Induction of ubiquitin C (UBC) gene transcription is mediated by HSF 1: role of proteotoxic and oxidative stress
Open accessAbstract
The polyubiquitin gene ubiquitin C (UBC) is considered a stress protective gene and is upregulated under various stressful conditions, which is probably a consequence of an increased demand for ubiquitin in order to remove toxic misfolded proteins. We previously identified heat shock elements (HSE s) within the UBC promoter, which are responsible for heat shock factor (HSF)1‐driven induction of the UBC gene and are activated by proteotoxic stress. Here, we determined the molecular players driving the UBC gene transcriptional response to arsenite treatment, mainly addressing the role of the nuclear factor‐erythroid 2‐related factor 2 (Nrf2)‐mediated antioxidant pathway. Exposure of HeLa cells to arsenite caused a time‐dependent increase of UBC mRNA, while cell viability and proteasome activity were not affected. Nuclear accumulation of HSF 1 and Nrf2 transcription factors was detected upon both arsenite and MG 132 treatment, while HSF 2 nuclear levels increased in MG 132‐treated cells. Notably, si RNA‐mediated knockdown of Nrf2 did not reduce UBC transcription under either basal or stressful conditions, but significantly impaired the constitutive and inducible expression of well‐known antioxidant response element‐dependent genes. A chromatin immunoprecipitation assay consistently failed to detect Nrf2 binding to the UBC promoter sequence. By contrast, depletion of HSF 1, but not HSF 2, significantly compromised stress‐induced UBC expression. Critically, HSF 1‐mediated UBC trans‐activation upon arsenite exposure relies on transcription factor binding to previously mapped distal HSE s, as demonstrated to occur under proteasome inhibition. These data highlight HSF 1 as the pivotal transcription factor that translates different stress signals into UBC gene transcriptional induction.
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
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?
Three genes overlapped between the microglial and astrocyte factors that were not part of consensus mouse gene lists (UBC, DDIT4 and HSPB1), and these are part of cellular stress and damage response machinery.
“Finally, there were three genes that overlapped between the microglial and astrocyte factors that were not a part of consensus mouse gene lists (UBC, DDIT4 and HSPB1), but which unsurprisingly are also part of cellular stress and damage response machinery52–55.”
From Dissection of artifactual and confounding glial signatures by single-cell sequencing of mouse and human brain (2022) · cites this paper as [55]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860 · see citing works
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,216 · see citing works
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999 · see citing works
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 · see citing works
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works
Primer3Plus, an enhanced web interface to Primer3
Untergasser, A., Nijveen, H., Rao, X., Bisseling, T., Geurts, R., & Leunissen, J. A. M. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm306 · Cited by 2,761 · see citing works
MatInspector and beyond: promoter analysis based on transcription factor binding sites
Cartharius, K., Frech, K., Grote, K., Klocke, B., Haltmeier, M., Klingenhoff, A., Frisch, M., Bayerlein, M., & Werner, T. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti473 · Cited by 1,962 · see citing works
Molecular basis of the Keap1–Nrf2 system
