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 901–999 of 999
Searching for the elusive mitochondrial longevity signal in C. elegans
Bennett, C. F., Choi, H., & Kaeberlein, M. R. (2014) · Worm · doi:10.4161/worm.29868 · Cited by 1
Key patient demographics shape innate immune topography in noncritical hypoxic COVID-19 pneumonia
Billi, A. C., Wasikowski, R., Ma, F., Yalavarthi, S., Hoy, C. K., Zuo, Y., Patrick, M. T., Shah, N., Parker, C., Aaronson, C., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.166110 · Cited by 1
Haak, J. L., Kregel, K. C., & Bloomer, S. A. (2023) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00610.2023 · Cited by 1
Mitochondrial dysfunction and metabolic syndrome
Bir, A., Ghosh, A., Müller, W. E., & Ganguly, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-85732-1.00043-8 · Cited by 1
The Chloroplast Genome and Nucleo-Cytosolic Crosstalk
Rochaix, J., & Ramundo, S. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1136-3_3 · Cited by 1
Aging in Drosophila melanogaster
Gumeni, S., & Trougakos, I. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11410-2 · Cited by 3
Moving beyond the current limits of data analysis in longevity and healthy lifespan studies
Goh, W. W. B., Thalappilly, S., & Thibault, G. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2019.08.008 · Cited by 2
Avendaño‐Monsalve, M. C., Ponce‐Rojas, J. C., & Funes, S. (2021) · TIP Revista Especializada en Ciencias Químico-Biológicas · doi:10.22201/fesz.23958723e.2021.370
Wender, N. (2013) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3753 · Cited by 1
Functional analysis of mammalian m-AAA proteases
Ehses, S. (2008) · Kölner Universitäts PublikationsServer (Universität zu Köln) · Cited by 1
Analysis of MTORC2 in regulating aging, metabolism and cardiac disease in Drosophila melanogaster
Chang, K. (2020) · Iowa State University Digital Repository (Iowa State University) · doi:10.31274/etd-20210114-24 · Cited by 1
OLA1 Phosphorylation: A Distress Signal from Damaged Endothelial Mitochondria?
Cloonan, S. M. (2022) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2022-0450ed · Cited by 1
Enhanced Inflammatory Signaling Driven by Metabolic Switch in Aicardi-Goutières SyndromePreprint
Batignes, M., Luka, M., Jagtap, S., de Cevins, C., Nemazanyy, I., Fali, T., García-Paredes, V., Carbone, F., Pérot, B. P., Neven, B., et al. (2023) · SSRN Electronic Journal · doi:10.1101/2023.02.23.529707 · Cited by 1
Activation of the mitochondrial unfolded protein response regulates the formation of stress granulesPreprint
Lopez-Nieto, M., Sun, Z., Relton, E., Safakli, R. N., Freibaum, B. D., Taylor, J. P., Ruggieri, A., Smyrnias, I., & Locker, N. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.26.564187 · Cited by 1
Maria Jose Perez, J., Lam, A., Weissleder, C., Bertoli, F., Raji, H., Bosch, M., Nemazanyy, I., Kalb, S., Kehili, M., Hirschberg, I., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.03.610925 · Cited by 1
Mitochondrial proteostatic stress disrupts mitoribosome biogenesis and translationPreprint
Holthusen, H., Trinkaus, V. A., Gonzalez, C. F., Saha, I., Pachmayr, I., Wade, O. K., Deiser, A., Hummel, B., Yuste‐Checa, P., Ehses, K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.05.673478 · Cited by 1
Revueltas, E. S., Almes, L., Tokoyoda, K., Deng, X., Subirana, A. C., Ferreira‐Gomes, M., Cornelis, R., Dong, J., Heinrich, F., Durek, P., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.02.714263 · Cited by 1
Durham, H. D. (2008) · Springer eBooks · doi:10.1007/978-1-4020-8231-3_10
Mouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · DSpace@MIT (Massachusetts Institute of Technology)
Emerging Concepts Linking Mitochondrial Stress Signalling and Parkinson's Disease
Ana, C., Miguel, L., & Loh, S. H. Y. (2012) · InTech eBooks · doi:10.5772/34689
Protein Expression In Prostate Cancer
Lexander, H. (2006) · Figshare
Yang, M. Q., King, D. C., & Elnitski, L. L. (2008) · doi:10.1002/9780470397428.ch15
Wosniak, J. (2008) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2008.tde-24062008-152937
Sánchez, M. E. G. (2013) · Gredos (University of Salamanca) · doi:10.14201/gredos.122970
Role of the AAA protease Yme1 in folding of proteins in the mitochondrial intermembrane space
Schreiner, B. (2013) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.15299
Xu, W. (2015) · DukeSpace (Duke University)
Crescio, C. (2013) · UnissResearch (Università degli Studi di Sassari)
A Brief Introduction to the Eukaryotic Cell Stress Proteins
