The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Roles of Molecular Chaperones in Endoplasmic Reticulum (ER) Quality Control and ER-Associated Degradation (ERAD)
Abstract
Secreted proteins are synthesized at the endoplasmic reticulum (ER), and a quality control mechanism in the ER is essential to maintain secretory pathway homeostasis. Newly synthesized soluble and integral membrane secreted proteins fold into their native conformations with the aid of ER molecular chaperones before they are transported to post-ER compartments. However, terminally mis-folded proteins may be retained in the ER and degraded by a process called ER-associated degradation (ERAD). Recent studies using yeast have shown that molecular chaperones both in the ER and in the cytosol play key roles during the ERAD of mis-folded proteins. One important role for chaperones during ERAD is to prevent substrate protein aggregation. Substrate selection is another important role for molecular chaperones during ERAD.
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
Roles of N-Linked Glycans in the Endoplasmic Reticulum
Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037
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
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
Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., Gurkan, C., Kellner, W., Matteson, J., Plutner, H., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.043 · Cited by 601
A Luminal Surveillance Complex that Selects Misfolded Glycoproteins for ER-Associated Degradation
Denic, V., Quan, E. M., & Weissman, J. S. (2006) · Cell · doi:10.1016/j.cell.2006.05.045 · Cited by 422
Cytoplasmic destruction of p53 by the endoplasmic reticulum‐resident ubiquitin ligase ‘Synoviolin’
Yamasaki, S., Yagishita, N., Sasaki, T., Nakazawa, M., Kato, Y., Yamadera, T., Bae, E., Toriyama, S., Ikeda, R., Zhang, L., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601490 · Cited by 275
ER stress causes widespread protein aggregation and prion formation
Hamdan, N., Kritsiligkou, P., & Grant, C. M. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612165 · Cited by 85
Metadata
- Authors
- Nishikawa, S.-I., Brodsky, J. L., & Nakatsukasa, K.
- Venue
- The Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-05-01
- Volume
- 137
- Issue
- 5
- Pages
- 551-555
- ISSN
- 0021-924X (ISSN-L)
- 1756-2651
- OpenAlex
- W2065022563
- Cited by
- 174
- References
- 2
- FWCI
- 4.49
- Type
- journal article
- Language
- en
- Open access
- closed
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: Roles of Molecular Chaperones in Endoplasmic Reticulum (ER) Quality Control and ER-Associated Degradation (ERAD). https://app.cochat.ai/papers/10.1093/jb/mvi068
- The paper
- Nishikawa, S.-I., Brodsky, J. L., & Nakatsukasa, K. (2005). Roles of Molecular Chaperones in Endoplasmic Reticulum (ER) Quality Control and ER-Associated Degradation (ERAD). The Journal of Biochemistry. https://doi.org/10.1093/jb/mvi068
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.
