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

Alzheimer’s disease pathology and the unfolded protein response: prospective pathways and therapeutic targets

Koss, D. J., & Platt, B. (2017) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000299 · Cited by 12

Disrupted endoplasmic reticulum-mediated autophagosomal biogenesis in a Drosophila model of C9-ALS-FTD

Sung, H., & Lloyd, T. E. (2023) · Autophagy · doi:10.1080/15548627.2023.2249750 · Cited by 11

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

Prolonged endoplasmic reticulum stress promotes mislocalization of immunoglobulins to the cytoplasm

Drori, A., Misaghi, S., Haimovich, J., Messerle, M., & Tirosh, B. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.03.006 · Cited by 11

Small GSK-3 Inhibitor Shows Efficacy in a Motor Neuron Disease Murine Model Modulating Autophagy

de Munck, E., Palomo, V., Muñoz‐Sáez, E., Pérez, D. I., Miguel, B. G., Solas, M. T., Gil, C., Martínez, A., & Arahuetes, R. M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0162723 · Cited by 11

Autophagy at the crossroads of metabolism and cellular defense

Begun, J., & Xavier, R. J. (2013) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e328365d34d · Cited by 10

Unconventional Protein Secretion in Brain Tumors Biology: Enlightening the Mechanisms for Tumor Survival and Progression

Iglesia, R. P., Prado, M. B., Alves, R. N., Melo-Escobar, M. I., Fernandes, C. F. D. L., Fortes, A. C. D. S., Souza, M. C. D. S., Boccacino, J. M., Cangiano, G., Soares, S. R., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.907423 · Cited by 11

The Emerging Role of the Major Histocompatibility Complex Class I in Amyotrophic Lateral Sclerosis

Chiarotto, G. B., Nardo, G., Trolese, M. C., França, M. C., Bendotti, C., & de Oliveira, A. L. R. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112298 · Cited by 10

Homeostatic interplay between FoxO proteins and ER proteostasis in cancer and other diseases

González-Quiroz, M., Urra, H., Limia, C. M., & Hetz, C. A. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.01.011 · Cited by 11

Dual role of IRE1α-XBP1 signaling in neurodegenerative diseases.

Wang, C.-L., Chang, Y., Zhu, J.-H., Ma, R., & Li, G. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.10.014 · Cited by 9

A panel of macroautophagy markers in lymphomonocytes of patients with amyotrophic lateral sclerosis

Sala, G., Tremolizzo, L., Melchionda, L., Stefanoni, G., Derosa, M., Susani, E. L., Pagani, A., Perini, M., Pettini, P., Tavernelli, F., et al. (2011) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482968.2011.611139 · Cited by 10

Are Proteinopathy and Oxidative Stress Two Sides of the Same Coin?

Mehta, N. J., Marwah, P. K., & Njus, D. (2019) · Cells · doi:10.3390/cells8010059 · Cited by 10

Muscle-specific lack of Gfpt1 triggers ER stress to alleviate misfolded protein accumulation

Zhang, R., Farshadyeganeh, P., Ohkawara, B., Nakajima, K., Takeda, J., Ito, M., Zhang, S., Miyasaka, Y., Ohno, T., Mori‐Yoshimura, M., et al. (2024) · Disease Models & Mechanisms · doi:10.1242/dmm.050768 · Cited by 9

Edaravone mitigates TDP-43 mislocalization in human amyotrophic lateral sclerosis neurons with potential implication of the SIRT1-XBP1 pathway

Mikuriya, S., Takegawa-Araki, T., & Tamura, M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.01.012 · Cited by 9

Future therapeutical strategies dictated by pre-clinical evidence in ALS.

