Circadian- and UPR-dependent control of CPEB4 mediates a translational response to counteract hepatic steatosis under ER stress

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,893 · see citing works

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 5,120 · see citing works

Manipulating the mouse embryo: A laboratory manual

Hogan, B., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,467 · 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

Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., & Ron, D. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,871 · see citing works

Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress

Tabas, I. A., & Ron, D. (2011) · Nature Cell Biology · doi:10.1038/ncb0311-184 · Cited by 2,603 · see citing works

Chemical Chaperones Reduce ER Stress and Restore Glucose Homeostasis in a Mouse Model of Type 2 Diabetes

Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413 · see citing works

Manipulating the mouse embryo: A laboratory manual

Johnson, M. (1986) · Trends in Genetics · doi:10.1016/0168-9525(86)90275-1 · Cited by 2,259 · see citing works

Obesity and nonalcoholic fatty liver disease: biochemical, metabolic, and clinical implications

Fabbrini, E., Sullivan, S., & Klein, S. (2010) · Hepatology · doi:10.1002/hep.23280 · Cited by 2,100 · see citing works

Perk is essential for translational regulation and cell survival during the unfolded protein response

Harding, H. P., Zhang, Y., Bertolotti, A., Zeng, H., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80330-5 · Cited by 2,021 · see citing works

Molecular mediators of hepatic steatosis and liver injury

Browning, J. D., & Horton, J. D. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200422422 · Cited by 1,772 · see citing works

Reinitiation involving upstream ORFs regulates <i>ATF4</i> mRNA translation in mammalian cells

Vattem, K. M., & Wek, R. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400541101 · Cited by 1,696 · see citing works

Protein misfolding in the endoplasmic reticulum as a conduit to human disease

Wang, M., & Kaufman, R. J. (2016) · Nature · doi:10.1038/nature17041 · Cited by 1,630 · see citing works

Plasma cell differentiation requires the transcription factor XBP-1

Reimold, A., Iwakoshi, N., Manis, J., Vallabhajosyula, P., Szomolanyi-Tsuda, E., Gravallese, E., Friend, D., Grusby, M., Alt, F., & Glimcher, L. (2001) · Nature · doi:10.1038/35085509 · Cited by 1,371 · see citing works

Coping with stress: eIF2 kinases and translational control

Wek, R. C., Jiang, H.-Y., & Anthony, T. G. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340007 · Cited by 1,290 · see citing works

Contribution of de novo fatty acid synthesis to hepatic steatosis and insulin resistance: lessons from genetically engineered mice

Postic, C., & Girard, J. R. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34275 · Cited by 1,200 · see citing works

Orchestrating the unfolded protein response in health and disease

Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216886 · Cited by 1,015 · see citing works

NAFLD, NASH and liver cancer

Michelotti, G. A., Machado, M. V., & Diehl, A. M. (2013) · Nature Reviews Gastroenterology &amp; Hepatology · doi:10.1038/nrgastro.2013.183 · Cited by 974 · see citing works

Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins

Rutkowski, D. T., Arnold, S. M., Miller, C. N., Wu, J., Li, J., Gunnison, K. M., Mori, K., Akha, A. A. S., Raden, D. L., & Kaufman, R. J. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040374 · Cited by 804 · see citing works

Time of feeding and the intrinsic circadian clock drive rhythms in hepatic gene expression.

Vollmers, C., Gill, S., DiTacchio, L., Pulivarthy, S. R., Le, H. D., & Panda, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909591106 · Cited by 765 · see citing works

The BioMart community portal: an innovative alternative to large, centralized data repositories

Smedley, D., Haider, S., Durinck, S., Pandini, L., Provero, P., Allen, J., Arnaiz, O., Awedh, M. H., Baldock, R., Barbiera, G., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv350 · Cited by 755 · see citing works

UPR Pathways Combine to Prevent Hepatic Steatosis Caused by ER Stress-Mediated Suppression of Transcriptional Master Regulators

Rutkowski, D. T., Wu, J., Back, S.-H., Callaghan, M. U., Ferris, S. P., Iqbal, J., Clark, R. L., Miao, H. Z., Hassler, J. R., Fornek, J. L., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.10.015 · Cited by 580 · see citing works

ER Stress Cooperates with Hypernutrition to Trigger TNF-Dependent Spontaneous HCC Development

Nakagawa, H., Umemura, A., Taniguchi, K., Font-Burgada, J., Dhar, D., Ogata, H., Zhong, Z., Valasek, M. A., Seki, E., Hidalgo, J., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.07.001 · Cited by 525 · see citing works

Coping with stress: eIF2 kinases and translational control

Jiang, H.-Y., Wek, R. C., & Anthony, T. G. (2005) · Biochemical Society Transactions · doi:10.1042/bst20060007 · Cited by 522 · see citing works

A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging

Mohrin, M., Shin, J., Liu, Y., Brown, K., Luo, H., Xi, Y., Haynes, C. M., & Chen, D. (2015) · Science · doi:10.1126/science.aaa2361 · Cited by 490 · see citing works

