The DOI matches its Crossref record; 137 of the 137 references it cites were found in a registry or an index.
Endoplasmic reticulum dysfunction in neurological disease
Open accessAbstract
Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible.
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In the citing paper
“Autosomal-dominant mutations in neuroserpin cause familial encephalopathy with Neuroserpin inclusion bodies, a rare, early-onset neurodegenerative dementia caused by protein aggregation within the endoplasmic reticulum (ER) and associated ER stress (Roussel et al., 2013).”
From Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models (2020) · cites this paper as Roussel et al., 2013
In the citing paper
“Previous work has linked disruptions to autophagy and lysosomal biology with AD72–74.”
From APOE genotypes differentially remodel the astrocytic lipid droplet proteome to shape lipid droplet dynamics (2026) · cites this paper as [74]
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1 retracted
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RetractedMutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310
IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
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Self-citationFamilial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024
A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress
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Research works printed but not linked: 1
- Harding, 2003, An integrated stress response regulates amino acid metabolism and resistance to oxidative stress, Mol Cell, 11, 619, 10.1016/S1097-2765(03)00105-9 · DOI
Cited by
Sorted by citations
The Role of Endoplasmic Reticulum Stress in Human Pathology
Oakes, S. A., & Papa, F. R. (2014) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104649 · Cited by 1,621
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 942
Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
Hetz, C., & Mollereau, B. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3689 · Cited by 684
Memory loss in Alzheimer's disease
Jahn, H. (2013) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2013.15.4/hjahn · Cited by 653
Pharmacological targeting of endoplasmic reticulum stress in disease
Marciniak, S. J., Chambers, J. E., & Ron, D. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00320-3 · Cited by 548
Self-citation
Metadata
- Authors
- Roussel, B. D., Kruppa, A. J., Miranda, E., Crowther, D. C., Lomas, D. A., & Marciniak, S. J.
- Affiliations
- Inserm (FR)
- University of Cambridge (GB)
- Istituto Pasteur (IT)
- Corresponding author
- Marciniak, Stefan J
- ORCID
- Venue
- The Lancet Neurology
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 12
- Issue
- 1
- Pages
- 105-118
- ISSN
- 1474-4422 (ISSN-L)
- OpenAlex
- W2051661723
- Cited by
- 441
- References
- 137
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 25 · 2023: 19 · 2022: 28 · 2021: 25 · 2020: 31 · 2019: 35 · 2018: 32 · 2017: 34 · 2016: 54 · 2015: 41 · 2014: 54 · 2013: 38
- FWCI
- 3.92
- Type
- journal article
- Language
- en
- Open access
- green
- inserm.hal.science
- Licence
- Locations
- The Lancet Neurology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by)
- HAL (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
- Apollo (University of Cambridge) (submittedVersion, cc-by-nc-nd)
- Apollo
- Funders
- Wellcome Trust (G1002610, 089703/Z/09/Z, 100140, 089703, 100140/Z/12/Z)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- endoplasmic reticulum dysfunction, endoplasmic reticulum stress, unfolded protein response, neurodegenerative diseases, cerebral ischemia, stroke, sleep apnea, Alzheimer's disease, amyloid-beta, neuroserpin, multiple sclerosis, amyotrophic lateral sclerosis, prion disease, Parkinson's disease, Huntington's disease, protein misfolding
- MeSH terms
- Animals, Endoplasmic Reticulum, Humans, Nervous System Diseases, Signal Transduction, Amyloid beta-Peptides, Protein Folding, Unfolded Protein Response
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