XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351

Autophagy in the Pathogenesis of Disease

Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069

Autophagy fights disease through cellular self-digestion

Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452

Signal integration in the endoplasmic reticulum unfolded protein response

Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,431

Autophagy and Viruses: Adversaries or Allies?

Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,444

Guidelines for the use and interpretation of assays for monitoring autophagy

Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996

Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882

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

Interactions Between Autophagy and the Unfolded Protein Response: Implications for Inflammatory Bowel Disease

Hooper, K. M., Barlow, P. G., Henderson, P., & Stevens, C. (2018) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izy380 · Cited by 39

How autophagy can restore proteostasis defects in multiple diseases?

Joshi, V., Upadhyay, A., Prajapati, V. K., & Mishra, A. (2020) · Medicinal Research Reviews · doi:10.1002/med.21662 · Cited by 40

The Enemy within: Innate Surveillance-Mediated Cell Death, the Common Mechanism of Neurodegenerative Disease

Richards, R. I., Robertson, S. A., O’Keefe, L. V., Fornarino, D. L., Scott, A., Lardelli, M. T., & Baune, B. T. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00193 · Cited by 39

Protein clearing pathways in ALS.

Ferrucci, M., Fulceri, F., Toti, L., Soldani, P., Siciliano, G., Paparelli, A., & Fornai, F. (2011) · PubMed · doi:10.4449/aib.v149i1.1258 · Cited by 35

ER stress signaling and neurodegeneration: At the intersection between Alzheimer's disease and Prion-related disorders

Torres, M., Matamala, J. M., Duran-Aniotz, C. A., Cornejo, V. H., Foley, A., & Hetz, C. A. (2014) · Virus Research · doi:10.1016/j.virusres.2014.12.018 · Cited by 39

Control of systemic proteostasis by the nervous system.

Mardones, P., Martínez, G., & Hetz, C. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.08.001 · Cited by 35

ER proteostasis disturbances in Parkinson's disease: novel insights

Mercado, G., Castillo, V., Vidal, R. L., & Hetz, C. A. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00039 · Cited by 35

Gene therapy to target ER stress in brain diseases

Valenzuela, V., Martínez, G., Duran-Aniotz, C. A., & Hetz, C. A. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.064 · Cited by 36

Melatonin Can Modulate Neurodegenerative Diseases by Regulating Endoplasmic Reticulum Stress

Yoo, Y., & Joo, S. S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032381 · Cited by 35

Autophagy and UPR in alpha-crystallin mutant knock-in mouse models of hereditary cataracts

Andley, U. P., & Goldman, J. W. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.06.001 · Cited by 34

Protein recycling pathways in neurodegenerative diseases

Fecto, F., Esengul, Y. T., & Siddique, T. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt243 · Cited by 34

3,4‐dihydroxybenzalacetone and caffeic acid phenethyl ester induce preconditioning ER stress and autophagy in SH‐SY5Y cells

Tomiyama, R., Takakura, K., Takatou, S., Le, T. M., Nishiuchi, T., Nakamura, Y., Konishi, T., Matsugo, S., & Hori, O. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26080 · Cited by 34

Network approach identifies Pacer as an autophagy protein involved in ALS pathogenesis

Beltrán, S., Nassif, M., Vicencio, E., Arcos, J., Labrador, L., Cortés, B. I., Cortéz, C., Bergmann, C. A., Espinoza, S., Hernandez, M. F., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0313-9 · Cited by 35

CIDeR: multifactorial interaction networks in human diseases

Lechner, M., Höhn, V., Brauner, B., Dunger-Kaltenbach, I., Fobo, G., Frishman, G., Montrone, C., Kastenmüller, G., Wägele, B., & Ruepp, A. (2012) · Genome biology · doi:10.1186/gb-2012-13-7-r62 · Cited by 32

Role of the unfolded protein response in the development of central nervous system

Murao, N., & Nishitoh, H. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx047 · Cited by 35

Retinal Damage in Amyotrophic Lateral Sclerosis: Underlying Mechanisms

Soldatov, V. O., Kukharsky, M. S., Белых, А. Е., Sobolev, A., & Deykin, A. V. (2021) · Eye and Brain · doi:10.2147/eb.s299423 · Cited by 35

