kawakami, K. (2012) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2012.02.016 · Cited by 12
Xie, W. F., Xu, R., Fan, C., Yang, C., Chen, H., & Cao, Y. (2021) · Frontiers in Public Health · doi:10.3389/fpubh.2021.724239 · Cited by 12
Altered cardiac mitochondrial dynamics and biogenesis in rat after short-term cocaine administration
Wen, S., Unuma, K., Funakoshi, T., Aki, T., & Uemura, K. (2021) · Scientific Reports · doi:10.1038/s41598-021-03631-y · Cited by 12
Patra, M., Weiss, C., Abu‐Libdeh, B., Ashhab, M., Abuzer, S., Elpeleg, O. N., Mahajnah, M. M., Kessel, A., & Azem, A. (2019) · European Journal of Human Genetics · doi:10.1038/s41431-019-0358-9 · Cited by 12
Jenkins, E. C., Chattopadhyay, M., & Germain, D. (2021) · Aging and Cancer · doi:10.1002/aac2.12035 · Cited by 11
The Role of Hsp90 in Retinal Proteostasis and Disease
Ziaka, K., & van der Spuy, J. (2022) · Biomolecules · doi:10.3390/biom12070978 · Cited by 13
Thosapornvichai, T., Huangteerakul, C., Jensen, A. N., & Jensen, L. T. (2022) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2022.104000 · Cited by 11
Mitochondrial Unfolded Protein Response (mtUPR) and Diseases
Yang, M., Luo, S., Chen, W., He, L., Liu, D., Wang, X., Xiao, L., & Sun, L. (2023) · Current Medicinal Chemistry · doi:10.2174/0929867331666230822095924 · Cited by 12
Jing, J., Wang, J., Wu, Q., Yin, S., He, Z., Tang, J., Jia, G., Liu, G., Chen, X., Tian, G., et al. (2024) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-024-01051-2 · Cited by 11
Self-citationImbalanced Skeletal Muscle Mitochondrial Proteostasis Causes Bone Loss
Jin, Z., Mao, Y., Guo, Q., Yin, Y., Kiram, A., Zhou, D., Yang, J., Zhou, Z., Xue, J., Feng, Z., et al. (2024) · Research · doi:10.34133/research.0465 · Cited by 13
Mitochondrial DNA removal is essential for sperm development and activity
Chen, Z., Zhang, F., Lee, A., Yamine, M., Wang, Z., Zhang, G., Combs, C. A., & Xu, H. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00377-5 · Cited by 13
Skeletal Phenotypes Due to Abnormalities in Mitochondrial Protein Homeostasis and Import
Zhao, T., Goedhart, C., Pfeffer, G., Greenway, S. C., Lines, M. A., Khan, A., Innes, A. M., & Shutt, T. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218327 · Cited by 12
Angius, A., Scanu, A. M., Arru, C., Muroni, M. R., Carru, C., Porcu, A., Cossu‐Rocca, P., & Miglio, M. R. D. (2021) · Medicina · doi:10.3390/medicina57111257 · Cited by 10
Perez, M. F., & Sarkies, P. (2021) · Genome biology · doi:10.1186/s13059-021-02541-6 · Cited by 11
TDP-43 is a potential marker of dopaminergic neuronal damage caused by atrazine exposure
Li, G., Wang, K., Zuo, K., Shi, G., Cai, Q., & Huang, M. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.114780 · Cited by 11
Lin, N., Sun, L., Chai, J., Qi, H., Zhao, Y., Ma, J., Xia, M., & Hu, X. (2024) · Cancer Cell International · doi:10.1186/s12935-024-03210-x · Cited by 12
Mitochondrial Compartmentalized Protein Folding and Tumor Cell Survival
Altieri, D. C. (2011) · Oncotarget · doi:10.18632/oncotarget.273 · Cited by 11
Magarin, M., Pohl, T., Lill, A., Schulz, H., Blaschke, F., Heuser, A., Thierfelder, L., Donath, S., & Drenckhahn, J. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.04.007 · Cited by 12
Guo, Z. S., Liu, Z., Sathaiah, M., Wang, J., Ravindranathan, R., Kim, E. S., Huang, S., Kenniston, T. W., Bell, J. C., Zeh, H. J., et al. (2017) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2017.09.007 · Cited by 11