The circadian clock and pathology of the ageing brain

Kondratova, A. A., & Kondratov, R. V. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3208 · Cited by 482 · see citing works

Inhibition of the sarcoplasmic reticulum Ca2+ transport ATPase by thapsigargin at subnanomolar concentrations

Sagara, Y., & Inesi, G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92726-2 · Cited by 455 · see citing works

Analysis of the role of microsomal triglyceride transfer protein in the liver of tissue-specific knockout mice

Raabe, M., Véniant, M. M., Sullivan, M. A., Zlot, C. H., Björkegren, J., Nielsen, L. B., Wong, J. S., Hamilton, R. L., & Young, S. G. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6576 · Cited by 424 · see citing works

A Combinatorial Code for CPE-Mediated Translational Control

Piqué, M., López, J. M., Foissac, S., Guigó, R., & Méndez, R. (2008) · Cell · doi:10.1016/j.cell.2007.12.038 · Cited by 386 · see citing works

Inhibition of apolipoprotein B100 secretion by lipid-induced hepatic endoplasmic reticulum stress in rodents

Ota, T., Gayet, C., & Ginsberg, H. N. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32752 · Cited by 376 · see citing works

Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA

Méndez, R., Hake, L. E., Andrésson, Þ., Littlepage, L. E., RUDERMAN, J. V., & Richter, J. D. (2000) · Nature · doi:10.1038/35005126 · Cited by 369 · see citing works

The unfolded protein response governs integrity of the haematopoietic stem-cell pool during stress

van Galen, P., Kreso, A., Mbong, N., Kent, D. G., Fitzmaurice, T., Chambers, J. E., Xie, S., Laurenti, E., Hermans, K., Eppert, K., et al. (2014) · Nature · doi:10.1038/nature13228 · Cited by 363 · see citing works

Circadian clock-dependent and -independent rhythmic proteomes implement distinct diurnal functions in mouse liver

Mauvoisin, D., Wang, J., Jouffe, C., Martin, E., Atger, F., Waridel, P., Quadroni, M., Gachon, F., & Naef, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314066111 · Cited by 329 · see citing works

Translational control by changes in poly(A) tail length: recycling mRNAs

Weill, L., Belloc, E., Bava, F.-A., & Méndez, R. (2012) · Nature Structural &amp; Molecular Biology · doi:10.1038/nsmb.2311 · Cited by 328 · see citing works

Discrete functions of nuclear receptor Rev-erbα couple metabolism to the clock

Zhang, Y., Fang, B., Emmett, M. J., Damle, M., Sun, Z., Feng, D., Armour, S. M., Remsberg, J. R., Jager, J., Soccio, R. E., et al. (2015) · Science · doi:10.1126/science.aab3021 · Cited by 321 · see citing works

Lipid-dependent regulation of the unfolded protein response

Volmer, R., & Ron, D. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.002 · Cited by 241 · see citing works

Quantitative profiling of initiating ribosomes in vivo

Gao, X., Wan, J., Liu, B., Ma, M., Shen, B., & Qian, S. (2014) · Nature Methods · doi:10.1038/nmeth.3208 · Cited by 238 · see citing works

Germ Cell Differentiation and Synaptonemal Complex Formation Are Disrupted in CPEB Knockout Mice

Tay, J., & Richter, J. D. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00025-9 · Cited by 231 · see citing works

Cytoplasmic Polyadenylation Element Binding Proteins in Development, Health, and Disease

Ivshina, M. P., Lasko, P. F., & Richter, J. D. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155831 · Cited by 223 · see citing works

Peroxisomal β-Oxidation and Steatohepatitis

Rao, M. S., & Reddy, J. K. (2001) · Seminars in Liver Disease · doi:10.1055/s-2001-12928 · Cited by 194 · see citing works

Neuralized1 Activates CPEB3: A Function for Nonproteolytic Ubiquitin in Synaptic Plasticity and Memory Storage

Pavlopoulos, E., Trifilieff, P., Chevaleyre, V., Fioriti, L., Zairis, S., Pagano, A., Malleret, G., & Kandel, E. R. (2011) · Cell · doi:10.1016/j.cell.2011.09.056 · Cited by 189 · see citing works

Circadian Clock-Coordinated 12 Hr Period Rhythmic Activation of the IRE1α Pathway Controls Lipid Metabolism in Mouse Liver

Cretenet, G., Clech, M. L., & Gachon, F. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2009.11.002 · Cited by 187 · see citing works

Effect of dietary fat content on the incidence of obesity among ad libitum fed mice.