The Role and Therapeutic Potential of the Integrated Stress Response in Amyotrophic Lateral Sclerosis

Marlin, E., Viu-Idocin, C., Arrasate, M., & Aragón, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147823 · Cited by 32

Acinar cell injury induced by inadequate unfolded protein response in acute pancreatitis

Barrera, K., Stanek, A., Okochi, K., Niewiadomska, Z., Mueller, C. M., Ou, P., John, D. G., Alfonso, A. E., Tenner, S. M., & Huan, C. (2018) · World Journal of Gastrointestinal Pathophysiology · doi:10.4291/wjgp.v9.i2.37 · Cited by 32

Protein Misfolding and Aggregation: The Relatedness between Parkinson’s Disease and Hepatic Endoplasmic Reticulum Storage Disorders

Padilla-Godínez, F. J., Ramos-Acevedo, R., Martínez-Becerril, H. A., Bernal-Conde, L. D., Garrido-Figueroa, J. F., Hiriart, M., Hernández-López, A., Argüero‐Sánchez, R., Callea, F., & Guerra‐Crespo, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212467 · Cited by 33

Sigma-1 Receptor is a Pharmacological Target to Promote Neuroprotection in the SOD1G93A ALS Mice

Gaja-Capdevila, N., Hernández, N., Navarro, X., & Herrando-Grabulosa, M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.780588 · Cited by 32

Inhibition of Excessive Oxidative Protein Folding Is Protective in MPP + Toxicity-Induced Parkinson's Disease Models

Lehtonen, Š., Jaronen, M., Vehviläinen, P., Lakso, M., Rudgalvyte, M., Keksa-Goldsteine, V., Wong, G., Courtney, M. J., Koıstınaho, J., & Goldsteins, G. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6402 · Cited by 32

Mst‐1 deficiency promotes post‐traumatic spinal motor neuron survival via enhancement of autophagy flux

Zhang, M., Tao, W., Yuan, Z., & Liu, Y. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14154 · Cited by 26

Neurotoxic Astrocytes Directly Converted from Sporadic and Familial ALS Patient Fibroblasts Reveal Signature Diversities and miR-146a Theragnostic Potential in Specific Subtypes

Gomes, C., Sequeira, C., Likhite, S. B., Dennys, C. N., Kolb, S. J., Shaw, P. J., Vaz, A. R., Kaspar, B. K., Meyer, K., & Brites, D. M. T. O. (2022) · Cells · doi:10.3390/cells11071186 · Cited by 32

Notch pathway is activated in cell culture and mouse models of mutant SOD1-related familial amyotrophic lateral sclerosis, with suppression of its activation as an additional mechanism of neuroprotection for lithium and valproate

Wang, S., Ren, M., Jiang, H., Wang, J., Jiang, H.-Q., Yin, X. L., Qi, Y., Wang, X.-D., Dong, G.-T., Wang, T., et al. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.06.002 · Cited by 34

Mechanisms of disordered neurodegenerative function: concepts and facts about the different roles of the protein kinase RNA-like endoplasmic reticulum kinase (PERK)

Taalab, Y. M., Ibrahim, N., Maher, A., Hassan, M., Mohamed, W. M. Y., Moustafa, A. A., Salama, M., Johar, D., & Bernstein, L. H. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0071 · Cited by 30

Unspliced XBP1 controls autophagy through FoxO1

Vidal, R. L., & Hetz, C. A. (2013) · Cell Research · doi:10.1038/cr.2013.9 · Cited by 30

Crosstalk of Autophagy and the Secretory Pathway and Its Role in Diseases

Zahoor, M., & Farhan, H. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2017.12.004 · Cited by 29

Impaired Autophagy in Motor Neurons: A Final Common Mechanism of Injury and Death

Porras, M. A. G., Sieck, G. C., & Mantilla, C. B. (2018) · Physiology · doi:10.1152/physiol.00008.2018 · Cited by 31

Spinal Muscular Atrophy autophagy profile is tissue-dependent: differential regulation between muscle and motoneurons

Sansa, A., Hidalgo, I. A., Miralles, M. P., de la Fuente, S., Pérez‐García, M. J., Munell, F., Soler, R. M., & Garcerá, A. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01223-5 · Cited by 31