Self-citationFailure to Guard: Mitochondrial Protein Quality Control in Cancer
Friedlander, J. E., Shen, N., Zeng, A., Korm, S., & Feng, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158306 · Cited by 11
Soo, S. K., & Raamsdonk, J. M. V. (2021) · PubMed Central · doi:10.17912/micropub.biology.000484 · Cited by 13
CHOP T/C and C/T haplotypes contribute to early‐onset type 2 diabetes in Italians
Gragnoli, C. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21553 · Cited by 11
Kumar, S., Chaudhary, A. K., Kumar, R., O’Malley, J., Dubrovska, A., Wang, X., Yadav, N., Goodrich, D. W., & Chandra, D. (2016) · Molecular Oncology · doi:10.1016/j.molonc.2016.03.007 · Cited by 11
A brief history of the discovery of the mitochondrial unfolded protein response in mammalian cells
Hoogenraad, N. J. (2017) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-017-9703-2 · Cited by 11
Self-citationMaria Jose Perez, J., Lam, A., Weissleder, C., Bertoli, F., Raji, H., Bosch, M., Nemazanyy, I., Kalb, S., Kehili, M., Hirschberg, I., et al. (2026) · Nature Neuroscience · doi:10.1038/s41593-026-02320-1 · Cited by 15
Mitochondrial Dysfunction: A Roadmap for Understanding and Tackling Cardiovascular Aging
Zhang, H., Muhetarijiang, M., Chen, R. J., Hu, X., Han, J., Zheng, L., & Chen, T. (2024) · Aging and Disease · doi:10.14336/ad.2024.0058 · Cited by 12
Unfolded proteins in the mitochondria activate HRI and inhibit mitochondrial protein translation
Wu, Y., Yang, Y., Qin, X., Zhang, Z., Ullah, M., Li, Y., & Zhang, Z. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111353 · Cited by 12
Deafness-associated mitochondrial 12S rRNA mutation reshapes mitochondrial and cellular homeostasis
He, Y., Tang, Z., Zhu, G., Cai, L., Chen, C., & Guan, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108124 · Cited by 10
Mitochondrial inorganic polyphosphate is required to maintain proteostasis within the organelle
da Costa, R. T., Urquiza, P., Perez, M. M., Du, Y., Khong, M. L., Zheng, H., Guitart‐Mampel, M., Elustondo, P. A., Scoma, E. R., Hambardikar, V. D., et al. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1423208 · Cited by 10
Intracellular and Intercellular Signalling Mechanisms following DNA Damage Are Modulated By PINK1
Temelie, M., Savu, D., & Moisoi, N. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1391387 · Cited by 10
Output Regulation and Function Optimization of Mitochondria in Eukaryotes
Zeng, M., He, Y. T., Du, H., Yang, J., & Wan, H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.598112 · Cited by 10
Mitochondrial protein import as a quality control sensor
Maity, S., & Chakrabarti, O. (2021) · Biology of the Cell · doi:10.1111/boc.202100002 · Cited by 10
Stress Responses Elicited by Misfolded Proteins Targeted to Mitochondria
Rao, K. B. N., Pandey, P., Sarkar, R., Ghosh, A., Mansuri, S., Ali, M., Majumder, P., Kumar, K. R., Ray, A., Raychaudhuri, S., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167618 · Cited by 10
Kim, S., Kim, J.-B., Kim, J., & Lee, J.-K. (2007) · Neuroreport · doi:10.1097/wnr.0b013e32801299cc · Cited by 10
Navarro, B. S., Michiels, N. K., Köhler, H., & D’SOUZA, T. G. (2009) · Hydrobiologia · doi:10.1007/s10750-009-9968-5 · Cited by 10
Mitochondria in Health and Disease
Meiliana, A., Dewi, N. M., & Wijaya, A. (2019) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v11i1.779 · Cited by 13