Fornai, F., Meininger, V., & Silani, V. (2011) · PubMed · doi:10.4449/aib.v149i1.1269 · Cited by 9

ATase inhibition rescues age-associated proteotoxicity of the secretory pathway

Murie, M., Peng, Y., Rigby, M. J., Dieterich, I. A., Farrugia, M. A., Endresen, A., Bhattacharyya, A., & Puglielli, L. (2022) · Communications Biology · doi:10.1038/s42003-022-03118-0 · Cited by 9

An Overview of Potential Targets for Treating Amyotrophic Lateral Sclerosis and Huntington’s Disease

de Paula, C. Z., Gonçalves, B. D. C., & Vieira, L. B. (2015) · BioMed Research International · doi:10.1155/2015/198612 · Cited by 8

The mTOR Signaling Pathway in Neurodegenerative Diseases

Francois, A., Vérité, J., Bilan, A. R., Janet, T., Calon, F., Fauconneau, B., Paccalin, M., & Page, G. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802733-2.00011-6 · Cited by 8

PERK modulation, with GSK2606414, Sephin1 or salubrinal, failed to produce therapeutic benefits in the SOD1G93A mouse model of ALS

Vieira, F. G., Tassinari, V. R., Kidd, J. D., Moreno, A., Thompson, K., Perrin, S., Gill, A., & Hatzipetros, T. (2024) · PLoS ONE · doi:10.1371/journal.pone.0292190 · Cited by 8

Effect of Denervation on XBP1 in Skeletal Muscle and the Neuromuscular Junction

Walter, L. A., Blake, L. P., Gallot, Y. S., Arends, C. J., Sozio, R. S., Onifer, S. M., & Bohnert, K. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010169 · Cited by 7

Protein Homeostasis Dysregulation in Pathogenesis of Neurodegenerative Diseases

Kukharsky, M. S., Everett, M. W., Lytkina, O. A., Raspopova, M. A., Kovrazhkina, E. A., Овчинников, Р. К., Antohin, A., & Московцев, А. А. (2022) · Molecular Biology · doi:10.1134/s0026893322060115 · Cited by 6

Targeting endoplasmic reticulum acetylation to restore proteostasis in Alzheimer’s disease

Duran-Aniotz, C. A., Cornejo, V. H., & Hetz, C. A. (2016) · Brain · doi:10.1093/brain/awv401 · Cited by 7

Protective effects of long-term lithium administration in a slowly progressive SMA mouse model

Biagioni, Ferrucci, M., & Ryskailn, L. (2018) · ARCHIVES ITALIENNES DE BIOLOGIE · doi:10.12871/00039829201749 · Cited by 9

Emerging perspectives in proteostasis: bridging mechanisms and therapeutics for human diseases

Borlepawar, A., Neu, M., Ma, Z., Deshpande, A., Bühringer, H., Hajieva, P., Frey, N., & Rangrez, A. Y. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02714-4 · Cited by 7

C/EBP Homologous Protein Expression in Retinal Ganglion Cells Induces Neurodegeneration in Mice

Mayhew, W., Kaipa, B. R., Li, L., Maddineni, P., Sundaresan, Y., Clark, A. F., & Zode, G. S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26051858 · Cited by 6

Autophagy in motor neuron diseases

Rodríguez‐Muela, N. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.03.009 · Cited by 7

Is there a relationship between early pregnancy loss and maternal serum human X-box binding protein 1 level?

Uzun, A., & Atılgan, A. E. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.110451 · Cited by 5

Disruption of Endoplasmic Reticulum Proteostasis in Age-Related Nervous System Disorders

Medinas, D. B., Hazari, Y., & Hetz, C. A. (2021) · Progress in molecular and subcellular biology · doi:10.1007/978-3-030-67696-4_12 · Cited by 7

Endoplasmic reticulum stress is involved in retinal injury induced by repeated transient spikes of intraocular pressure

Yang, X., Yu, X., Zhao, Z., He, Y., Zhang, J., Su, X., Sun, N., & Fan, Z. (2021) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2100053 · Cited by 6

Emerging drug targets in amyotrophic lateral sclerosis

Bova, M. P., & Kinney, G. G. (2012) · Expert Opinion on Orphan Drugs · doi:10.1080/21678707.2013.744949 · Cited by 6

Autophagy Activation Is Involved in Acidic Fibroblast Growth Factor Ameliorating Parkinson’s Disease via Regulating Tribbles Homologue 3