Suzuki, T., & Yamamoto, M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.006 · Cited by 995 · see citing works
Enhancement of proteasome activity by a small-molecule inhibitor of USP14
Lee, B., Lee, M. J., Park, S., Oh, D., Elsasser, S., Chen, P., Gartner, C. A., Dimova, N. V., Hanna, J. W., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 943 · see citing works
Diversity of degradation signals in the ubiquitin–proteasome system
Ravid, T., & Hochstrasser, M. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2468 · Cited by 831 · see citing works
Shen, S., Li, X., Cullen, W., Weinfeld, M., & Le, X. C. (2013) · Chemical Reviews · doi:10.1021/cr300015c · Cited by 822 · see citing works
Malhotra, D., Portales-Casamar, É., Singh, A., Srivastava, S., Arenillas, D. J., Happel, C., Shyr, C., Wakabayashi, N., Kensler, T. W., Wasserman, W. W., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq212 · Cited by 796 · see citing works
Buendía, I., Michalska, P., Navarro, E., Gameiro‐Ros, I., Egea, J., & Leon, R. M. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.11.003 · Cited by 683 · see citing works
McMahon, M. J., Itoh, K., Yamamoto, M. P., Chanas, S. A., Henderson, C. J., McLellan, L. I., Wolf, C. R., Cavin, C., & Hayes, J. D. (2001) · PubMed · Cited by 657 · see citing works
Nguyen, T., Sherratt, P. J., Huang, H.-C., Yang, C. S., & Pickett, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207293200 · Cited by 615 · see citing works
Identification of novel NRF2-regulated genes by ChIP-Seq: influence on retinoid X receptor alpha
Chorley, B. N., Campbell, M. R., Wang, X., Karaca, M., Sambandan, D., Bangura, F., Xue, P., Pi, J., Kleeberger, S. R., & Bell, D. A. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks409 · Cited by 557 · see citing works
Ahn, S., & Thiele, D. J. (2003) · Genes & Development · doi:10.1101/gad.1044503 · Cited by 449 · see citing works
Ubiquitin Conjugation Is Not Required for the Degradation of Oxidized Proteins by Proteasome
Shringarpure, R., Grune, T., Mehlhase, J., & Davies, K. J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206279200 · Cited by 438 · see citing works
Ubiquitin–proteasome pathway and cellular responses to oxidative stress
Shang, F., & Taylor, A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.031 · Cited by 436 · see citing works
Zambelli, F., Pesole, G., & Pavesi, G. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp464 · Cited by 402 · see citing works
Suzuki, T., & Yamamoto, M. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.800169 · Cited by 402 · see citing works
Nguyen, T., Sherratt, P. J., Nioi, P., Yang, C. S., & Pickett, C. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503074200 · Cited by 341 · see citing works
Vihervaara, A., & Sistonen, L. (2014) · Journal of Cell Science · doi:10.1242/jcs.132605 · Cited by 305 · see citing works
Using TESS to Predict Transcription Factor Binding Sites in DNA Sequence
Schug, J. (2008) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0206s21 · Cited by 301 · see citing works
A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling
Dantuma, N. P., Groothuis, T. A., Salomons, F. A., & Neefjes, J. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200510071 · Cited by 265 · see citing works
Kaiser, S. E., Riley, B. E., Shaler, T. A., Trevino, R., Becker, C. H., Schulman, H., & Kopito, R. R. (2011) · Nature Methods · doi:10.1038/nmeth.1649 · Cited by 242 · see citing works
Modulation of proteostasis by transcription factor NRF2 and impact in neurodegenerative diseases
Pajares, M., Cuadrado, A., & Rojo, A. I. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.006 · Cited by 219 · see citing works