mTORC2 orchestrates monocytic and granulocytic lineage commitment by an ATF5-mediated pathway
Zhao, Y., Zhao, C., Guo, H., Zhang, Z., Xu, H., Shi, M., Xu, Y., Dong, W., & Zhao, Y. (2023) · iScience · doi:10.1016/j.isci.2023.107540 · Cited by 9
Targeting mitochondrial quality control for myocardial ischemia-reperfusion injury
Yuxuan, H., Sixu, R., Liu, C., Zheng, X., & Zhu, C. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102046 · Cited by 11
Stressful situations: Molecular insights on mitochondrial quality control pathways
Romanelli, S., & Trempe, J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110483 · Cited by 11
Maintenance of protein homeostasis in glia extends lifespan in C. elegans
Wang, L., & Bianchi, L. K. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113648 · Cited by 8
Li, G., Gu, J., Zhou, X., Wu, T., Li, X., Hua, R., Hai, Z., Xiao, Y., Su, J., Yeung, W. S. B., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1122012 · Cited by 10
Ikeda, H., Muroi, M., Kondoh, Y., Ishikawa, S., Kakeya, H., Osada, H., & Imoto, M. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00381 · Cited by 11
Insight into the Interactome of Intramitochondrial PKA Using Biotinylation-Proximity Labeling
Amer, Y. O., & Hébert-Chatelain, É. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218283 · Cited by 9
A tRNA processing enzyme is a key regulator of the mitochondrial unfolded protein response
Held, J. P., Feng, G., Saunders, B. R., Pereira, C. V., Burkewitz, K., & Patel, M. R. (2022) · eLife · doi:10.7554/elife.71634 · Cited by 8
Li, C., Li, N., Zhang, Z., Song, Y., Li, J., Wang, Z., Hai, B., & Zhang, Y. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1127524 · Cited by 10
Protein Misfolding as a Disease Determinant
Gow, A. (2004) · Elsevier eBooks · doi:10.1016/b978-012439510-7/50095-4 · Cited by 9
The mitochondrial unfolded protein response: acting near and far
Charmpilas, N., Li, Q., & Hoppe, T. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0107 · Cited by 8
Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress
Ehses, K., López-Alonso, J. P., Antico, O., Lang, Y., Rudack, T., Azem, A., Muqit, M. M. K., Ubarretxena‐Belandia, I., & Fernández‐Busnadiego, R. (2026) · Science Advances · doi:10.1126/sciadv.aed3579 · Cited by 8
Key, J., Gispert, S., Koepf, G., Steinhoff‐Wagner, J., Reichlmeir, M., & Auburger, G. W. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417503 · Cited by 9
Ergun, Y., Imamoglu, G., Cozzolino, M., Demirkiran, C., Başar, M., Garg, A., Yildirim, R. M., & Seli, E. U. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031866 · Cited by 8
Caenorhabditis elegans homologue of Fam210 is required for oogenesis and reproduction
Kang, J. X., Zhou, H., Sun, F., Chen, Y., Zhao, J., Yang, W., Xu, S., & Chen, C. (2020) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2020.10.008 · Cited by 9
Mitochondrial Membrane Intracellular Communication in Healthy and Diseased Myocardium
Kumar, V. K., Lackey, A. I., Snyder, J. E., Karhadkar, S. S., Rao, A. D., DiCarlo, A., & Sato, P. Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.609241 · Cited by 8
The Many Roles Mitochondria Play in Mammalian Aging
Batalha, C. M. P. F., Vercesi, A. E., & de Souza-Pinto, N. C. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0074 · Cited by 8