The transrepression arm of glucocorticoid receptor signaling is protective in mutant huntingtin-mediated neurodegeneration

Varadarajan, S., Breda, C., Smalley, J. L., Butterworth, M., Farrow, S. N., Giorgini, F., & Cohen, G. M. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.1 · Cited by 29

Ultrastructural features of aberrant glial cells isolated from the spinal cord of paralytic rats expressing the amyotrophic lateral sclerosis-linked SOD1G93A mutation

Jiménez, M., Díaz‐Amarilla, P., Isasi, E., Casanova, G., Barbeito, L., & Olivera‐Bravo, S. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2681-1 · Cited by 34

Evidence Linking Protein Misfolding to Quality Control in Progressive Neurodegenerative Diseases

Kabir, M. T., Uddin, M. S., Abdeen, A., Ashraf, G. M., Perveen, A., Hafeez, A., Bin-Jumah, M. N., & Abdel‐Daim, M. M. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200618114924 · Cited by 29

Exosomes derived from microglia overexpressing miR-124-3p alleviate neuronal endoplasmic reticulum stress damage after repetitive mild traumatic brain injury

Wang, Y., Li, D., Zhang, L., Yin, Z., Han, Z., Ge, X., Li, M., Zhao, J. T., Zhang, S., Zuo, Y., et al. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.391189 · Cited by 28

Effects of Cellular Pathway Disturbances on Misfolded Superoxide Dismutase-1 in Fibroblasts Derived from ALS Patients

Keskin, I., Forsgren, E., Lange, D. J., Weber, M., Birve, A., Synofzik, M., Gilthorpe, J. D., Andersen, P. M., & Marklund, S. L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0150133 · Cited by 29

Novel interactions of GRP78: UPR and estrogen responses in the brain

Ávila-Rodriguez, M., Cabezas, R., Torrente, D., González, J., Morales, L., Alvarez, L., Capani, F., & Barreto, G. E. (2013) · Cell Biology International · doi:10.1002/cbin.10058 · Cited by 28

A comparison of in vitro properties of resting SOD1 transgenic microglia reveals evidence of reduced neuroprotective function

Sargsyan, S. A., Blackburn, D. J., Barber, S. C., Großkreutz, J., Vos, K. J. D., Monk, P. N., & Shaw, P. J. (2011) · BMC Neuroscience · doi:10.1186/1471-2202-12-91 · Cited by 28

Amyotrophic Lateral Sclerosis Pathogenesis Converges on Defects in Protein Homeostasis Associated with TDP-43 Mislocalization and Proteasome-Mediated Degradation Overload

Lin, G., Mao, D., & Bellen, H. J. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.004 · Cited by 29

Fine-Tuning ER Stress Signal Transducers to Treat Amyotrophic Lateral Sclerosis

Medinas, D. B., González, J. V., Falcón, P., & Hetz, C. A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00216 · Cited by 27

The Role of IRE1 Signaling in the Central Nervous System Diseases

Ni, H., Rui, Q., Li, D., Gao, R., & Chen, G. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180416094646 · Cited by 27

Intracellular Citrate/acetyl-CoA flux and endoplasmic reticulum acetylation: Connectivity is the answer

Fernandez-Fuente, G., Rigby, M. J., & Puglielli, L. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101653 · Cited by 30

Cell-type specific variation in the induction of ER stress and downstream events in chikungunya virus infection

Khongwichit, S., Wikan, N., Abere, B., Thepparit, C., Kuadkitkan, A., Ubol, S., & Smith, D. R. (2016) · Microbial Pathogenesis · doi:10.1016/j.micpath.2016.11.009 · Cited by 27

PERK prevents rhodopsin degradation during retinitis pigmentosa by inhibiting IRE1-induced autophagy

Zhao, N., Li, N., & Wang, T. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202208147 · Cited by 27

ALS genetic modifiers that increase survival of SOD1 mice and are suitable for therapeutic development

Riboldi, G. M., Nizzardo, M., Simone, C., Falcone, M., Bresolin, N., Comi, G. P., & Corti, S. P. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.07.009 · Cited by 26

