Targeting the unfolded protein response for disease intervention.

Autophagy fights disease through cellular self-digestion

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The unfolded protein response: controlling cell fate decisions under ER stress and beyond

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XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response

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

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Autophagy Is Activated for Cell Survival after Endoplasmic ReticulumStress

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The Role of Endoplasmic Reticulum Stress in Human Pathology

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EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

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A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress

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IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein responsePreprint

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EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity

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Transcriptional Induction of Mammalian ER Quality Control Proteins Is Mediated by Single or Combined Action of ATF6α and XBP1

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ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation

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Targeting the unfolded protein response in disease

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Endoplasmic Reticulum Stress Plays a Central Role in Development of Leptin Resistance

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Bortezomib as the First Proteasome Inhibitor Anticancer Drug: Current Status and Future Perspectives

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Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease

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Pharmacological brake-release of mRNA translation enhances cognitive memory

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Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases

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Protein quality control in the early secretory pathway

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Discovery of 7-Methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1 H -indol-5-yl)-7 H -pyrrolo[2,3- d ]pyrimidin-4-amine (GSK2606414), a Potent and Selective First-in-Class Inhibitor of Protein Kinase R (PKR)-like Endoplasmic Reticulum Kinase (PERK)

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Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

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Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice

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The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule

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Suppression of eIF2α kinases alleviates Alzheimer's disease–related plasticity and memory deficits

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

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Fighting neurodegeneration with rapamycin: mechanistic insights

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Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent

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Identification of an Ire1alpha endonuclease specific inhibitor with cytotoxic activity against human multiple myeloma

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The Flavonoid Baicalein Inhibits Fibrillation of α-Synuclein and Disaggregates Existing Fibrils

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A transgenic mouse model for monitoring endoplasmic reticulum stress

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When ER stress reaches a dead end

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Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit

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Blockade of XBP1 splicing by inhibition of IRE1α is a promising therapeutic option in multiple myeloma

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Fine-Tuning of the Unfolded Protein Response: Assembling the IRE1α Interactome

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Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity

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AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP

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Grape-Derived Polyphenolics Prevent A Oligomerization and Attenuate Cognitive Deterioration in a Mouse Model of Alzheimer's Disease

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Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons

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Aggregation-prone c9FTD/ALS poly(GA) RAN-translated proteins cause neurotoxicity by inducing ER stress

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Expression of Concern: Antioxidant compounds have potent anti‐fibrillogenic and fibril‐destabilizing effects for α‐synuclein fibrils in vitro

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Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins

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Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease

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Dietary flavonoids as proteasome inhibitors and apoptosis inducers in human leukemia cells

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Antioxidant properties of natural polyphenols and their therapeutic potentials for Alzheimer's disease

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Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy.

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Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 1. An overview.

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Dual and opposing roles of the unfolded protein response regulated by IRE1α and XBP1 in proinsulin processing and insulin secretion

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Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds

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Sodium 4-Phenylbutyrate Protects against Cerebral Ischemic Injury

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Olive-Oil-Derived Oleocanthal Enhances β-Amyloid Clearance as a Potential Neuroprotective Mechanism against Alzheimer’s Disease: In Vitro and in Vivo Studies

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Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment

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MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis

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Protein Disulfide Isomerase A6 Controls the Decay of IRE1α Signaling via Disulfide-Dependent Association

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A molecular chaperone inducer protects neurons from ER stress

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Pharmacological dimerization and activation of the exchange factor eIF2B antagonizes the integrated stress response

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Flavonols and flavones as BACE-1 inhibitors: Structure–activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features

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Discovery of GSK2656157: An Optimized PERK Inhibitor Selected for Preclinical Development

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Mutations in a translation initiation factor identify the target of a memory-enhancing compound

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Inhibition of Proteasomal Function by Curcumin Induces Apoptosis through Mitochondrial Pathway

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The Polyphenol Oleuropein Aglycone Protects TgCRND8 Mice against Aß Plaque Pathology

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Tauroursodeoxycholic acid in the treatment of patients with amyotrophic lateral sclerosis

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Control of dopaminergic neuron survival by the unfolded protein response transcription factor XBP1

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Potent and Selective Inhibitors of the Inositol-requiring Enzyme 1 Endoribonuclease

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Druggable sensors of the unfolded protein response

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Flavonol Activation Defines an Unanticipated Ligand-Binding Site in the Kinase-RNase Domain of IRE1

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Chemical and Biological Approaches for Adapting Proteostasis to Ameliorate Protein Misfolding and Aggregation Diseases-Progress and PrognosisPreprint