Salmon, D. M., & Flatt, J. P. (1985) · PubMed · Cited by 187 · see citing works

Specificity of RNA Binding by CPEB: Requirement for RNA Recognition Motifs and a Novel Zinc Finger

Hake, L. E., Méndez, R., & Richter, J. D. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.685 · Cited by 170 · see citing works

Circadian control of mRNA polyadenylation dynamics regulates rhythmic protein expressionPreprint

Kojima, S., Sher-Chen, E. L., & Green, C. B. (2012) · Genes & Development · doi:10.1101/gad.208306.112 · Cited by 169 · see citing works

CPEB1 coordinates alternative 3′-UTR formation with translational regulation

Bava, F.-A., Eliscovich, C., Ferreira, P. G., Miñana, B., Ben-Dov, C., Guigó, R., Valcárcel, J., & Méndez, R. (2013) · Nature · doi:10.1038/nature11901 · Cited by 164 · see citing works

The CPEB-family of proteins, translational control in senescence and cancer

Fernández‐Miranda, G., & Méndez, R. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.03.004 · Cited by 151 · see citing works

Key contribution of CPEB4-mediated translational control to cancer progression

Zapater, E. O., Pineda, D., Martínez‐Bosch, N., Fernández‐Miranda, G., Iglesias, M., Alameda, F., Moreno, M., Eliscovich, C., Eyras, E., Real, F. X., et al. (2011) · Nature Medicine · doi:10.1038/nm.2540 · Cited by 149 · see citing works

CPEB regulation of human cellular senescence, energy metabolism, and p53 mRNA translation

Burns, D. M., & Richter, J. D. (2008) · Genes &amp; Development · doi:10.1101/gad.1697808 · Cited by 134 · see citing works

Lipolysis Response to Endoplasmic Reticulum Stress in Adipose Cells

Deng, J., Liu, S., Zou, L., Xu, C. B., Geng, B., & Xu, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.299115 · Cited by 122 · see citing works

SUMOylation Is an Inhibitory Constraint that Regulates the Prion-like Aggregation and Activity of CPEB3

Drisaldi, B., Colnaghi, L., Fioriti, L., Rao, N., Myers, C., Snyder, A. M., Metzger, D. J., Tarasoff, J., Konstantinov, E., Fraser, P. E., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.061 · Cited by 120 · see citing works

The Unfolded Protein Response Triggers Selective mRNA Release from the Endoplasmic Reticulum

Reid, D. W., Chen, Q., Tay, A. S. L., et al. (2014) · Cell · doi:10.1016/j.cell.2014.08.012 · Cited by 120 · see citing works

Integration of UPRER and Oxidative Stress Signaling in the Control of Intestinal Stem Cell Proliferation

Wang, L., Zeng, K. X., Ryoo, H. D., & Jasper, H. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004568 · Cited by 120 · see citing works

Meiosis requires a translational positive loop where CPEB1 ensues its replacement by CPEB4

Igea, A., & Méndez, R. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.111 · Cited by 116 · see citing works

A deadenylation negative feedback mechanism governs meiotic metaphase arrest

Belloc, E., & Méndez, R. (2008) · Nature · doi:10.1038/nature06809 · Cited by 111 · see citing works

ePAT: A simple method to tag adenylated RNA to measure poly(A)-tail length and other 3′ RACE applications

Jänicke, A., VanCuylenberg, J. B., Boag, P. R., Traven, A., & Beilharz, T. H. (2012) · RNA · doi:10.1261/rna.031898.111 · Cited by 109 · see citing works

A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteinsPreprint

Afroz, T., Skříšovská, L., Belloc, E., et al. (2014) · Genes & Development · doi:10.1101/gad.241133.114 · Cited by 91 · see citing works

Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic Expression of Vascular Endothelial Growth Factor and Angiogenesis in Chronic Liver Disease

Calderone, V., Gallego, J. G., Fernández‐Miranda, G., et al. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.11.038 · Cited by 87 · see citing works

CPEB4 is regulated during cell cycle by ERK2/Cdk1-mediated phosphorylation and its assembly into liquid-like droplets

Guillén‐Boixet, J., Buzón, V., Salvatella, X., et al. (2016) · eLife · doi:10.7554/elife.19298 · Cited by 69 · see citing works

htSeqTools: high-throughput sequencing quality control, processing and visualization in R

Planet, E., Attolini, C. S., Reina, Ó., et al. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr700 · Cited by 63 · see citing works

How does protein misfolding in the endoplasmic reticulum affect lipid metabolism in the liver?

Wang, S., & Kaufman, R. J. (2014) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000056 · Cited by 55 · see citing works

CPEB4 Is a Cell Survival Protein Retained in the Nucleus upon Ischemia or Endoplasmic Reticulum Calcium Depletion

Kan, M.-C., Oruganty-Das, A., Cooper-Morgan, A., Jin, G., Swanger, S. A., Bassell, G. J., Florman, H. M., van Leyen, K., & Richter, J. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00716-10 · Cited by 53 · see citing works

Cytoplasmic Polyadenylation Element Binding Protein Deficiency Stimulates PTEN and Stat3 mRNA Translation and Induces Hepatic Insulin Resistance

Alexandrov, I. M., Ivshina, M. P., Jung, D. Y., Friedline, R. H., Ko, H. J., Xu, M. F., O’Sullivan-Murphy, B., Bortell, R., Huang, Y., Urano, F., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002457 · Cited by 52 · see citing works

Cpeb4-Mediated Translational Regulatory Circuitry Controls Terminal Erythroid Differentiation

Hu, W., Yuan, B., & Lodish, H. F. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.07.008 · Cited by 51 · see citing works

Comprehensive translational control of tyrosine kinase expression by upstream open reading frames