Sleep, Aging, and Cellular Health: Aged-Related Changes in Sleep and Protein Homeostasis Converge in Neurodegenerative Diseases

Hafycz, J. M., & Naidoo, N. N. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00140 · Cited by 28

Time-Point Dependent Activation of Autophagy and the UPS in SOD1G93A Mice Skeletal Muscle

Oliván, S., Calvo, A. C., Gasco, S., Muñoz, M. J., Zaragoza, P., & Osta, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134830 · Cited by 27

Chaperone-Dependent Mechanisms as a Pharmacological Target for Neuroprotection

Воронин, М. В., Абрамова, Е. В., Verbovaya, E. R., Vakhitova, Y. V., & Середенин, С. Б. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010823 · Cited by 27

Food restriction-induced autophagy modulates degradation of mutant SOD1 in an amyotrophic lateral sclerosis mouse model

Zhang, K., Shi, P., An, T., Wang, Q., Wang, J., Li, Z., Duan, W., Li, C., & Guo, Y. (2013) · Brain Research · doi:10.1016/j.brainres.2013.04.050 · Cited by 25

Inositol-requiring enzyme 1 alpha endoribonuclease specific inhibitor STF-083010 protects the liver from thioacetamide-induced oxidative stress, inflammation and injury by triggering hepatocyte autophagy

Zhan, F., Zhao, G., Li, X., Yang, S., Yang, W., Zhou, S., & Zhang, F. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.04.051 · Cited by 26

Deficiency of hepatocystin induces autophagy through an mTOR-dependent pathway

Yang, J. H., Zhao, Y., Ma, K., Jiang, F.-J., Liao, W., Zhang, P., Zhou, J., Tu, B., Wang, L., Kampinga, H. H., et al. (2011) · Autophagy · doi:10.4161/auto.7.7.15822 · Cited by 25

Endoplasmic reticulum stress: A key player in immune cell regulation and autoimmune disorders.

Moreews, M., & Karlsson, M. C. I. (2025) · Seminars in Immunology · doi:10.1016/j.smim.2025.101954 · Cited by 20

Inhibition of Cytohesins Protects against Genetic Models of Motor Neuron Disease

Zhai, J., Zhang, L., Mojsilovic‐Petrovic, J., Jian, X., Thomas, J., Homma, K., Schmitz, A., Famulok, M., Ichijo, H., Argon, Y., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5032-13.2015 · Cited by 24

The Role of PERK in Understanding Development of Neurodegenerative Diseases

Smedley, G. D., Walker, K. E., & Yuan, S. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158146 · Cited by 27

Neuroprotective Effect of a Multistrain Probiotic Mixture in SOD1G93A Mice by Reducing SOD1 Aggregation and Targeting the Microbiota-Gut-Brain Axis

Xin, Z., Xin, C., Huo, J., Liu, Q., Dong, H., Li, R., & Liu, Y. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-03988-x · Cited by 26

A Novel Interaction Between Aging and ER Overload in a Protein Conformational Dementia

Schipanski, A., Lange, S., Segref, A., Gutschmidt, A., Lomas, D. A., Miranda, E., Schweizer, M., Hoppe, T., & Glatzel, M. (2013) · Genetics · doi:10.1534/genetics.112.149088 · Cited by 24

The pathogenic human Torsin A in Drosophila activates the unfolded protein response and increases susceptibility to oxidative stress

Kim, A., Seo, J. B., Kim, W., Choi, H. J., Kim, S.-Y., Morrow, G., Tanguay, R. M., Steller, H., & Koh, Y. H. (2015) · BMC Genomics · doi:10.1186/s12864-015-1518-0 · Cited by 24

Tissue‐selective regulation of protein homeostasis and unfolded protein response signalling in sporadic ALS

Montibeller, L., Tan, L. Y., Kim, J. K., Paul, P., & de Belleroche, J. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15170 · Cited by 22

Autophagy in Acute Pancreatitis: Organelle Interaction and microRNA Regulation

Yuan, X., Wu, J., Guo, X., Li, W., Luo, C., Li, S., Wang, B., Tang, L., & Sun, H. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8811935 · Cited by 23