Park (2009) · Oncology Reports · doi:10.3892/or_00000427 · Cited by 175 · see citing works
Ryu, K., Maehr, R., Gilchrist, C. A., Long, M. A., Bouley, D. M., Mueller, B., Ploegh, H. L., & Kopito, R. R. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601722 · Cited by 156 · see citing works
Raychaudhuri, S., Loew, C., Körner, R., Pinkert, S., Theis, M., Hayer-Hartl, M. K., Buchholz, F., & Hartl, F. U. (2014) · Cell · doi:10.1016/j.cell.2014.01.055 · Cited by 149 · see citing works
Transcriptional response to stress in the dynamic chromatin environment of cycling and mitotic cells
Vihervaara, A., Sergelius, C., Vasara, J., Blom, M. A. H., Elsing, A. N., Roos‐Mattjus, P., & Sistonen, L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305275110 · Cited by 149 · see citing works
Transcription factors Hsf1 and Nrf2 engage in crosstalk for cytoprotection
Naidu, S. D., Kostov, R. V., & Dinkova‐Kostova, A. T. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.10.011 · Cited by 141 · see citing works
Design and characterization of decoy oligonucleotides containing locked nucleic acids
Crinelli, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.11.2435 · Cited by 140 · see citing works
Self-citationProteasome Inhibition Induces Glutathione Synthesis and Protects Cells from Oxidative Stress
Yamamoto, N., Sawada, H., Izumi, Y., Kume, T., Katsuki, H., Shimohama, S., & Akaike, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603712200 · Cited by 133 · see citing works
Arsenic, Reactive Oxygen, and Endothelial Dysfunction
Ellinsworth, D. C. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.223289 · Cited by 124 · see citing works
Cellular ubiquitin pool dynamics and homeostasis
Park, C.-W., & Ryu, K. (2014) · BMB Reports · doi:10.5483/bmbrep.2014.47.9.128 · Cited by 122 · see citing works
HSF1-Dependent Upregulation of Hsp70 by Sulfhydryl-Reactive Inducers of the KEAP1/NRF2/ARE Pathway
Zhang, Y., Ahn, Y., Benjamin, I. J., Honda, T., Hicks, R. J., Calabrese, V., Cole, P. A., & Dinkova‐Kostova, A. T. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.09.008 · Cited by 113 · see citing works
Regulation of the members of the mammalian heat shock factor family
Björk, J., & Sistonen, L. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07828.x · Cited by 95 · see citing works
Oxidative stress and proteasome inhibitors in multiple myeloma
Lipchick, B. C., Fink, E. E., & Nikiforov, M. A. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.01.029 · Cited by 95 · see citing works
Beyond antioxidant genes in the ancient Nrf2 regulatory network
Lacher, S. E., Lee, J. S., Wang, X., Campbell, M. R., Bell, D. A., & Slattery, M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.044 · Cited by 77 · see citing works
Satoh, T., Rezaie, T., Seki, M., Sunico, C. R., Tabuchi, T., Kitagawa, T., Yanagitai, M., Senzaki, M., Kosegawa, C., Taira, H., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07449.x · Cited by 63 · see citing works
Li, B., Li, X., Zhu, B., Zhang, X., Wang, Y., Xu, Y., Wang, H., Hou, Y., Zheng, Q., & Sun, G. (2011) · Environmental Toxicology · doi:10.1002/tox.20731 · Cited by 55 · see citing works
Ryu, K., Baker, R. T., & Kopito, R. R. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.03.038 · Cited by 54 · see citing works
Bianchi, M., Giacomini, E., Crinelli, R., Radici, L., Carloni, E., & Magnani, M. (2015) · Gene · doi:10.1016/j.gene.2015.07.030 · Cited by 52 · see citing works
Self-citationUbiquitin C gene: Structure, function, and transcriptional regulation
Radici, L., Bianchi, M., Crinelli, R., & Magnani, M. (2013) · Advances in Bioscience and Biotechnology · doi:10.4236/abb.2013.412141 · Cited by 49 · see citing works