Zhong, X., Wang, B., Zhang, G., Yuan, Y., Hu, X., Xiong, J., Zheng, P., Liu, Y., Xu, K., Xiao, J., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01428 · Cited by 6

Intrinsically accelerated cellular degradation is amplified by TDP-43 loss in ALS-vulnerable motor neurons in a zebrafish model

Asakawa, K., Tomita, T., Shioya, S., Handa, H., Saeki, Y., & Kawakami, K. (2025) · Nature Communications · doi:10.1038/s41467-025-65097-0 · Cited by 5

A KO mouse model for the lncRNA Lhx1os produces motor neuron alterations and locomotor impairment

Pellegrini, F., Padovano, V., Biscarini, S., Santini, T., Setti, A., Galfrè, S. G., Silenzi, V., Vitiello, E., Mariani, D., Nicoletti, C., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105891 · Cited by 5

Roflupram alleviates autophagy defects and reduces mutant hSOD1-induced motor neuron damage in cell and mouse models of amyotrophic lateral sclerosis

Huo, D., Liang, W., Wang, D., Liu, Q., Wang, H., Wang, Y., Zhang, C., Cong, C., Su, X., Tan, X., et al. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109812 · Cited by 5

Endoplasmic reticulum, oxidative stress and their complex crosstalk in neurodegeneration: proteostasis, signaling pathways and molecular chaperones

Ambrosi, G., Milani, P., & 2 383 King Street, 9. S. F. (2017) · AIMS molecular science · doi:10.3934/molsci.2017.4.424 · Cited by 5

Amyotrophic lateral sclerosis: mechanisms and therapeutic strategies

Bosch, L. V. D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805120-7.00011-7 · Cited by 5

Beclin1 decreases the RIPA-insoluble fraction of amyotrophic lateral sclerosis-linked SOD1 mutant via autophagy

Wei, Y., & Han, B. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.10.025 · Cited by 5

CDNF rescues motor neurons in three animal models of ALS by targeting ER stressPreprint

Lorenzo, F. D., Lüningschrör, P., Nam, J. H., Pilotto, F., Galli, E., Lindholm, P., von Collenberg, C. R., Mungwa, S. T., Jablonka, S., Kauder, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.05.078618 · Cited by 5

The Role of mTOR in Amyotrophic Lateral Sclerosis

Nogueira-Machado, J. A., Rocha-Silva, F., & Gomes, N. A. (2025) · Biomedicines · doi:10.3390/biomedicines13040952 · Cited by 4

Interplay between autophagy, the unfolded protein response and the cytoplasmic heat stress response during heat stress in maize

Tang, J., Jayasinghe, V., Li, Z., & Bassham, D. C. (2025) · BMC Plant Biology · doi:10.1186/s12870-025-07736-8 · Cited by 4

Repaglinide Induces ATF6 Processing and Neuroprotection in Transgenic SOD1G93A Mice

Gonzalo‐Gobernado, R., Moreno‐Martínez, L., González, P., Dopazo, X. M., Calvo, A. C., GUEVARA, I. P.-L. D., Seisdedos, E., Díaz-Muñoz, R., Mellström, B., Osta, R., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115783 · Cited by 6

Dual Role of Autophagy in Neurodegenerative Diseases: The Case of Amyotrophic Lateral Sclerosis

Bargsted, L., Vidal, R. L., Hetz, C. A., & Matus, S. (2015) · Current topics in neurotoxicity · doi:10.1007/978-3-319-13939-5_4 · Cited by 4

Multiple Routes of Motor Neuron Degeneration in ALS

Hee, J., & Keun, J. S. (2013) · InTech eBooks · doi:10.5772/56625 · Cited by 5

ALS sensitive spinal motor neurons enter a degenerative downward spiral of impaired splicing and proteostasisPreprint

Iannitelli, D. E., Tan, A., Nguyen, E., Babu, A., Elorza, S. D., Joseph, T., Zaaijer, S., An, D., Ward, M. E., & Mazzoni, E. O. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.26.485939 · Cited by 5

GABRA1 frameshift variants impair GABA A receptor proteostasisPreprint

Williams, M. P., Wang, Y., Kang, J., Perryman, J. H., & Mu, T.-W. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.28.625971 · Cited by 4

Assays to Study IRE1 Activation and Signaling.