Comparison and contrast of plant, yeast, and mammalian ER stress and UPR

Chakraborty, R., Baek, J. H., Bae, E. Y., Kim, W., Lee, S. Y., & Kim, M. G. (2016) · Applied Biological Chemistry · doi:10.1007/s13765-016-0167-6 · Cited by 22

Novel prosurvival function of Yip1A in human cervical cancer cells: constitutive activation of the IRE1 and PERK pathways of the unfolded protein response

Taguchi, Y., Horiuchi, Y., Kano, F., & Murata, M. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.147 · Cited by 24

Meta-analysis of Genetic Modifiers Reveals Candidate Dysregulated Pathways in Amyotrophic Lateral Sclerosis

Yanagi, K. S., Wu, Z. J., Amaya, J., Chapkis, N., Duffy, A., Hajdarovic, K. H., Held, A., Mathur, A. D., Russo, K., Ryan, V. H., et al. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.10.033 · Cited by 22

α-Mangostin Reduced ER Stress-mediated Tumor Growth through Autophagy Activation

Kim, S., Hong, E., Lee, B., Park, M. H., Kim, J., Pyun, A.-R., Kim, Y., Chang, S., Chin, Y., & Ko, H. (2012) · Immune Network · doi:10.4110/in.2012.12.6.253 · Cited by 23

Signaling the Unfolded Protein Response in primary brain cancers

Reste, P. L., Avril, T., Quillien, V., Morandi, X., & Chevet, É. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.015 · Cited by 21

Cell Death-Autophagy Loop and Glutamate-Glutamine Cycle in Amyotrophic Lateral Sclerosis

Yuan, S., Zhang, Z.-W., & Li, Z.-L. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00231 · Cited by 21

IRE1α deficiency promotes tumor cell death and eIF2α degradation through PERK dipendent autophagy

Storniolo, A., Alfano, V., Carbotta, S., Ferretti, E., & Renzo, L. D. (2018) · Cell Death Discovery · doi:10.1038/s41420-017-0002-9 · Cited by 21

In a search for efficient treatment for amyotrophic lateral sclerosis: Old drugs for new approaches

Kukharsky, M. S., Skvortsova, V. I., Бачурин, С. О., & Buchman, V. L. (2020) · Medicinal Research Reviews · doi:10.1002/med.21725 · Cited by 21

The neuroprotective effects of activated α7 nicotinic acetylcholine receptor against mutant copper–zinc superoxide dismutase 1-mediated toxicity

Ito, T., Inden, M., Ueda, T., Asaka, Y., Kurita, H., & Hozumi, I. (2020) · Scientific Reports · doi:10.1038/s41598-020-79189-y · Cited by 23

Protein disulfide isomerase ERp57 protects early muscle denervation in experimental ALS

Rozas, P., Pinto, C., Traub, F. M., Dı́az, R., Pérez, V., Becerra, D., Ojeda, P., Ojeda, J., Wright, M. T., Mella, J., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01116-z · Cited by 21

Endoplasmic reticulum acetyltransferases Atase1 and Atase2 differentially regulate reticulophagy, macroautophagy and cellular acetyl-CoA metabolism

Rigby, M. J., Lawton, A. J., Kaur, G., Banduseela, V. C., Kamm, W. E., Lakkaraju, A., Denu, J. M., & Puglielli, L. (2021) · Communications Biology · doi:10.1038/s42003-021-01992-8 · Cited by 20

Autophagic Organelles in DNA Damage Response

Kim, J., Lee, S.-M., Kim, H., Lee, H., Seong, K. M., Youn, H., & Youn, B. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.668735 · Cited by 21

Protein Disulfide Isomerase and the Endoplasmic Reticulum in Amyotrophic Lateral Sclerosis

Walker, A. K. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0408-10.2010 · Cited by 21

A highly sensitive assay of IRE1 activity using the small luciferase NanoLuc: Evaluation of ALS-related genetic and pathological factors

Hikiji, T., Norisada, J., Hirata, Y., Okuda, K., Nagasawa, H., Ishigaki, S., Sobue, G., Kiuchi, K., & Oh‐hashi, K. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.05.132 · Cited by 20

Inhibition of Endoplasmic Reticulum Associated Degradation Reduces Endoplasmic Reticulum Stress and Alters Lysosomal Morphology and Distribution