Wethmar, K., Schulz, J. F., Muro, E. M., et al. (2015) · Oncogene · doi:10.1038/onc.2015.233 · Cited by 38 · see citing works

Changes in poly(A) tail length dynamics from the loss of the circadian deadenylase Nocturnin

Kojima, S., Gendreau, K. L., Sher-Chen, E. L., Gao, P., & Green, C. B. (2015) · Scientific Reports · doi:10.1038/srep17059 · Cited by 36 · see citing works

Comparative in Silico Analyses of Cpeb1–4 with Functional Predictions

Wang, X., & Cooper, N. G. F. (2010) · Bioinformatics and Biology Insights · doi:10.4137/bbi.s5087 · Cited by 35 · see citing works

Global Analysis of CPEBs Reveals Sequential and Non-Redundant Functions in Mitotic Cell Cycle

Giangarrà, V., Igea, A., Castellazzi, C. L., Bava, F.-A., & Méndez, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138794 · Cited by 34 · see citing works

Role and therapeutic potential of vascular stem/progenitor cells in pathological neovascularisation during chronic portal hypertension

García‐Pras, E., Gallego, J. G., Coch, L., et al. (2016) · Gut · doi:10.1136/gutjnl-2015-311157 · Cited by 15 · see citing works

Perturbed rhythmic activation of signaling pathways in mice deficient for Sterol Carrier Protein 2-dependent diurnal lipid transport and metabolism

Jouffe, C., Gobet, C., Martín, E., Métairon, S., Morin‐Rivron, D., Masoodi, M., & Gachon, F. (2016) · Scientific Reports · doi:10.1038/srep24631 · Cited by 12 · see citing works

The circadian clock and liver function in health and disease

Mukherji, A., Bailey, S. M., Staels, B., & Baumert, T. F. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.03.020 · Cited by 246 · see citing works

CPEB4 Increases Expression of PFKFB3 to Induce Glycolysis and Activate Mouse and Human Hepatic Stellate Cells, Promoting Liver Fibrosis.

Mejías, M., Gallego, J., Naranjo-Suárez, S., Ramírez, M., Pell, N., Manzano, A., Suñer, C., Bartrons, R., Méndez, R., & Fernandez, M. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.03.008 · Cited by 147 · see citing works

Homeostasis control in health and disease by the unfolded protein response

Acosta‐Alvear, D., Harnoss, J. M., Walter, P., & Ashkenazi, A. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00794-0 · Cited by 139 · see citing works

Spatial transcriptomics of healthy and fibrotic human liver at single-cell resolution

Watson, B. R., Paul, B., Rahman, R. U., Amir-Zilberstein, L., Segerstolpe, Å., Epstein, E. T., Murphy, S., Geistlinger, L., Lee, T., Shih, A., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55325-4 · Cited by 123 · see citing works

Antagonizing circRNA_002581–miR-122–CPEB1 axis alleviates NASH through restoring PTEN–AMPK–mTOR pathway regulated autophagy

Jin, X., Gao, J., Zheng, R.-H., Yu, M., Ren, Y., Yan, T.-L., Huang, Y., & Li, Y.-M. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2293-7 · Cited by 100 · see citing works

Clock mediates liver senescence by controlling ER stress

Yuan, G., Hua, B., Cai, T., Xu, L., Li, E., Huang, Y., Sun, N., Yan, Z., Lü, C., & Qian, R. (2017) · Aging · doi:10.18632/aging.101353 · Cited by 90 · see citing works

Paediatric fatty liver disease (PeFLD): All is not NAFLD – Pathophysiological insights and approach to management

Hegarty, R., Deheragoda, M. G., Fitzpatrick, E., & Dhawan, A. K. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.02.006 · Cited by 74 · see citing works

Metabolic Reprogramming of Liver Fibrosis

Delgado, M. E., Cárdenas, B., Farran, N., & Fernández, M. (2021) · Cells · doi:10.3390/cells10123604 · Cited by 73 · see citing works

Endoplasmic Reticulum Stress Signaling and the Pathogenesis of Hepatocarcinoma

Wei, J., & Fang, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041799 · Cited by 69 · see citing works

Identification of leukemia stem cell expression signatures through Monte Carlo feature selection strategy and support vector machine

Li, J., Lü, L., Zhang, Y., Xu, Y., Liu, M., Feng, K., Chen, L., Kong, X., Huang, T., & Cai, Y. (2019) · Cancer Gene Therapy · doi:10.1038/s41417-019-0105-y · Cited by 64 · see citing works

Central and peripheral circadian clocks and their role in Alzheimer's disease

Chauhan, R., Chen, K.-F., Kent, B. A., & Crowther, D. C. (2017) · Disease Models &amp; Mechanisms · doi:10.1242/dmm.030627 · Cited by 58 · see citing works

Deficiency of Mitochondrial Glycerol 3‐Phosphate Dehydrogenase Contributes to Hepatic Steatosis

Zheng, Y., Qu, H., Xiong, X., Wang, Y., Liu, X., Zhang, L., Liao, X., Liao, Q., Sun, Z., Ouyang, Q., et al. (2019) · Hepatology · doi:10.1002/hep.30507 · Cited by 61 · see citing works