Moraga, P., Aravena, R., Urra, H., & Hetz, C. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1732-8_10 · Cited by 3

Restoration of pancreatic beta cell identity and autophagy in KATP-induced diabetes by intermittent fasting

Castelblanco, E., Shyr, Z. A., SOTERO, I. R., Yan, Z., Chen, S. X., Diwan, A., & Remedi, M. S. (2025) · Diabetologia · doi:10.1007/s00125-025-06545-w · Cited by 3

Expression of protein disulfide isomerase A3Q481K variant associated with amyotrophic lateral sclerosis triggers disease features in mice

Sepulveda, M., Traub, F. M., Ojeda, P., Perez, V., Ojeda, J., Mella, J., Dı́az, R., Rozas, P., Mansilla-Jaramillo, M., Zuleta, A., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106947 · Cited by 3

Therapeutic potential of insulin-like growth factor 2 in Huntington’s disease: controlling proteostasis to alleviate the load of misfolded protein

Hetz, C. A., Vidal, R. L., & Troncoso-Escudero, P. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.303020 · Cited by 3

Molecular Mechanisms Underlying the Role of Autophagy in Neurodegenerative Diseases

Ahmad, S. T., & Lee, J.-A. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-405530-8.00003-0 · Cited by 3

Life-or-Death Decisions upon Axonal Damage

Roselli, F., & Caroni, P. (2012) · Neuron · doi:10.1016/j.neuron.2012.01.009 · Cited by 3

Roles of Endoplasmic Reticulum Stress in Neurodegenerative Diseases

Wang, S. K. H. (2012) · Translational Medicine · doi:10.4172/2161-1025.1000e108 · Cited by 3

Potential Therapeutic Use of Withania somnifera for Treatment of Amyotrophic Lateral Sclerosis

Dutta, K., Swarup, V., & Julien, J. (2017) · Springer eBooks · doi:10.1007/978-3-319-59192-6_19 · Cited by 3

Non-cell autonomous autophagy in amyotrophic lateral sclerosis: A new promising target?

Rosso, F., Magdalena, R., Torazza, C., Bacchetti, F., Milanese, M., Poletti, A., Bonanno, G., Cristofani, R., & Bonifacino, T. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107203 · Cited by 5

Dual targeting of the UPS and autophagy as a novel therapy for neurodegenerative proteinopathies

Lines, G., Helley, M., Gillotin, S., Brownlees, J., Duce, J., & Smethurst, P. (2026) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2026.1738415 · Cited by 2

The endoplasmic reticulum unfolded protein response and neurodegeneration

Ron, D. (2012) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-27928-7_2 · Cited by 2

Acetyl-CoA and acetylation in biology and disease

Puglielli, L., Rigby, M. J., & Fernandez-Fuente, G. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95582-9.00009-7 · Cited by 2

Effect of miR-98/IL-6/STAT3 on Autophagy and Apoptosis of Cardiac Stem Cells Under Hypoxic Conditions In vitro

Li, X., Zhang, Y., & Zhang, G. (2024) · Current Stem Cell Research & Therapy · doi:10.2174/011574888x294637240517050849 · Cited by 2

The Role of the Integrated Stress Response (ISR) in Neuropsychiatric Disorders

Ilyin, N. P., Nikitin, V. S., & Kalueff, A. V. (2024) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s002209302406005x · Cited by 2

Inhibition of Salt‐Inducible Kinase 2 Protects Motor Neurons From Degeneration in ALS by Activating Autophagic Flux and Enhancing mTORC1 Activity

Liang, W., Zhang, C., Wang, D., Su, X., Tan, X., Yang, Y., Cong, C., Wang, Y., Huo, D., Wang, H., et al. (2025) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70341 · Cited by 2