Elfrink, H. L., Zwart, R., Baas, F., & Scheper, W. (2013) · Molecules and Cells · doi:10.1007/s10059-013-2286-9 · Cited by 20

Mechanisms of Neuroprotection by Protein Disulphide Isomerase in Amyotrophic Lateral Sclerosis

Walker, A. K., & Atkin, J. D. (2011) · Neurology Research International · doi:10.1155/2011/317340 · Cited by 19

Immune regulation of the unfolded protein response at the mucosal barrier in viral infection

Wang, R., Moniruzzaman, M., Shuffle, E. M., Lourie, R., & Hasnain, S. Z. (2018) · Clinical & Translational Immunology · doi:10.1002/cti2.1014 · Cited by 18

Selected terpenoids from medicinal plants modulate endoplasmic reticulum stress in metabolic disorders

Beukes, N., Levendal, R., & Frost, C. L. (2014) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12267 · Cited by 19

Principles of brain aging: Status and challenges of modeling human molecular changes in mice

Kluever, V., & Fornasiero, E. F. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101465 · Cited by 18

Are Sigma Receptor Modulators a Weapon Against Multiple Sclerosis Disease?

Collina, S., Rui, M., Stotani, S., Bignardi, E., Rossi, D., Curti, D., Giordanetto, F., Malacrida, A., Scuteri, A., & Cavaletti, G. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0122 · Cited by 17

Targeting EDEM protects against ER stress and improves development and survival in C. elegans

Ghenea, S., Chiritoiu‐Butnaru, M., Tăcutu, R., Miranda‐Vizuete, A., & Petrescu, S. M. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010069 · Cited by 19

Unraveling the role of motoneuron autophagy in ALS

Valenzuela, V., Nassif, M., & Hetz, C. A. (2018) · Autophagy · doi:10.1080/15548627.2018.1432327 · Cited by 17

The cyclic phosphodiesterase CNP and RNA cyclase RtcA fine-tune noncanonical XBP1 splicing during ER stress

Ünlü, I., Lu, Y., & Wang, X. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004872 · Cited by 17

Endocannabinoids and amyotrophic lateral sclerosis

de Lago, E., Moreno‐Martet, M., Espejo‐Porras, F., & Fernández‐Ruíz, J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-417041-4.00005-9 · Cited by 17

Expression analysis of protein homeostasis pathways in the peripheral blood mononuclear cells of sporadic amyotrophic lateral sclerosis patients

Vats, K., Gourie‐Devi, M., Ahuja, K., Sharma, A., Wajid, S., Ganguly, N. K., & Taneja, V. (2018) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2018.01.035 · Cited by 18

Animal Models in the Study of the Unfolded Protein Response

Bommiasamy, H., & Popko, B. (2011) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-385928-0.00006-7 · Cited by 17

Beneficial effect of ER stress preconditioning in protection against FFA-induced adipocyte inflammation via XBP1 in 3T3-L1 adipocytes

Wang, M., Chen, X., Zheng, Z., Yu, S., Zhou, B., Liu, Y., Liu, D., Chen, Y., & Qian, X. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03627-3 · Cited by 16

Small heterodimer partner (SHP) aggravates ER stress in Parkinson’s disease-linked LRRK2 mutant astrocyte by regulating XBP1 SUMOylation

Lee, J. H., Han, J., Joe, E.-H., & Jou, I. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00747-1 · Cited by 17

Hypoxia causes autophagic stress and derangement of metabolic adaptation in a cell model of amyotrophic lateral sclerosis

Cimini, S., Rizzardini, M., Biella, G., & Cantoni, L. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12642 · Cited by 18

Natural Compounds Play Therapeutic Roles in Various Human Pathologies via Regulating Endoplasmic Reticulum Pathway

Ma, R., Ni, Z., Thakur, K., Zhang, F., Zhang, Y., Zhang, J., & Wei, Z. (2020) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2020.100065 · Cited by 16

Essential roles of the unfolded protein response in intestinal physiology

Hetz, C. A., Silva-Agüero, J. F., & Ellerby, L. (2024) · eGastroenterology · doi:10.1136/egastro-2024-100129 · Cited by 17

Oligomannose-Type Glycan Processing in the Endoplasmic Reticulum and Its Importance in Misfolding Diseases