Self-citationLu, M., Kim, H.-E., Li, C.-R., Kim, S., Kwak, I.-J., Lee, Y., Kim, S., Moon, J., Kim, C. H., Kim, D., et al. (2008) · Biochemistry · doi:10.1021/bi702185u · Cited by 47 · see citing works
Resveratrol fuels HER2 and ERα-positive breast cancer behaving as proteasome inhibitor
Andreani, C., Bartolacci, C., Wijnant, K., Crinelli, R., Bianchi, M., Magnani, M., Hysi, A., Iezzi, M., Amici, A. R. D., & Marchini, C. (2017) · Aging · doi:10.18632/aging.101175 · Cited by 47 · see citing works
Self-citationProteome Stability as a Key Factor of Genome Integrity
Gumeni, S., Evangelakou, Z., Gorgoulis, V. G., & Trougakos, I. P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102036 · Cited by 41 · see citing works
Khalil, S. E., Luciano, J. A., Chen, W., & Liu, A. Y. ‐. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20599 · Cited by 31 · see citing works
Kim, M.-N., Choi, J., Ryu, H.-W., & Ryu, K. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.02.010 · Cited by 30 · see citing works
Dastagir, K., Reimers, K., Lazaridis, A., Jahn, S., Maurer, V., Strauß, S., Dastagir, N., Radtke, C., Kampmann, A., Bucan, V., et al. (2014) · Cellular Reprogramming · doi:10.1089/cell.2014.0005 · Cited by 29 · see citing works
Crinelli, R., Bianchi, M., Menotta, M., Carloni, E., Giacomini, E., Pennati, M., & Magnani, M. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9864-8 · Cited by 28 · see citing works
Self-citationCrinelli, R., Bianchi, M., Radici, L., Carloni, E., Giacomini, E., & Magnani, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136882 · Cited by 22 · see citing works
Self-citationBianchi, M., Crinelli, R., Giacomini, E., Carloni, E., Radici, L., & Magnani, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065932 · Cited by 22 · see citing works
Self-citationRyu, H.-W., & Ryu, K. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.12.004 · Cited by 15 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Marsh, S. E., Walker, A. J., Kamath, T., Dissing-Olesen, L., Hammond, T. R., de Soysa, T. Y., Young, A. M. H., Murphy, S., Abdulraouf, A., Nadaf, N., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01022-8 · Cited by 432 · see citing works
Li, Y., Li, S., & Wu, H. (2022) · Cells · doi:10.3390/cells11050851 · Cited by 384 · see citing works
Endoplasmic reticulum stress-mediated mitochondrial dysfunction in aged hearts
Chen, Q., Samidurai, A., Thompson, J., Hu, Y., Das, A., Willard, B. B., & Lesnefsky, E. J. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165899 · Cited by 80 · see citing works
Deneweth, J., de Peer, Y. V., & Vermeirssen, V. (2022) · BMC Genomics · doi:10.1186/s12864-021-08215-8 · Cited by 62 · see citing works
Multiomic analyses uncover immunological signatures in acute and chronic coronary syndromes
Pekayvaz, K., Losert, C., Knottenberg, V., Gold, C., van Blokland, I. V., Oelen, R., Groot, H. E., Benjamins, J. W., Brambs, S., Kaiser, R. W. J., et al. (2024) · Nature Medicine · doi:10.1038/s41591-024-02953-4 · Cited by 59 · see citing works
Bianchi, M., Crinelli, R., Giacomini, E., Carloni, E., Radici, L., Scarpa, E. S., Tasini, F., & Magnani, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-54973-7 · Cited by 27 · see citing works
Self-citationModulation of the ubiquitin-proteasome system by marine natural products
Vasilopoulou, M. Α., Ioannou, E., Roussis, V., & Chondrogianni, N. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101897 · Cited by 27 · see citing works
Sha, Z., & Goldberg, A. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001323117 · Cited by 25 · see citing works
