The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders
Open accessAbstract
Introduction ER stress and the UPR ER stress–induced apoptosis ER stress and autophagy The UPR and neurodegenerative disease Future perspectives The stimuli for neuronal cell death in neurodegenerative disorders are multi‐factorial and may include genetic predisposition, environmental factors, cellular stressors such as oxidative stress and free radical production, bioenergy failure, glutamate‐induced excitotoxicity, neuroinflammation, disruption of Ca 2+‐regulating systems, mitochondrial dysfunction and misfolded protein accumulation. Cellular stress disrupts functioning of the endoplasmic reticulum (ER), a critical organelle for protein quality control, leading to induction of the unfolded protein response (UPR). ER stress may contribute to neurodegeneration in a range of neurodegenerative disorders. This review summarizes the molecular events occurring during ER stress and the unfolded protein response and it specifically evaluates the evidence suggesting the ER stress response plays a role in neurodegenerative disorders.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
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
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835
Mediators of endoplasmic reticulum stress-induced apoptosis
Szegezdi, E., Logue, S. E., Gorman, A. M., & Samali, A. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400779 · Cited by 2,345
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 · cited 2×
“Several genetic mutations have been linked to the recessive form of PD including Parkin, an E3 ligase which forms part of the cascade reaction which targets misfolded proteins for degradation by the proteasome [84].”
BackgroundUnfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
One step at a time: endoplasmic reticulum-associated degradation
Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299
Toxic Proteins in Neurodegenerative Disease
Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251
The role of the Atg1/ULK1 complex in autophagy regulation
Mizushima, N. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.004 · Cited by 1,062
Cited by
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600
Sleep and the single neuron: the role of global slow oscillations in individual cell rest
Vyazovskiy, V. V., & Harris, K. D. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3494 · Cited by 386
Endoplasmic Reticulum Stress: Its Role in Disease and Novel Prospects for Therapy
Schönthal, A. H. (2012) · Scientifica · doi:10.6064/2012/857516 · Cited by 353
Glycogen synthase kinase-3 beta (GSK-3β) signaling: Implications for Parkinson's disease
Golpich, M., Amini, E., Hemmati, F., Ibrahim, N. M., Rahmani, B., Mohamed, Z., Raymond, A. A., Dargahi, L., Ghasemi, R., & Ahmadiani, A. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.03.010 · Cited by 276
Exosomal secretion of α-synuclein as protective mechanism after upstream blockage of macroautophagy
Fussi, N., Höllerhage, M., Chakroun, T., Nykänen, N.-P., Rösler, T. W., Koeglsperger, T., Wurst, W., Behrends, C., & Höglinger, G. U. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0816-2 · Cited by 161
Metadata
- Authors
- Doyle, K. M., Kennedy, D., Gorman, A. M., Gupta, S., Healy, S. J. M., & Samali, A.
- Venue
- Journal of Cellular and Molecular Medicine
- Publisher
- Wiley
- Published
- 2011-09-26
- Volume
- 15
- Issue
- 10
- Pages
- 2025-2039
- ISSN
- 1582-1838 (ISSN-L)
- 1582-4934
- OpenAlex
- W1975167087
- Cited by
- 321
- References
- 18
- FWCI
- 11.85
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders. https://app.cochat.ai/papers/10.1111/j.1582-4934.2011.01374.x
- The paper
- Doyle, K. M., Kennedy, D., Gorman, A. M., Gupta, S., Healy, S. J. M., & Samali, A. (2011). Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders. Journal of Cellular and Molecular Medicine. https://doi.org/10.1111/j.1582-4934.2011.01374.x
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.