The Neuroprotective and Therapeutic Effects of Anthocyanins and Their Metabolites In Vitro and in a Mouse Model of Amyotrophic Lateral Sclerosis

Winter, A. N. (2016) · Digital Commons - DU (University of Denver) · Cited by 2

Contribution of Aberrant Astrocytes to Motor Neuron Damage and Death in the SOD1G93A Rat Experimental Model of ALS

Damianovich, G. O., Parada, O. C., Díaz‐Amarilla, P., Isasi, E., Pereira, C. I. B., & Olivera‐Bravo, S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.84695 · Cited by 2

Sigma Receptors as New Target for Multiple Sclerosis

Rui, M., Rossino, G., Rossi, D., & Collina, S. (2019) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016070-00264 · Cited by 2

Expression of amyotrophic lateral sclerosis associated protein disulfide isomerase A3 D217N variant recapitulates early morphological alterations at the neuromuscular junction

Sepulveda, M., Traub, F. M., Ojeda, P., Mella, J., Ojeda, J., Pinto, C., Dı́az, R., Rozas, P., Sepúlveda, C., Kerr, B., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107045 · Cited by 1

Exercise impact on IRE1α signaling: Novel insights into Alzheimer's disease prevention and treatment

Haixia, T., & Bo, X. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.153156 · Cited by 1

Bioinformatic Analyses of the Ataxin-2 Family Since Algae Emphasize Its Small Isoforms, Large Chimerisms, and the Importance of Human Exon 1B as Target of Therapies to Prevent Neurodegeneration

Auburger, G. W. J., Key, J., Gispert, S., Lastres‐Becker, I., Almaguer-Mederos, L.-E., Bassa, C., Auburger, A., Auburger, G. W. J., Arsović, A., Deller, T., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27031499 · Cited by 2

Cellular Responses to Flavivirus Infections: Stress Signaling at the Crossroads of Host Defense and Virus Infection

Badu, P., González, E. T. C., & Pager, C. T. (2026) · Viruses · doi:10.3390/v18070748 · Cited by 1

Krüppel-like factor 6 involvement in the endoplasmic reticulum homeostasis of extravillous trophoblasts

Kourdova, L. T., Miranda, A. L., Ovejero, M., Anastasía, A., Genti‐Raimondi, S., Racca, A. C., & Panzetta-Dutari, G. M. (2024) · Placenta · doi:10.1016/j.placenta.2024.08.002 · Cited by 1

Endoplasmic Reticulum Stress and Protein Misfolding in Neurodegenerative Diseases

Samaddar, S., Redhwan, M. A. M., & Eraiah, M. M. (2025) · Springer eBooks · doi:10.1007/978-981-96-6202-9_15 · Cited by 1

Physiological ER Stress: The Model of Insulin-Secreting Pancreatic b-Cells

Bensellam, M., Gilon, P., & Jonas, J. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_8 · Cited by 1

ER Stress in Intestinal Inflammatory Disease

Tomczak, M. F., Kaser, A., & Blumberg, R. S. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_12 · Cited by 1

Functional clustering of splice-altering variants in whole genome sequencing data reveals hidden heritability in rare variant disorderPreprint

Wang, Y., van Dijk, C., Timpanaro, I. S., Hop, P. J., Kenna, B., Kooyman, M., Aronica, E., Pasterkamp, R. J., van den Berg, L. H., Cooper‐Knock, J., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.30.542855 · Cited by 1

When the Good Turns Bad

Nassif, M., Medinas, D. B., Castillo, K., Gherardelli, C., & Hetz, C. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801033-4.00017-5

Protein Degradation in Neurodegeneration: The Ubiquitin Pathway

Bedford, L., Layfield, R., Rezvani, N., Paine, S., Lowe, J. S., & Mayer, R. J. (2011) · Wiley eBooks · doi:10.1002/9781444341256.ch5

The Identification of Novel Mechanisms in Neuronal Development and Degeneration

Jablonski, A. M. (2015) · ScholarlyCommons (University of Pennsylvania)

Targeting Protein Quality Control Pathways in Spinal and Bulbar Muscular Atrophy

Wang, A. M. (2012) · Deep Blue (University of Michigan)