Linkage studies for T2D in Chop and C/EBPbeta chromosomal regions in Italians
Gragnoli, C., Pierpaoli, L., Piumelli, N., & Chiaramonte, F. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21132 · Cited by 8
Yang, J., Gu, J., Hu, Y., Wang, N., Gao, J., & Wang, P. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01160-7 · Cited by 8
Matthews, T. A., Abel, A., Demme, C., Sherman, T., Pan, P., Halterman, M. W., Parkkila, S., & Nehrke, K. W. (2013) · Brain Research · doi:10.1016/j.brainres.2013.11.018 · Cited by 8
LonP1 Orchestrates UPR mt and UPR ER and Mitochondrial Dynamics to Regulate Heart FunctionPreprint
Lü, B., Shangguan, F., Huang, D., Gong, S., Shi, Y., Song, Z., Jia, L., Xu, J., Yan, C., Chen, T., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/564492 · Cited by 8
Lung, spleen and oesophagus tissue remains stable for scRNAseq in cold preservationPreprint
Madissoon, E., Wilbrey-Clark, A., Miragaia, R. J., Saeb‐Parsy, K., Mahbubani, K. T. A., Georgakopoulos, N., Harding, P., Polański, K., Nowicki-Osuch, K., Fitzgerald, R. C., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/741405 · Cited by 8
Quality control of proteins in the mitochondrion
Nolden, M., Kisters–Woike, B., Langer, T., & Graef, M. (2006) · Springer eBooks · doi:10.1007/4735_106 · Cited by 8
Türkel, İ., Kubat, G. B., Fatsa, T., Acet, O., Özerkliğ, B., Yazgan, B., Şımşek, G., Singh, K. K., & Koşar, Ş. N. (2024) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2024.149532 · Cited by 8
The mitochondrial intermembrane space – a permanently proteostasis-challenged compartment
Weith, M., Weiss, K., Stobbe, D., & Riemer, J. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0108 · Cited by 10
Kirmes, I., Hung, G. C. C., Hahn, A., Dai, C.-Y., Campbell, D., Ahier, A., Lee, R. S. Y., Palmer, A., & Zuryn, S. (2025) · Nature Communications · doi:10.1038/s41467-025-67198-2 · Cited by 7
Wang, P., Chen, L., Wang, N., Miao, L., & Zhao, Y. (2024) · Development · doi:10.1242/dev.202165 · Cited by 7
Cilleros-Holgado, P., Gómez-Fernández, D., Piñero-Pérez, R., Romero-Domínguez, J. M., Talaverón-Rey, M., Reche-López, D., Suarez-Rivero, J. M., Álvarez-Córdoba, M., Romero-González, A., López-Cabrera, A., et al. (2024) · Biomolecules · doi:10.3390/biom14050598 · Cited by 7
Safakli, R., Gray, S., Bernardi, N., & Smyrnias, I. (2024) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2024.106704 · Cited by 7
Ghadanian, T., Iyer, S., Lazzari, L., & Vera, M. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-12-0564 · Cited by 10
Wolff, S., & Dillin, A. G. (2013) · Nature · doi:10.1038/497442a · Cited by 7
Discovery of novel indolin-2-one compounds as potent inhibitors of HsClpP for cancer treatment
Song, R., Yang, Y., Huang, J., Qiao, W., Luo, B., Ju, Y., Yang, T., & Luo, Y. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104820 · Cited by 7
Zhou, X., Mikaeloff, F., Curbo, S., Zhao, Q., Kuiper, R., Végvári, Á., Neogi, U., & Karlsson, A. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab168 · Cited by 7
Self-citationHandling of human short-chain acyl-CoA dehydrogenase (SCAD) variant proteins in transgenic mice
Kragh, P. M., Pedersen, C. B., Schmidt, S. P., Winter, V., Vajta, G., Gregersen, N., Bolund, L., & Corydon, T. J. (2007) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2007.03.005 · Cited by 7
Mitochondrial proteases and their roles in mitophagy in plants, animals, and yeast