Tang, C., Border, J. J., Zhang, H., Gregory, A., Bai, S., Fang, X., Liu, Y., Wang, S., Hwang, S. H., Gao, W., et al. (2025) · GeroScience · doi:10.1007/s11357-025-01550-8 · Cited by 22 · see citing works
Scarpa, E. S., Tasini, F., Crinelli, R., Ceccarini, C., Magnani, M., & Bianchi, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155435 · Cited by 22 · see citing works
Self-citationRegulation of polyubiquitin genes to meet cellular ubiquitin requirement
Han, S.-W., Jung, B.-K., & Ryu, K. (2021) · BMB Reports · doi:10.5483/bmbrep.2021.54.4.005 · Cited by 23 · see citing works
Stress modulation as a means to improve yeasts for lignocellulose bioconversion
Brandt, B. A., Jansen, T., Volschenk, H., Görgens, J. F., van Zyl, W. H., & den Haan, R. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11383-y · Cited by 21 · see citing works
De novo sphingolipid biosynthesis necessitates detoxification in cancer cells
Spears, M. E., Lee, N., Hwang, S., Park, S. J., Carlisle, A. E., Li, R., Doshi, M. B., Armando, A. M., Gao, J., Simin, K. J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111415 · Cited by 20 · see citing works
Szebeni, G. J., Balog, J. Á., Demjén, A., Alföldi, R., Végi, V., Fehér, L. Z., Mán, I., Kotogány, E., Gubán, B., Batár, P., et al. (2018) · Molecules · doi:10.3390/molecules23112845 · Cited by 18 · see citing works
Zaman, M. S., BARMAN, S. K., Corley, S., Wilkins, M. R., Malladi, C. S., & Wu, M. J. (2021) · Metallomics · doi:10.1093/mtomcs/mfab026 · Cited by 17 · see citing works
Peter, R. M., Sarwar, M. S., Mostafa, S. Z., Wang, Y., Su, X., & Kong, A. T. (2023) · Molecular Carcinogenesis · doi:10.1002/mc.23551 · Cited by 16 · see citing works
Chromatin accessibility dynamics of Chlamydia-infected epithelial cells
Hayward, R. J., Marsh, J. W., Humphrys, M. S., Huston, W. M., & Myers, G. S. A. (2020) · Epigenetics & Chromatin · doi:10.1186/s13072-020-00368-2 · Cited by 13 · see citing works
Pan, N., Bhatti, M. Z., Zhang, W., Ni, B., Fan, X., & Chen, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-87680-3 · Cited by 13 · see citing works
Munno, C. D., Busiello, R. A., Calonne, J., Salzano, A. M., Miles-Chan, J. L., Scaloni, A., Ceccarelli, M., de Lange, P., Lombardi, A., Senese, R., et al. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.631176 · Cited by 12 · see citing works
Hashimoto, E., Okuno, S., Hirayama, S., Arata, Y., Goto, T., Kosako, H., Hamazaki, J., & Murata, S. (2020) · iScience · doi:10.1016/j.isci.2020.101299 · Cited by 11 · see citing works
Modulation of Orosomucoid-like Protein 3 Activity in the Management of Inflammatory Bowel Disease
Maličević, U., Rai, V., Škrbić, R., & Agrawal, D. K. (2024) · Journal of Biotechnology and Biomedicine · doi:10.26502/jbb.2642-91280167 · Cited by 9 · see citing works
Circadian clock crosstalks with autism
Yurdakul, E., Barlas, Y., & Ülgen, K. Ö. (2023) · Brain and Behavior · doi:10.1002/brb3.3273 · Cited by 6 · see citing works
Gubat, J., Sjöstrand, L., Selvaraju, K., Telli, K., & D’Arcy, P. (2024) · Scientific Reports · doi:10.1038/s41598-024-63791-5 · Cited by 4 · see citing works
Poloni, J. D. F., Rispoli, T., Rossetti, M. L. R., Trindade, C., & Vargas, J. E. (2021) · BioMed Research International · doi:10.1155/2021/5262000 · Cited by 4 · see citing works
Perumal, N., Yurugi, H., Dahm, K., Rajalingam, K., Grus, F. H., Pfeiffer, N., & Manicam, C. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128464 · Cited by 3 · see citing works
HSF1 in aging: The output selection model
Khatatneh, S., Sőti, C., & Somogyvári, M. (2026) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2026.112225 · Cited by 2 · see citing works
