The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Cotranslocational Degradation Protects the Stressed Endoplasmic Reticulum from Protein Overload
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Citations
Cites
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099
Orchestrating the unfolded protein response in health and disease
Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216886 · Cited by 1,015
Targeted disruption of the chop gene delays endoplasmic reticulum stress-mediated diabetes
Oyadomari, S., Koizumi, A., Takeda, K., Gotoh, T., Akira, S., Araki, E., & Mori, M. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0214550 · Cited by 752
Self-citationYan, W., Frank, C. L., Korth, M. J., Sopher, B. L., Novoa, I., Ron, D., & Katze, M. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252341799 · Cited by 385
Self-citation
Cited by
Endoplasmic Reticulum Stress: Signaling the Unfolded Protein Response
Lai, E., Teodoro, T., & Volchuk, A. (2007) · Physiology · doi:10.1152/physiol.00050.2006 · Cited by 478
Pobre, K. F. R., Poet, G. J., & Hendershot, L. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002804 · Cited by 429
The role of the unfolded protein response in cancer progression: From oncogenesis to chemoresistance
Madden, E., Logue, S. E., Healy, S. J., Manie, S., & Samali, A. (2019) · Biology of the Cell · doi:10.1111/boc.201800050 · Cited by 359
Oxidative and endoplasmic reticulum stress interplay in sporadic amyotrophic lateral sclerosis
Ilieva, E. V., Ayala, V., Jove, M., Dalfo, E., Cacabelos, D., Povedano, M., Bellmunt, M. J., Ferrer, I., Pamplona, R., & Portero-Otin, M. (2007) · Brain · doi:10.1093/brain/awm190 · Cited by 358
N-glycan structure dictates extension of protein folding or onset of disposal
Molinari, M. (2007) · Nature Chemical Biology · doi:10.1038/nchembio880 · Cited by 300
Metadata
- Authors
- Oyadomari, S., Yun, C., Fisher, E. A., Kreglinger, N., Kreibich, G., Oyadomari, M., Harding, H. P., Goodman, A. G., Harant, H., Garrison, J. L., Taunton, J., Katze, M. G., & Ron, D.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-08
- Volume
- 126
- Issue
- 4
- Pages
- 727-739
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2016983085
- Cited by
- 252
- References
- 5
- FWCI
- 9.99
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Cotranslocational Degradation Protects the Stressed Endoplasmic Reticulum from Protein Overload. https://app.cochat.ai/papers/10.1016/j.cell.2006.06.051
- The paper
- Oyadomari, S., Yun, C., Fisher, E. A., Kreglinger, N., Kreibich, G., Oyadomari, M., Harding, H. P., Goodman, A. G., Harant, H., Garrison, J. L., Taunton, J., Katze, M. G., & Ron, D. (2006). Cotranslocational Degradation Protects the Stressed Endoplasmic Reticulum from Protein Overload. Cell. https://doi.org/10.1016/j.cell.2006.06.051
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.