Ludwig, K., & Czarna, M. (2025) · Plant and Cell Physiology · doi:10.1093/pcp/pcaf038 · Cited by 5
Mitochondrial tRNA processing defects reprogram mitochondrial and cellular homeostasis
Zhu, G., He, Y., Li, X., Xiao, Y., Zhan, H., Duan, M., & Guan, M. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110334 · Cited by 6
Li, X., Maaß, S., Ferrero‐Bordera, B., Zhang, Z., Wang, M., Sietsema, E., Liu, L., Divinagracia, M. L., van Dijl, J. M., & Buist, G. (2025) · Virulence · doi:10.1080/21505594.2025.2514790 · Cited by 6
Epigenetic regulation of the respiratory chain by a mitochondrial distress-related redox signal
Baeken, M. W., Borlepawar, A., Kötzner, P., Richly, H., Behl, C., Moosmann, B., & Hajieva, P. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1608400 · Cited by 6
Jeong, J., Kim, J. H., & Kim, M. S. (2025) · Genes · doi:10.3390/genes16080957 · Cited by 6
Wang, H., Liu, Y., Liu, J., Zhang, S., Li, X., Sun, L., Liu, F., Liu, Y., & Xiao, L. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115641 · Cited by 6
Function and regulation of the mitochondrial stress response
Sheetz, J. B., Chandrasekhar, S., & Rapé, M. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01769-9 · Cited by 8
Mitochondrial quality control in health and disease: mechanisms and therapeutic targets
Creus, A., Mohapatra, S., Ortega, L., & Sebastián, D. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02813-2 · Cited by 7
iMPAQT reveals that adequate mitohormesis from TFAM overexpression leads to life extension in mice
Igami, K., Kittaka, H., Yagi, M., Gotoh, K., Matsushima, Y., Ide, T., Ikeda, M., Ueda, S., Nitta, S.-I., Hayakawa, M., et al. (2024) · Life Science Alliance · doi:10.26508/lsa.202302498 · Cited by 6
Ye, Z., Chai, R., Luan, Y., Du, Y., Xue, W., Shi, S., Wu, H., Yi, W., Zhang, L., & Hu, Y. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1146963 · Cited by 6
Molecular mechanisms of hepatic lipid metabolism disorders: Focus on mitochondrial quality control
Yu, J., Huang, J., Xia, T., Li, M., & Li, R. (2024) · Portal hypertension & cirrhosis · doi:10.1002/poh2.95 · Cited by 6
Ranjan, K. (2020) · Gastrointestinal Disorders · doi:10.3390/gidisord2030024 · Cited by 6
Deocaris, C. C., Kaul, S. C., & Wadhwa, R. (2012) · Springer eBooks · doi:10.1007/978-94-007-3027-4_2 · Cited by 6
Signaling pathway of mitochondrial stress
Xue, F., & Zhang, H. (2017) · Frontiers in Laboratory Medicine · doi:10.1016/j.flm.2017.02.009 · Cited by 7
Expression of chaperonin 60 in the hippocampus of the streptozotocin diabetic rat
Yuan, J., Young, B. J., & Martinus, R. D. (2006) · Neuroreport · doi:10.1097/01.wnr.0000201503.15632.06 · Cited by 6
Cross-Organ Mitochondrial Communication in Stress and Disease
Shen, K., Durieux, J., & Dillin, A. G. (2025) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-062124-024150 · Cited by 5
Proteostasis of organelles in aging and disease
Nabawi, Y., Doğan, C., Petrovic, D., Perçin, G. I., Koyuncu, S., & Vílchez, D. (2026) · FEBS Journal · doi:10.1111/febs.70439 · Cited by 6
Mitochondrial Precursor Overaccumulation Stress
Coyne, L. P., & Chen, X. J. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051424-061016 · Cited by 7
mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import
Banerjee, R., Trauschke, V., Bertram, N., Aretz, I., Osman, C., Lamb, D. M., & Mokranjac, D. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2526136123 · Cited by 6