The Biological Clock: A Pivotal Hub in Non-alcoholic Fatty Liver Disease Pathogenesis

Mazzoccoli, G., Cosmo, S. D., & Mazza, T. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00193 · Cited by 59 · see citing works

Interplay Between Macrophages and Angiogenesis: A Double-Edged Sword in Liver Disease

Ramírez-Pedraza, M., & Fernández, M. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02882 · Cited by 56 · see citing works

Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases

Liudkovska, V., & Dziembowski, A. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1622 · Cited by 51 · see citing works

Liver function and dysfunction – a unique window into the physiological reach of ER stress and the unfolded protein response

Rutkowski, D. T. (2018) · FEBS Journal · doi:10.1111/febs.14389 · Cited by 51 · see citing works

The role of CPEB family proteins in the nervous system function in the norm and pathology

Kozlov, E., Shidlovskii, Y. V., Gilmutdinov, R. A., Schedl, P. D., & Zhukova, M. V. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00577-6 · Cited by 46 · see citing works

CPEB3-mediated MTDH mRNA translational suppression restrains hepatocellular carcinoma progression

Zhang, H., Zou, C., Zou, C., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02984-y · Cited by 46 · see citing works

Tissue-specific mechanisms of fat metabolism that focus on insulin actions

Wu, S., Tan, J., Zhang, H., Hou, D., & He, J. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.12.009 · Cited by 43 · see citing works

Endoplasmic reticulum stress promotes sorafenib resistance via miR-188-5p/hnRNPA2B1-mediated upregulation of PKM2 in hepatocellular carcinoma

Zhou, B., Lu, D., Wang, A., Cui, J., Zhang, L., Li, J., Fan, L., Wei, W., Liu, J., & Sun, G. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.09.014 · Cited by 42 · see citing works

Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice

Lackey, A. I., Chen, T., Zhou, Y. X., Arias, N. M. B., Doran, J. M., Zacharisen, S. M., Gajda, A. M., Jonsson, W. O., Córsico, B., Anthony, T. G., et al. (2020) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00120.2019 · Cited by 39 · see citing works

Comparative analyses of vertebrate CPEB proteins define two subfamilies with coordinated yet distinct functions in post-transcriptional gene regulation

Duran-Arqué, B., Cañete, M., Castellazzi, C. L., Bartomeu, A., Ferrer-Caelles, A., Reina, Ó., Caballé, A., Gay, M., Arauz‐Garofalo, G., Belloc, E., et al. (2022) · Genome biology · doi:10.1186/s13059-022-02759-y · Cited by 35 · see citing works

Preservation of circadian rhythms by the protein folding chaperone, BiP

Pickard, A., Chang, J., Alachkar, N., Calverley, B. C., Garva, R., Arvan, P. R., Meng, Q., & Kadler, K. E. (2019) · The FASEB Journal · doi:10.1096/fj.201802366rr · Cited by 33 · see citing works

Restoration of CPEB4 prevents muscle stem cell senescence during aging

Zeng, W., Zhang, W., Tse, E. H. Y., Liu, J., Dong, A., Lam, K. S. W., Luan, S., Küng, W., Chan, T. C., & Cheung, T. H. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.05.012 · Cited by 34 · see citing works

Recent advances in signal integration mechanisms in the unfolded protein response

Karagöz, G., Aragón, T., & Acosta-Alvear, D. (2019) · F1000Research · doi:10.12688/f1000research.19848.1 · Cited by 25 · see citing works

The RNA binding protein CPEB2 regulates hormone sensing in mammary gland development and luminal breast cancer

Pascual, R., Martín, J., Salvador, F., Reina, Ó., Chanes, V., Millanes‐Romero, A., Suñer, C., Fernández‐Miranda, G., Bartomeu, A., Huang, Y., et al. (2020) · Science Advances · doi:10.1126/sciadv.aax3868 · Cited by 27 · see citing works

Subcellular delivery of lipid nanoparticles to endoplasmic reticulum and mitochondria

Shi, Y., Luo, Z., & You, J. (2022) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1803 · Cited by 29 · see citing works

Unfolded Protein Response Sensors in Hepatic Lipid Metabolism and Nonalcoholic Fatty Liver Disease

Henkel, A. S. (2018) · Seminars in Liver Disease · doi:10.1055/s-0038-1670677 · Cited by 26 · see citing works

Macrophage inflammation resolution requires CPEB4-directed offsetting of mRNA degradation

Suñer, C., Sibilio, A., Martín, J., et al. (2022) · eLife · doi:10.7554/elife.75873 · Cited by 24 · see citing works

Gut microbiota—a positive contributor in the process of intermittent fasting-mediated obesity control

Rong, B., Wu, Q., Saeed, M., & Sun, C. (2021) · Animal nutrition · doi:10.1016/j.aninu.2021.09.009 · Cited by 24 · see citing works

Role of endoplasmic reticulum stress in hepatic glucose and lipid metabolism and therapeutic strategies for metabolic liver disease