Pekayvaz, K., Losert, C., Knottenberg, V., van Blokland, I. V., Oelen, R., Groot, H. E., Benjamins, J. W., Brambs, S., Kaiser, R. W. J., Eivers, L., et al. (2023) · medRxiv · doi:10.1101/2023.05.02.23289392 · Cited by 2 · see citing works
Tsukamoto, Y., Nakamura, Y., Hirata, M., Okuzaki, D., Sakate, R., & Kimura, T. (2023) · FEBS Letters · doi:10.1002/1873-3468.14628 · Cited by 1 · see citing works
Faulconnier, Y., Pawłowski, K., Chambon, C., Durand, D., Pires, J., & Leroux, C. (2024) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2024.101326 · Cited by 1 · see citing works
Candida albicans -induced ubiquitination of EGFR reveals novel host–fungal interaction pathways
Lortal, L., Griffiths, J. S., Priest, E. L., Kempf, A., Paulin, O. K. A., Ponde, N. O., Tsavou, A., Wickramasinghe, D. N., Donkin, A. J., Lyon, C. M., et al. (2026) · mBio · doi:10.1128/mbio.03448-25 · Cited by 2 · see citing works
Garcia-Baucells, P., Bartra, C., Sarroca, S., Reinoite, F., Senserrich, J., Corpas, R., Griñán‐Ferré, C., & Sanfeliu, C. (2026) · Antioxidants · doi:10.3390/antiox15060698 · Cited by 1 · see citing works
Shokri, M. R., Tohidfar, M., & Moghaddam, S. (2023) · Research Square · doi:10.21203/rs.3.rs-2736473/v1
Systems genetics identifies the association between Enc1 and cognitive function in the hippocampusPreprint
He, H., Tao, R., Han, Z., Yin, Q., Pan, S., Lu, L., Bajpai, A. K., Mi, J., Qi, D., Li, H., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.23.563569
Guo, W., Ye, F., Hou, Z., & Pang, Q. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262210884
Additional file 7 of Chromatin accessibility dynamics of Chlamydia-infected epithelial cells
Hayward, R. J., Marsh, J. W., Humphrys, M. S., Huston, W. M., & Myers, G. S. A. (2020) · Figshare · doi:10.6084/m9.figshare.13151998
Additional file 2 of Chromatin accessibility dynamics of Chlamydia-infected epithelial cells
Hayward, R. J., Marsh, J. W., Humphrys, M. S., Huston, W. M., & Myers, G. S. A. (2020) · Figshare · doi:10.6084/m9.figshare.13151983
Additional file 4 of Chromatin accessibility dynamics of Chlamydia-infected epithelial cells
Hayward, R. J., Marsh, J. W., Humphrys, M. S., Huston, W. M., & Myers, G. S. A. (2020) · Figshare · doi:10.6084/m9.figshare.13151989
Sabo, A. R., Nanamatsu, A., Wischmeier, D., Gulbronson, C. J., Khan, S., Micanovic, R., Winfree, S., El‐Achkar, T. M., & LaFavers, K. A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.26.708299
Liu, Q., Xu, L., Deng, Z., Luan, Q., Han, X., & Yang, C. (2026) · Industrial Crops and Products · doi:10.1016/j.indcrop.2026.124429
An integrated resource for systems-level analysis of aging hallmarks and associated genes
Tiwari, R., Balaji, M., Chivukula, N., Sil, P., & Samal, A. (2026) · Biogerontology · doi:10.1007/s10522-026-10520-2
- Authors
- Bianchi, M., Crinelli, R., Arbore, V., & Magnani, M.
- Affiliations
- University of Urbino (IT)
- Corresponding author
- Bianchi, Marzia
- Venue
- FEBS Open Bio
- Publisher
- Wiley
- Published
- 2018-07-24
- Volume
- 8
- Issue
- 9
- Pages
- 1471-1485
- ISSN
- 2211-5463 (ISSN-L)
- PMC
- PMC6120222
- OpenAlex
- W2809815475
- Cited by
- 40
- References
- 56
- Citations by year
- 2026: 6 · 2025: 2 · 2024: 4 · 2023: 7 · 2022: 4 · 2021: 7 · 2020: 8 · 2019: 1 · 2018: 1
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- FEBS Open Bio (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- FanoAteneo and University of Urbino
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- heat shock factor 1, HSF2, heat shock element, Nrf2, arsenite, oxidative stress, proteotoxic stress, antioxidant response element, proteasome inhibition, MG132, stress response genes
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