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Unfolded protein response in cancer: the Physician's perspective

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Inhibition of the proteasome activity, a novel mechanism associated with the tumor cell apoptosis-inducing ability of genistein

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Targeting endoplasmic reticulum stress in metabolic disease

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Targeting autophagy in neurodegenerative diseases

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Regulation of innate immunity by signaling pathways emerging from the endoplasmic reticulum

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Development of Radicicol Analogues

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Activation of the unfolded protein response enhances motor recovery after spinal cord injury

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The Endoplasmic Reticulum Stress Sensor, ATF6α, Protects against Neurotoxin-induced Dopaminergic Neuronal Death

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Structure and mechanism of action of the hydroxy–aryl–aldehyde class of IRE1 endoribonuclease inhibitors

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Bone and the Unfolded Protein Response: In Sickness and in Health

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Inositol-Requiring Enzyme 1 Alpha Endoribonuclease Specific Inhibitor STF-083010 Alleviates Carbon Tetrachloride Induced Liver Injury and Liver Fibrosis in Mice

Chen, Q., Zhang, C., Qin, M.-Q., Li, J., Wang, H., Xu, D., & Wang, J. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01344 · Cited by 18 · see citing works

The role of the unfolded protein response in axial spondyloarthritis

Smith, J. (2016) · Clinical Rheumatology · doi:10.1007/s10067-015-3117-5 · Cited by 15 · see citing works

Endoplasmic reticulum stress and proteasome pathway involvement in human podocyte injury with a truncated COL4A3 mutation

Zhang, H., Huang, J.-N., Liu, Y., Ren, H., Xie, J., & Chen, N. (2019) · Chinese Medical Journal · doi:10.1097/cm9.0000000000000294 · Cited by 16 · see citing works

Preconditioning of endoplasmic reticulum stress protects against acrylonitrile-induced cytotoxicity in primary rat astrocytes: The role of autophagy

Bai, Y., Wenjun, Z., Changsheng, Y., Yuntao, F., Ma, J., Li, B., Hai, Q., Xing, G., Suhua, W., Li, F., et al. (2016) · NeuroToxicology · doi:10.1016/j.neuro.2016.05.020 · Cited by 14 · see citing works

Network pharmacology, molecular docking, and in vitro experimental verification of the mechanism of Guanxining in treating diabetic atherosclerosis

Wang, W., Wang, S., Li, Y., Zhu, M., Xu, Q., Luo, B., Liu, Y., & Liu, Y. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.117792 · Cited by 13 · see citing works

HSP90 inhibitors in the context of heat shock and the unfolded protein response: effects on a primary canine pulmonary adenocarcinoma cell line*

Graner, A. N., Hellwinkel, J. E., Lencioni, A., Madsen, H. J., Harland, T., Marchando, P., Nguyen, G. J., Wang, M. X., Russell, L. M., Bemis, L., et al. (2016) · International Journal of Hyperthermia · doi:10.1080/02656736.2016.1256503 · Cited by 12 · see citing works

Identification of BRaf-Sparing Amino-Thienopyrimidines with Potent IRE1α Inhibitory Activity

Beveridge, R. E., Wallweber, H. A., Ashkenazi, A., Beresini, M. H., Clark, K., Gibbons, P., Ghiro, É., Kaufman, S., Larivée, A., Leblanc, M., et al. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00344 · Cited by 11 · see citing works

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 · see citing works

Azetidine-2-Carboxylic Acid-Induced Oligodendrogliopathy: Relevance to the Pathogenesis of Multiple Sclerosis

Sobel, R. A., Albertelli, M. A., Hinojoza, J. R., Eaton, M. J., Grimes, K., & Rubenstein, E. (2022) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlac028 · Cited by 10 · see citing works

A fluorescent analogue of tauroursodeoxycholic acid reduces ER stress and is cytoprotective

Gavin, J., Quilty, F., Májer, F., Gilsenan, G., Byrne, A.-M., Long, A., Radics, G., & Gilmer, J. F. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.06.059 · Cited by 9 · see citing works

Rce1 expression in renal cell carcinoma and its regulatory effect on 786-O cell apoptosis through endoplasmic reticulum stress

Li, J., Wang, D., Liu, J., Qin, Y., Huang, L., Qiangfeng, Z., Xiao, M., Hu, J., Yang, Q., He, J., et al. (2017) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmx002 · Cited by 8 · see citing works

An Overview of the Unfolded Protein Response (UPR) and Autophagy Pathways in Human Viral Oncogenesis

Dutta, S., Ganguly, A., & Roy, S. G. (2024) · International review of cytology · doi:10.1016/bs.ircmb.2024.01.004 · Cited by 7 · see citing works