Zheng, W., Sun, Q., Li, L., Cheng, Y. H., Chen, Y., Lv, M., & Xiang, X. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109458 · Cited by 23 · see citing works

Antitumor T‐cell function requires CPEB4‐mediated adaptation to chronic endoplasmic reticulum stress

Fernández‐Alfara, M., Sibilio, A., Martín, J., Uxó, E. T., Malumbres, M., Alcalde, V., Chanes, V., Cañellas-Socias, A., Palomo‐Ponce, S., Batlle, E., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022111494 · Cited by 22 · see citing works

Foie gras and liver regeneration: a fat dilemma

Fazia, M. A. D., & Servillo, G. (2018) · Cell Stress · doi:10.15698/cst2018.07.144 · Cited by 21 · see citing works

Roles of the Translation Initiation Factor eIF2α Phosphorylation in Cell Structure and Function

Back, S. (2020) · Cell Structure and Function · doi:10.1247/csf.20013 · Cited by 19 · see citing works

Targeting the cytoplasmic polyadenylation element-binding protein CPEB4 protects against diet-induced obesity and microbiome dysbiosis

Pell, N., García‐Pras, E., Gallego, J. G., Naranjo‐Suarez, S., Balvey, A., Suñer, C., Fernández‐Alfara, M., Chanes, V., Carbo, J., Ramírez-Pedraza, M., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101388 · Cited by 20 · see citing works

Control of immediate early gene expression by CPEB4-repressor complex-mediated mRNA degradation

Poetz, F., Lebedeva, S., Schott, J., Lindner, D., Ohler, U., & Stoecklin, G. (2022) · Genome Biology · doi:10.1186/s13059-022-02760-5 · Cited by 19 · see citing works

Insights into the molecular mechanisms of malnutrition‐associated steatohepatitis: A review

Sharma, V., & Patial, V. (2024) · Liver International · doi:10.1111/liv.15932 · Cited by 20 · see citing works

Clock-dependent chromatin accessibility rhythms regulate circadian transcription

Yuan, Y., Chen, Q., Brovkina, M. V., Clowney, E. J., & Yadlapalli, S. (2024) · PLoS Genetics · doi:10.1371/journal.pgen.1011278 · Cited by 18 · see citing works

The role of endoplasmic reticulum stress in type 2 diabetes mellitus mechanisms and impact on islet function

He, Z., Liu, Q., Wang, Y., Zhao, B., Zhang, L., Yang, X. V., & Wang, Z. (2025) · PeerJ · doi:10.7717/peerj.19192 · Cited by 16 · see citing works

Recent Advances in Practical Methods for Liver Cell Biology: A Short Overview

Torres, S., Abdullah, Z., Brol, M. J., Hellerbrand, C., Fernández, M., Fiorotto, R., Klein, S., Königshofer, P., Liedtke, C., Lotersztajn, S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062027 · Cited by 16 · see citing works

Circadian Clock's Cancer Connections

Walton, Z. E., Altman, B. J., Brooks, R. C., & Dang, C. V. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030617-050216 · Cited by 15 · see citing works

Olfactory-Experience- and Developmental-Stage-Dependent Control of CPEB4 Regulates c-Fos mRNA Translation for Granule Cell Survival

Tseng, C.-S., Chao, H., Huang, H., & Huang, Y. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.100 · Cited by 15 · see citing works

A temporal hierarchy underpins the transcription factor–DNA interactome of the maize UPR

Ko, D. K., & Brandizzí, F. (2020) · The Plant Journal · doi:10.1111/tpj.15044 · Cited by 14 · see citing works

Immune translational control by CPEB4 regulates intestinal inflammation resolution and colorectal cancer development

Sibilio, A., Suñer, C., Fernández‐Alfara, M., Martín, J., Berenguer, A., Calon, A., Chanes, V., Millanes‐Romero, A., Fernández‐Miranda, G., Batlle, E., et al. (2022) · iScience · doi:10.1016/j.isci.2022.103790 · Cited by 14 · see citing works

Genetic loss-of-function of activating transcription factor 3 but not C-type lectin member 5A prevents diabetic peripheral neuropathy

Kan, H., Chang, C.-H., Chang, Y., Ko, Y.-T., & Hsieh, Y. (2021) · Laboratory Investigation · doi:10.1038/s41374-021-00630-5 · Cited by 14 · see citing works

The RNA-binding protein Cpeb4 is a novel positive regulator of osteoclast differentiation

Arasaki, Y., Li, M., Akiya, T., Nozawa, I., Ezura, Y., & Hayata, T. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.05.089 · Cited by 12 · see citing works

CPEB4 modulates liver cancer progression by translationally regulating hepcidin expression and sensitivity to ferroptosis

Delgado, M. E., Naranjo‐Suarez, S., Ramírez-Pedraza, M., Cárdenas, B., Gallardo-Martínez, C., Balvey, A., Belloc, E., Martín, J., Boyle, M., Méndez, R., et al. (2024) · JHEP Reports · doi:10.1016/j.jhepr.2024.101296 · Cited by 11 · see citing works

RNA-binding proteins in metabolic-associated fatty liver disease (MAFLD): From mechanism to therapy