A multilayered stress‐response circuit: The mammalian mitochondrial UPR
Czechowicz, P., Więch, A., Kozioł, S., Dudzik, J., Collawn, J. F., & Bartoszewski, R. (2026) · FEBS Journal · doi:10.1111/febs.70607 · Cited by 5
Mitochondrial “dysmorphology” in variant classification
Shamseldin, H. E., Alhashem, A. M., Tabarki, B. M., Abdulwahab, F., Hashem, M., Sougrat, R., & Alkuraya, F. S. (2021) · Human Genetics · doi:10.1007/s00439-021-02378-w · Cited by 6
Senese, R., Petito, G., Silvestri, E., Ventriglia, M., Mosca, N., Potenza, N., Russo, A., Falvo, S., Manfrevola, F., Cobellis, G., et al. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1464773 · Cited by 5
UPRmt alleviates bone cancer pain through the restoration of mitochondrial function
Li, D., Xie, M., Zeng, H., Yu, J., Xu, R., Wang, Z., Huang, Y., Yang, Y., & Sun, Y. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114568 · Cited by 5
Grün, B., Tirre, M., Pyschny, S., Singh, V. P., Kehl, H.-G., Jux, C., & Drenckhahn, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1011639 · Cited by 5
Pathological implications of cellular stress in cardiovascular diseases
Ulaganathan, T., Perales, S. G., Mani, S., Baskhairoun, B. A., & Rajasingh, J. (2023) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2023.106397 · Cited by 6
Perera, G., Power, L. H., Larson, A., Codden, C. J., Awata, J., Batorsky, R., Strathdee, D., & Chin, M. T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411594 · Cited by 5
Testicular expression of heat SHOCK proteins 60, 70, and 90 in cryptorchid horses
Cinone, M., Albrizio, M., Guaricci, A. C., Lacitignola, L., & Desantis, S. (2024) · Theriogenology · doi:10.1016/j.theriogenology.2024.01.019 · Cited by 5
Metadata
- Authors
- Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J.
- Affiliations
- La Trobe University (AU)
- Corresponding author
- Hoogenraad, Nicholas J.
- ORCID
- Zhao, Quan
- Venue
- The EMBO Journal
- Published
- 2002-09-02
- Volume
- 21
- Issue
- 17
- Pages
- 4411-4419
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC126185
- OpenAlex
- W2108738634
- Cited by
- 1,026
- References
- 55
- Citations by year
- 2026: 58 · 2025: 64 · 2024: 71 · 2023: 59 · 2022: 71 · 2021: 88 · 2020: 77 · 2019: 60 · 2018: 60 · 2017: 46 · 2016: 50 · 2015: 42 · 2014: 45 · 2013: 38 · 2012: 29
- FWCI
- 4.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council
- Australian Research Council
- National Health and Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitochondrial stress response, unfolded protein accumulation, mitochondrial matrix, CHOP, C/EBPβ, transcriptional regulation, chaperonin 60, GroES, ClpP, unfolded protein response, mammalian cells
- MeSH terms
- Adenosine Triphosphatases, Animals, Cell Nucleus, Chlorocebus aethiops, Gene Expression Regulation, Genes, Dominant, Heat-Shock Proteins, Mitochondria, Ornithine Carbamoyltransferase, Promoter Regions, Genetic, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Regulatory Sequences, Nucleic Acid, Serine Endopeptidases, Stress, Physiological, Transcription Factors, Transcription, Genetic, Transfection, Signal Transduction, Sequence Deletion, Protein Folding, Chaperonin 60, Chaperonin 10, COS Cells, Protein Transport, CCAAT-Enhancer-Binding Proteins, Endopeptidase Clp, HSP40 Heat-Shock Proteins, Transcription Factor CHOP
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