Neural repair: basic cellular and molecular processes

Selzer, M. E., Clarke, S., Cohen, L. G., Kwakkel, G., & Miller, R. H. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511995583.020

Dissection of Prosurvival and Apoptotic Signalling By Human IRE1α

Fenech, E. J. (2014) · Durham e-Theses (Durham University)

The Unfolded Protein Response and Therapeutic Opportunities

Sayers, C. M., Dey, S., Lehman, S. L., & Koumenis, C. (2013) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-1-4614-9167-5_10

CSSI workshop in Brazil highlights “Stress Responses in the Nervous System” in relation to neurodegenerative diseases and neuroprotection

Brown, I. R. (2012) · Cell Stress and Chaperones · doi:10.1007/s12192-012-0366-y

Developing Human Stem Cell Derived Motor Neuron Models of Amyotrophic Lateral Sclerosis

Sandoe, J. (2014) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)

Laurie Glimcher: Merging cell biology and immune function

Sedwick, C. E. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.1892pi

The role of microRNAs during endoplasmic reticulum stress induced cell death

Cawley, K. (2012) · Arrow@dit (Dublin Institute of Technology) · doi:10.13025/17487

The Role of the Endoplasmic Reticulum Stress Transducer Ire1 during Photoreceptor Differentiation in Drosophila

Coelho, D. S. (2013) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

RAB24 ja GOSR1-proteiinien vuorovaikutus ja rooli autofagiassa

Viljanen, S. (2015) · Työväentutkimus Vuosikirja

Reprint of: 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.2016.06.021

Physiological Role of Autophagy and Implications in Disease

Karanasios, E., & Ktistakis, N. T. (2016) · Springer eBooks · doi:10.1007/978-3-319-33145-4_5

AUTOPHAGY IN AMYOTROPHIC LATERAL SCLEROSIS

Gál, J., & Zhu, H. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0009

The role of ALS associated genes and c-Jun in neurodegeneration

Acosta‐Saltos, A. (2016) · UCL Discovery (University College London)

Identification of Risk Factors Associated with Aetiology of Amyotrophic Lateral Sclerosis Based on Systematic Review and Meta-Analysis

Wang, M. (2014) · uO Research (University of Ottawa) · doi:10.20381/ruor-3755

REVIEW Autophagy, inflammation and neurodegenerative disease

Alirezaei, M., Kemball, C. C., & Whitton, J. L. (2015)

Endoplasmic reticulum stress induced by gemcitabine/cannabinoid combination triggers autophagy in pancreatic cancer cells through a ROS mediated mechanism.

Zaniboni, T. (2011)

Examining the Role of Endoplasmic Reticulum Stress in Pancreatic Beta-cell Biology

Teodoro, T. (2012) · TSpace (University of Toronto)

Endoplasmic reticulum stress induction by an endogenous retrovirus glycoprotein during neuroinflammation: regulation by a free radical scavenger

Deslauriers, A. M. (2010) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3rp6v

Unfolded protein response pathways in skeletal muscle homeostasis.

Bohnert, K. R. (2018) · doi:10.18297/etd/3033

Investigation of endoplasmic reticulum stress and protein aggregates in C9ORF72 mutant induced pluripotent stem cell-derived spinal motor neurons

Gane, A. B. (2018) · ERA

Endoplasmic Reticulum Stress is Transmissible among Cells of the Central Nervous System

Sprenkle, N. T. (2017) · doi:10.33915/etd.6704

Knight in Splicing Armor: Alternative Splicing as a Neuroprotective Mechanism

Park, J., Tao, X., & Zhai, R. G. (2020) · OBM Genetics · doi:10.21926/obm.genet.2001106

A CHCHD10 variant causing ALS elicits an unfolded protein response through the IRE1/XBP1 pathwayPreprint

Straub, I. R., Weraarpachai, W., & Shoubridge, E. A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.05.078881

IRE-1 regulates cellular homeostasis during disrupted lipid metabolism

Koh, J. H. (2021) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/152743

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