Xu, J., Liu, X., Shu-qin, W., Zhang, D., Liu, X., Xia, P., Ling, J., Zheng, K., Xu, M., Shen, Y., et al. (2023) · BioScience Trends · doi:10.5582/bst.2022.01473 · Cited by 10 · see citing works

Translational Control in Liver Disease

Balvey, A., & Fernández, M. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.795298 · Cited by 10 · see citing works

Emerging roles of RNA‐binding proteins in fatty liver disease

Adesanya, O. A., Das, D., & Kalsotra, A. (2024) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1840 · Cited by 9 · see citing works

Cytoplasmic regulation of the poly(A) tail length as a potential therapeutic target

Fernández, M., & Mendez, R. (2025) · RNA · doi:10.1261/rna.080333.124 · Cited by 9 · see citing works

Circadian rhythms in metabolism and mental health: a reciprocal regulatory network with implications for metabolic and neuropsychiatric disorders

Lloyd, M., Prakash, B. A., Zhao, L., Ni, G., Ru, Y., & Vasudevan, S. R. (2025) · Current Opinion in Physiology · doi:10.1016/j.cophys.2025.100836 · Cited by 9 · see citing works

CPEB4 links the clock and the UPR to protect the liver

Moore, P. C., & Oakes, S. A. (2017) · Nature Cell Biology · doi:10.1038/ncb3460 · Cited by 7 · see citing works

CPEB4–CLOCK crosstalk during temporal lobe epilepsy

de Diego-García, L., Brennan, G. P., Auer, T., Menéndez‐Méndez, A., Parras, A., Martín‐Gil, A., Mitra, M., Ollà, I., Villalba‐Benito, L., Gil, B., et al. (2023) · Epilepsia · doi:10.1111/epi.17736 · Cited by 7 · see citing works

Pericytes in the Gut

Ramirez, M., Pell, N., Mejías, M., & Fernández, M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-11093-2_5 · Cited by 7 · see citing works

Identification of novel genes associated with exercise and calorie restriction effects in skeletal muscle

Kang, J. S., Kim, M. J., Kwon, E., Lee, K., Kim, C., Kwon, K., & Yang, Y. R. (2023) · Aging · doi:10.18632/aging.204793 · Cited by 5 · see citing works

Crosstalk Between Angiogenesis and Fibrogenesis in Liver Disease

Mejías, M., Balvey, A., & Fernández, M. (2020) · Current Tissue Microenvironment Reports · doi:10.1007/s43152-020-00013-w · Cited by 4 · see citing works

Rheb Promotes Triglyceride Secretion and Ameliorates Diet-Induced Steatosis in the Liver

Du, C., Yang, W., Yu, Z., Yuan, Q., Pang, D., Tang, P., Jiang, W., Chen, M., & Xiao, B. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.808140 · Cited by 4 · see citing works

Posttranscriptional reprogramming controls MASLD progression through chronic ER stress adaptation

Belloc, E., Calderone, V., Suárez, S. N., Mateo, L., Martín, J., Malizia, F., Sibilio, A., Chanes, V., Ramírez-Pedraza, M., Delgado, M. E., et al. (2026) · Science Advances · doi:10.1126/sciadv.aea4125 · Cited by 3 · see citing works

Sorafenib-associated translation reprogramming in hepatocellular carcinoma cells

Contreras, L., Rodríguez‐Gil, A., Muntané, J., et al. (2025) · RNA Biology · doi:10.1080/15476286.2025.2483484 · Cited by 3 · see citing works

mTOR signaling contributes to system-driven rhythmic gene expression in mouse liver

Sahasrabudhe, A., Guy, C. R., Jacq, A., Ho, C.-W., Greenwell, B. J., & Menet, J. S. (2026) · Science Advances · doi:10.1126/sciadv.aec0131 · Cited by 3 · see citing works

Melatonin Reduces Apoptosis Resistance of Hepatocellular Carcinoma Cells by Inhibiting BMAL1

Wang, A., Zhou, B., Zhu, Y., et al. (2022) · Integrative Cancer Therapies · doi:10.1177/15347354221099539 · Cited by 2 · see citing works

Mammalian Cis-Acting RNA Sequence Elements

Louis, I. V.-S., & Sagarsky, C. (2018) · InTech eBooks · doi:10.5772/intechopen.72124 · Cited by 2 · see citing works

miR-363-5p regulates liver disease via the MAPK/ERK signaling pathway by targeting CPEB2 in chicken

Xiang, J., Jia, B., Luo, Z., He, H., Zhang, Y., Cui, C., Yin, H., Han, S., & Liu, C. (2025) · Poultry Science · doi:10.1016/j.psj.2025.105660 · Cited by 1 · see citing works

DETERMINATION OF THE CIRCADIAN OSCILLATION PATTERN OF UNFOLDED PROTEIN RESPONSE SIGNALING COMPONENTS IN HUMAN EMBRYONIC KIDNEY HEK293 CELLS

Erzurumlu, Y., Doğan, H. K., & Çataklı, D. (2024) · Ankara Universitesi Eczacilik Fakultesi Dergisi · doi:10.33483/jfpau.1487169 · Cited by 1 · see citing works