In Silico Drug Target Discovery Through Proteome Mining from M. tuberculosis: An Insight into Antivirulent Therapy

Bhattacharya, S., Ghosh, P., Banerjee, D., Banerjee, A., & Ray, S. (2020) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207323666200219120903 · Cited by 7 · see citing works

Proteotoxicity and endoplasmic reticulum stress-mediated cell death

Wang, M., Law, M. E., & Law, B. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814208-0.00006-3 · Cited by 6 · see citing works

Inhibition of the TRPM2 cation channel attenuates morphine tolerance by modulating endoplasmic reticulum stress and apoptosis in rats

ÇİLTAŞ, A. Ç., Özdemir, E., Güneş, H., & Öztürk, A. (2025) · Neuroscience Letters · doi:10.1016/j.neulet.2025.138168 · Cited by 5 · see citing works

Sequence-to-Structure Relation in Proteins-Amyloidogenic Proteins with Chameleon Sequences

Banach, M., Kalinowska, B., Konieczny, L., & Roterman, I. (2016) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000415 · Cited by 5 · see citing works

Proteostasis and Diseases of the Motor Unit

Rinaldi, C., Mäger, I., & Wood, M. J. A. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00164 · Cited by 5 · see citing works

Pharmacological Targeting of the ER-Resident Chaperones GRP94 or Cyclophilin B Induces Secretion of IL-22 Binding Protein Isoform-1 (IL-22BPi1)

Gómez-Fernández, P., Urtasun, A., Astobiza, I., Mena, J., Alloza, I., & Vandenbroeck, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102440 · Cited by 2 · see citing works

Multiple unfolded protein response pathways cooperate to link cytosolic dsDNA release to stimulator of interferon gene activation

Hu, T., Liu, Y., Fleck, J., King, C. R., Schalk, E., Zhang, Z., Mehle, A., & Smith, J. A. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1358462 · Cited by 1 · see citing works

Calcium overload induces reactive oxygen species to enhance glioblastoma radiosensitivity

Lai, X., Lu, Y., Li, J., Liu, L., Yuan, S., & Qian, J. (2026) · Medical Gas Research · doi:10.4103/mgr.medgasres-d-26-00022 · Cited by 1 · see citing works

Molecular Genetics of the Cartilage Collagenopathies

Lamandé, S. R., Cameron, T. L., Savarirayan, R., & Bateman, J. F. (2017) · Springer eBooks · doi:10.1007/978-3-319-45803-8_6 · Cited by 1 · see citing works

miRNA- 125b Signaling Ameliorates Liver Injury Against Obstructive Jaundice-Induced Excessive Fibrosis in Experimental Rats

Zhang, X., Zhang, F., Chang-xi, Z., & Li, J. (2021) · Yonsei Medical Journal · doi:10.3349/ymj.2021.62.5.453 · Cited by 1 · see citing works

PREFACE: Divergent roles of ER stress in neurodegeneration and brain disorders

Hetz, C. A., & Saxena, S. (2016) · Brain Research · doi:10.1016/j.brainres.2016.09.014 · Cited by 1 · see citing works

New molecular insights in pathogenesis of congenital hypothyroidism

Stoupa, A. (2021) · doi:10.70675/ba72d900z86edz4200z8ddcz1af6c6d513ae

BindingDB Entry 50011475: Identification of BRaf-Sparing Amino-Thienopyrimidines with Potent IRE1α Inhibitory Activity.

BindingDB (2022) · UC San Diego · doi:10.7270/q24q7zmd

Targeting the unfolded protein response in disease

Hetz, C. A., Chevet, É., & Harding, H. P. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd3976 · Cited by 908 · see citing works

Pharmacological targeting of the unfolded protein response for disease intervention

Hetz, C. A., Axten, J. M., & Patterson, J. B. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0326-2 · Cited by 252 · see citing works

Targeting unfolded protein response: a new horizon for disease control

Khanna, M., Agrawal, N., Chandra, R., & Dhawan, G. (2021) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2021.2 · Cited by 37 · see citing works

Pharmacological targeting of endoplasmic reticulum stress in disease

Marciniak, S., Chambers, J. E., & Ron, D. (2021) · Nature reviews. Drug discovery · doi:10.1038/s41573-021-00320-3 · Cited by 1 · see citing works

Small Molecules to Improve ER Proteostasis in Disease

Gonzalez‐Teuber, V., Albert‐Gascó, H., Auyeung, V. C., Papa, F. R., Mallucci, G. R., & Hetz, C. A. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.07.003 · Cited by 77 · see citing works