Henderson, B. E. (2013) · Heat shock proteins · doi:10.1007/978-94-007-6787-4_2
Experimental Inhibition of Peptide Fibrillogenesis by Synthetic Peptides, Carbohydrates and Drugs
Srinivasan, A. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_12
Functional characterization of NLRC3
Bremer, L. (2014) · MACAU: Open Access Repository of Kiel University (University Library Kiel)
Effects of metformin on human monocytic THP-1 cells - Implications for type 2 diabetes mellitus
Tsuei, A.-C. (2010) · Research Commons (University of Waikato)
Chaperones and Proteases of Mitochondria: From Protein Folding and Degradation to Mitophagy
Voos, W., Rüb, C., & Bruderek, M. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_12
Raschke, I. (2009) · Kölner Universitäts PublikationsServer (Universität zu Köln)
Djohari, M., As’ád, S., Arif, M., & Wijaya, A. (2013) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v5i1.49
Torelli, N. Q. (2014) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.46.2014.tde-25032015-115054
The impact of the mitochondrial bottleneck on mtDNA disease risk and embryogenesis
Otten, A. B. C. (2016) · Research Publications (Maastricht University) · doi:10.26481/dis.20161115ao
Role of Energy Metabolism in the Thermogenic Gene Program
Nam, M. (2017) · eScholarship@UMassChan · doi:10.13028/m2np4f
Deol, N. (2016) · TSpace (University of Toronto)
Ramakrishnan, A. (2014) · TSpace (University of Toronto)
Hormesis and Hormetins in Aging
Rattan, S. I. S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11282-6
Taşkin, A. A., Poveda-Huertes, D., & Vögtle, F. ‐. (2019) · Molecular & Cellular Oncology · doi:10.1080/23723556.2019.1698256
Mitochondria as a Key Player in Aging
Banerjee, R., & Rath, P. C. (2020) · Springer eBooks · doi:10.1007/978-981-32-9005-1_10
Epigenetic codes of mitochondrial homeostasis
Liu, Y. (2021) · Nature Aging · doi:10.1038/s43587-021-00034-6
A tRNA processing enzyme is a central regulator of the mitochondrial unfolded protein responsePreprint
Held, J. P., Saunders, B. R., Pereira, C. V., & Patel, M. R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.22.449331
Mitochondrial Dynamics and Stress Signaling in Cancer
Rubio‐Patiño, C., & Chipuk, J. E. (2021) · Oxford University Press eBooks · doi:10.1093/oxfordhb/9780190932183.013.19
Mitochondrial metabolism and carcinogenesis
Aras, S., Purandare, N., & Grossman, L. I. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822416-8.00001-4
Placentation and Placental Function in Normal and Preeclamptic Pregnancies
Burton, G. J., Cindrová‐Davies, T., Yung, H. W., & Taylor, R. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-818417-2.00004-x
Hekimi, S. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717982023.793471865
Michaelis, J. B. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.69732
Wang, P., Wang, Q., Chen, L., Cao, Z. H., Zhao, H., Su, R., Wang, N., Ma, X., Jin, S., Chen, X., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-2162150/v1
Tamura, T., & Hamachi, I. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2863-8_11
Resolving Geroplasticity to the Balance of Rejuvenins and Geriatrins
TABIBZADEH, S. S. (2022) · Aging and Disease · doi:10.14336/ad.2022.0414
Plasticidade mitocondrial na doença de Chagas
Ribeiro, M. A. C. (2022) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2022.tde-21082023-154733
Wu, Y., Yang, Y., Qin, X., Zhang, Z., Ullah, M., Li, Y., & Zhang, Z. (2024) · Research Square · doi:10.21203/rs.3.rs-4121132/v1
Mitochondrial Unfolded Protein Response and Its Research Progress in Some Malignant Tumors
王, 延. (2024) · Advances in Clinical Medicine · doi:10.12677/acm.2024.143814
Ojha, R., Tantray, I., Banerjee, S., Rimal, S., Thirunavukkarasu, S., Srikris, S., Chiu, W., Mete, U. K., Sharma, A. J., Kakkar, N., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4899860/v1
Graves, P. R., Fennell, E. M. J., Ashamalla, H. L., Carter, S. A., Holmuhamedov, E., & Graves, L. M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00019-3
Thapa, B. V., Das, M., Held, J. P., & Patel, M. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.03.636310
Differential effects of lifespan-extending genetic manipulations in an animal model of MJD/SCA3
Costa, M. D., Silva, J. D. D., Almeida, D., Pereira‐Sousa, J., Vilasboas‐Campos, D., Fernandes, J. H., Teixeira‐Castro, A., & Maciel, P. (2025) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2025.112064
Bunnell, D., Buhl, M., McGee, J., Milas, G., & Chtarbanova, S. (2025) · Research Square · doi:10.21203/rs.3.rs-6816306/v1
A canonical chloroplast unfolded protein response triggered by misfolded polypeptidesPreprint