PERK links the clock and protein stress in cancer

Sánchez‐Álvarez, M., & Bakal, C. (2017) · Nature Cell Biology · doi:10.1038/s41556-017-0019-6 · Cited by 1 · see citing works

Pathological Angiogenesis: The New Culprit behind Chronic Liver Disease

Ramirez, M., & Fernández, M. (2019) · OBM Hepatology and Gastroenterology · doi:10.21926/obm.hg.1903030 · Cited by 1 · see citing works

Modelling non-alcoholic fatty liver disease using patient derived liver stem cells and hepatic organoids

Lim, Y. S. (2019) · doi:10.32657/10356/139651

Review of roles of RNA-binding proteins on NAFLD and the related pharmaceutical measures

Li, C., Yang, F., Yuan, Z., & Wei, X. (2025) · Biomolecules and Biomedicine · doi:10.17305/bb.2025.12465

Applications of Multifractal Detrended Fluctuation Analysis

Dai, D., Hu, Y., Qian, H., et al. (2023) · Journal of Information and Computing Science · doi:10.4208/jics-2023-006

Hepatocyte FAM210A deficiency disrupts mitochondrial function and triggers juvenile steatosis with compensatory repair in adulthood

Wang, Y., Chu, L., Zhou, Y., Jin, Z., Kim, K., Heiden, K. D., Monreal, M. A. G., Ren, J., Li, Y., Cheng, Z., et al. (2026) · Communications Biology · doi:10.1038/s42003-026-10769-w

Additional file 2 of Control of immediate early gene expression by CPEB4-repressor complex-mediated mRNA degradation

Poetz, F., Lebedeva, S., Schott, J., Lindner, D., Ohler, U., & Stoecklin, G. (2022) · Figshare · doi:10.6084/m9.figshare.21087353

Additional file 1 of Comparative analyses of vertebrate CPEB proteins define two subfamilies with coordinated yet distinct functions in post-transcriptional gene regulation

Duran-Arqué, B., Cañete, M., Castellazzi, C. L., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21087563

Additional file 14 of Control of immediate early gene expression by CPEB4-repressor complex-mediated mRNA degradation

Poetz, F., Lebedeva, S., Schott, J., Lindner, D., Ohler, U., & Stoecklin, G. (2022) · Figshare · doi:10.6084/m9.figshare.21087347

Additional file 3 of Comparative analyses of vertebrate CPEB proteins define two subfamilies with coordinated yet distinct functions in post-transcriptional gene regulation

Duran-Arqué, B., Cañete, M., Castellazzi, C. L., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21087572

Additional file 4 of Comparative analyses of vertebrate CPEB proteins define two subfamilies with coordinated yet distinct functions in post-transcriptional gene regulation

Duran-Arqué, B., Cañete, M., Castellazzi, C. L., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21087575

Stress-Induced Down-Regulation of CPEB4 Disrupts Sodium Channel Regulation and Myocardial Excitability

Kang, G.-J., Kim, E., Xie, A., et al. (2026) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2026.101514

CPEB4 deficiency promotes vasculogenic mimicry and resistance to anti-angiogenic therapy in hepatocellular carcinoma

Cárdenas, B., Suárez, S. N., Baroja, I., Mendez, A., Bosch-i-Crespo, P., Gallardo-Martínez, C., Ramírez-Pedraza, M., Delgado, M. E., Morató, L., Belloc, E., et al. (2026) · Gut · doi:10.1136/gutjnl-2026-338325

Aging-associated loss of CPEB4 impairs mitochondrial adaptation and promotes stress-induced senescence in alveolar type II cells

Li, X., Fu, Z., Sun, D., Jin, Z., & Jiao, H. (2026) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2026.112258

Polystyrene nanoplastics perturb macrophage mitochondrial homeostasis and inflammatory responses: Evidence implicating CPEB4

Li, X., Yu, X., Zhang, S., Han, L., & Liu, Y. (2026) · Environmental Pollution · doi:10.1016/j.envpol.2026.129326

Endoplasmic Reticulum Stress in Hearing Loss

Wang, Y., Liu, X., & Xu, Z. (2017) · Journal of Otorhinolaryngology Hearing and Balance Medicine · doi:10.3390/ohbm1010003 · Cited by 3 · see citing works

Endoplasmic reticulum stress in health and disease

Zhao, L., & Ackerman, S. L. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.005 · Cited by 440 · see citing works

Endoplasmic reticulum stress and pancreatic β-cell death

Fonseca, S. G., Gromada, J., & Urano, F. (2011) · Trends in Endocrinology &amp; Metabolism · doi:10.1016/j.tem.2011.02.008 · Cited by 384 · see citing works

Endoplasmic reticulum and unfolded protein response

Wang, H. (2010) · Zhonghua zhongliu fangzhi zazhi

Endoplasmic Reticulum Stress-Related Inflammation and Cardiovascular Diseases

Gotoh, T., Endo, M., & Oike, Y. (2011) · International Journal of Inflammation · doi:10.4061/2011/259462 · Cited by 96 · see citing works