Kuribara, T., & Totani, K. (2022) · Biology · doi:10.3390/biology11020199 · Cited by 14

Activation of XBP1s attenuates disease severity in models of proteotoxic Charcot–Marie–Tooth type 1B

Touvier, T., Veneri, F. A., Claessens, A., Ferri, C., Mastrangelo, R., Sorgiati, N., Bianchi, F., Valenzano, S., Carro, U. D., Rivellini, C., et al. (2024) · Brain · doi:10.1093/brain/awae407 · Cited by 15

Autophagy meets fused in sarcoma-positive stress granules

Matus, S., Bosco, D. A., & Hetz, C. A. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.08.019 · Cited by 15

Rab-dependent cellular trafficking and amyotrophic lateral sclerosis

Parakh, S., Perri, E. R., Jagaraj, C. J., Ragagnin, A., & Atkin, J. D. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1553926 · Cited by 15

Crosstalk between protein misfolding and endoplasmic reticulum stress during ageing and their role in age-related disorders

Hemagirri, M., Chen, Y., Gopinath, S. C. B., Sahreen, S., Adnan, M., & Sasidharan, S. (2023) · Biochimie · doi:10.1016/j.biochi.2023.10.019 · Cited by 15

Autophagy in spinal muscular atrophy: from pathogenic mechanisms to therapeutic approaches

Rashid, S., & Dimitriadi, M. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1307636 · Cited by 17

Modulation of Autophagy-Like Processes by Tumor Viruses

Mack, H. I. D., & Münger, K. (2012) · Cells · doi:10.3390/cells1030204 · Cited by 14

Endoplasmic reticulum stress intolerance in EIF2B3 mutant oligodendrocytes is modulated by depressed autophagy

Chen, N., Dai, L., Jiang, Y., Wang, J., Hao, H.-J., Ren, Y., Leng, X., Zang, L., & Wu, Y. (2015) · Brain and Development · doi:10.1016/j.braindev.2015.11.002 · Cited by 14

ER chaperones in neurodegenerative disease: Folding and beyond

García-Huerta, P., Bargsted, L., Rivas, A., Matus, S., & Vidal, R. L. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.070 · Cited by 14

A Molecular Reporter for Monitoring Autophagic Flux in Nervous System In Vivo

Castillo, K., Valenzuela, V., Oñate, M., & Hetz, C. A. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.077 · Cited by 15

The functions of IRE1α in neurodegenerative diseases: Beyond ER stress.

Chen, L., Bi, M.-X., Zhang, Z., Du, X.-X., Chen, X., Jiao, Q., & Jiang, H. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101774 · Cited by 13

Candidate Genes That Affect Aging Through Protein Homeostasis

Argon, Y., & Gidalevitz, T. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-2404-2_2 · Cited by 13

XBP-1 deficiency in the nervous system reveals a homeostatic switch to activate autophagy

Matus, S., Nassif, M., Glimcher, L. H., & Hetz, C. A. (2009) · Autophagy · doi:10.4161/auto.5.8.10247 · Cited by 43

Corrigendum: XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagyPreprint

Hetz, C. A., Thielen, P., Matus, S., Nassif, M., Court, F. A., Kiffin, R., Martínez, G., Cuervo, A. M., Brown, R. H., & Glimcher, L. H. (2024) · Genes & Development · doi:10.1101/gad.352249.124 · Cited by 1

Autophagy for the avoidance of neurodegenerationPreprint

Madeo, F., Eisenberg, T., & Kroemer, G. (2009) · Genes & Development · doi:10.1101/gad.1858009 · Cited by 97

The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)

Crippa, V., Sau, D., Rusmini, P., Boncoraglio, A., Onesto, E., Bolzoni, E., Galbiati, M., Fontana, E., Marino, M., Carra, S., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq257 · Cited by 330

Artificial enforcement of the unfolded protein response reduces disease features in multiple preclinical models of ALS/FTD

Valenzuela, V., Becerra, D., Astorga, J. I., Fuentealba, M., Diaz, G., Bargsted, L., Chacón, C., Martinez, A. N., Gozalvo, R., Jackson, K. L., et al. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.01.004 · Cited by 11