Cantoia, A., Bertero, F., Berrocal, R., Ceccarelli, E. A., Blanco, N. E., & Rosano, G. L. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.11.659047
Genetic mapping of lifespan and mitochondrial stress response in C. elegansPreprint
Li, X., Li, W., Gao, A. W., Zhu, Y., Katsyuba, E., Overmyer, K. A., Li, T. Y., Wang, Z., Legon, L., Plantade, L., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.26.661693
The Role of Autophagy and Mitophagy in Cardiomyocyte Ischemic Injury
Gottlieb, R. A., & Pourpirali, S. (2025) · Learning materials in biosciences · doi:10.1007/978-3-031-88121-3_10
Ravera, F., Angelini, F., Bocchino, P. P., Marcelli, G., Gobello, G., Giannino, G., Merlino, G., Guidi, B. D., Destefanis, A., Prever, G. M. B. D., et al. (2025) · Cardiogenetics · doi:10.3390/cardiogenetics15030020
Multisite Assessment of Methods for Cell Preservation Upstream of Single-Cell RNA Sequencing
Kolling, F., Podnar, J. W., Wilkins, O. M., Fraser, C. J., MacDonald, M. L., Polson, S. W., Herbert, Z. T., Chittur, S. V., Hayden, A., Kuentzel, M. L., et al. (2026) · Journal of Biomolecular Techniques JBT · doi:10.7171/001c.162768 · Cited by 1
Adedoja, A., Stuhr, N., Zhou, Y., Zhang, Y., Yerevanian, A. I., & Soukas, A. A. (2025) · Genes & Development · doi:10.1101/gad.352979.125
Hypoxia-induced mitoROS triggers M1 linear ubiquitin chains and activates NF-κB signalingPreprint
Tal, K., Ram, J., Reis, N., Maniv, I., Alban, O., Glickman, M. H., & Sulkshane, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.06.686916
Yang, W., Fan, S., Guevara, C. R., Kratochwil, M., Thilmany, S. C., Sugawa, M. D., Dencher, N. A., & Poetsch, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262211155
Thapa, B. V., Das, M., Taylor, D. I., Held, J. P., & Patel, M. R. (2025) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkaf298
Liu, Y., Zhang, L., Zhang, S., Liu, J., Li, X., Yang, K., Danyi, Y., Liu, Y., Sun, L., 刘伏友, et al. (2023) · Figshare · doi:10.6084/m9.figshare.22688753
Jing, J., He, Y., Liu, Y., Tang, J., Wang, L., Jia, G., Liu, G., Chen, X., Tian, G., Cai, J., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23292129
Jing, J., He, Y., Liu, Y., Tang, J., Wang, L., Jia, G., Liu, G., Chen, X., Tian, G., Cai, J., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23292120
Jing, J., He, Y., Liu, Y., Tang, J., Wang, L., Jia, G., Liu, G., Chen, X., Tian, G., Cai, J., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23292123
Jing, J., Wang, J., Wu, Q., Yin, S., He, Z., Tang, J., Jia, G., Liu, G., Chen, X., Tian, G., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26737491
Self-citationLin, N., Sun, L., Chai, J., Qi, H., Zhao, Y., Ma, J., Xia, M., & Hu, X. (2024) · Figshare · doi:10.6084/m9.figshare.26669193
Jing, J., Wang, J., Wu, Q., Yin, S., He, Z., Tang, J., Jia, G., Liu, G., Chen, X., Tian, G., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26737488
Self-citationLi, C., Lu, C., Ma, Z., Zhao, T., Xiao, M., Xu, Z., Sun, Z., Wu, Q., Wang, L., & Zhao, L. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1717925
Bnip3lb-driven mitophagy maintains fate of the embryonic hematopoietic stem cell pool
Meader, E., Walcheck, M. T., Leder, M. R., Delaney, P., Falchetti, M., Jing, R., Li, C., Kambli, N. K., Wrighton, P. J., Sugden, W. W., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69593-9
Jeejo, M., Mathew, M., Mohanakumar, K. P., & Rajamma, U. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102148 · Cited by 2
Modulation of the immuno-metabolism axis in type-1 diabetes
Boubenna, N. (2010) · theses.fr (ABES) · doi:10.70675/2f05b49ez9e17z4db0zaa84z316c3f57dfd9
Links between Germline and Longevity in Caenorhabditis elegans
Goudeau, J. F. (2011) · theses.fr (ABES) · doi:10.70675/544ae7cczac83z426azbb95zd11d7e7a73ab
Role of alphaOGG1 in the Maintenance of Mitochondrial Physiology
Lia, D. (2018) · theses.fr (ABES) · doi:10.70675/679004d9z93c1z48b3zbba9zf7828ee3d37a
The roles of FANCD2 in the maintenance of common fragile site stability
Fernandes, P. (2018) · theses.fr (ABES) · doi:10.70675/0d35c80ezf356z4cabza1edz594f25dbe717
Hammoudi, N. (2021) · theses.fr (ABES) · doi:10.70675/4595a58dzcce7z43f2zbd07z10eb7653d7c5
Mitochondrial RNA metabolism defects in the development of mitochondrial diseases
Cafournet, C. (2022) · theses.fr (ABES) · doi:10.70675/eb6cbbdfz9f35z424ezb43bz7ec5049f8ec0
Habieb, M. E., Ali, M. M., Abd-ElRaouf, A., & Abdou, F. Y. (2026) · Scientific Reports · doi:10.1038/s41598-026-46553-3
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