The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Protein Folding and Modification in the Mammalian Endoplasmic Reticulum
Abstract
Analysis of the human genome reveals that approximately a third of all open reading frames code for proteins that enter the endoplasmic reticulum (ER), demonstrating the importance of this organelle for global protein maturation. The path taken by a polypeptide through the secretory pathway starts with its translocation across or into the ER membrane. It then must fold and be modified correctly in the ER before being transported via the Golgi apparatus to the cell surface or another destination. Being physically segregated from the cytosol means that the ER lumen has a distinct folding environment. It contains much of the machinery for fulfilling the task of protein production, including complex pathways for folding, assembly, modification, quality control, and recycling. Importantly, the compartmentalization means that several modifications that do not occur in the cytosol, such as glycosylation and extensive disulfide bond formation, can occur to secreted proteins to enhance their stability before their exposure to the extracellular milieu. How these various machineries interact during the normal pathway of folding and protein secretion is the subject of this review.
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
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853
Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.092707.153558 · Cited by 1,163
Hammond, C., & Helenius, A. (1994) · The Journal of cell biology · doi:10.1083/jcb.126.1.41 · Cited by 443
Hendershot, L., Bole, D., Köhler, G., & Kearney, J. F. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.3.761 · Cited by 340
Protein quality control in the ER: The recognition of misfolded proteins
Määttänen, P., Gehring, K., Bergeron, J. J. M., & Thomas, D. Y. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.006 · Cited by 284
Mesd Encodes an LRP5/6 Chaperone Essential for Specification of Mouse Embryonic Polarity
Hsieh, J.-C., Lee, L., Zhang, L., Wefer, S., Brown, K., DeRossi, C., Wines, M. E., Rosenquist, T., & Holdener, B. C. (2003) · Cell · doi:10.1016/s0092-8674(03)00045-x · Cited by 237
Cited by
Endoplasmic reticulum stress signals in the tumour and its microenvironment
Chen, X., & Cubillos-Ruiz, J. R. (2021) · Nature Reviews Cancer · doi:10.1038/s41568-020-00312-2 · Cited by 1,356
Endoplasmic reticulum stress signalling-from basic mechanisms to clinical applications
Almanza, A., Carlesso, A., Chintha, C., Creedican, S., Doultsinos, D., Leuzzi, B., Luís, A., McCarthy, N., Montibeller, L., More, S., et al. (2019) · The FEBS Journal · doi:10.1111/febs.14608 · Cited by 1,034
Autophagy-Independent Functions of the Autophagy Machinery
Galluzzi, L., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.026 · Cited by 863
“Conventional and Non-conventional Secretion Conventional protein secretion involves the anterograde transport of ER-derived vesicles to the GA, vesicle trafficking from the cis though the trans GA, and ultimately, fusion of vesicles released from the trans GA with the plasma membrane (Braakman and Bulleid, 2011).”
BackgroundDisturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
Hetz, C., & Mollereau, B. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3689 · Cited by 684
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
The Challenge and Promise of Glycomics
Cummings, R. D., & Pierce, J. M. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.12.010 · Cited by 400
Chemistry and Enzymology of Disulfide Cross-Linking in Proteins
Fass, D., & Thorpe, C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00123 · Cited by 321
Tumor microenvironment signaling and therapeutics in cancer progression
Goenka, A., Khan, F., Verma, B., Sinha, P., Dmello, C. C., Jogalekar, M. P., Gangadaran, P., & Ahn, B. (2023) · Cancer Communications · doi:10.1002/cac2.12416 · Cited by 323
Yan, W., Diao, S., & Fan, Z. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02194-z · Cited by 167
Two phases of disulfide bond formation have differing requirements for oxygen
Koritzinsky, M., Levitin, F., van den Beucken, T., Rumantir, R. A., Harding, N. J., Chu, K. C., Boutros, P. C., Braakman, I., & Wouters, B. G. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201307185 · Cited by 136
Self-citationEfficient expression of full-length antibodies in the cytoplasm of engineered bacteria
Robinson, M.-P., Ke, N., Lobstein, J., Peterson, C., Szkodny, A., Mansell, T. J., Tuckey, C., Riggs, P. D., Colussi, P. A., Noren, C. J., et al. (2015) · Nature Communications · doi:10.1038/ncomms9072 · Cited by 131
Wang, W., Mao, X., Zhang, R., Zhou, X.-X., Liu, Y., Zhou, H., Jia, J., & Yan, B. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c02769 · Cited by 106
The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins
Feige, M. J., Gräwert, M. A., Marcinowski, M., Hennig, J., Behnke, J., Ausländer, D., Herold, E. M., Peschek, J., Castro, C. D., Flajnik, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321502111 · Cited by 91
Use of the SHuffle strains in production of proteins
Ren, G., Ke, N., & Berkmen, M. (2016) · Current Protocols in Protein Science · doi:10.1002/cpps.11 · Cited by 60
Endoplasmic Reticulum Stress and Reactive Oxygen Species in Plants
Cao, J., Wang, C., Hao, N., Fujiwara, T., & Wu, T. (2022) · Antioxidants · doi:10.3390/antiox11071240 · Cited by 58
Alzheimer’s as a Systems-Level Disease Involving the Interplay of Multiple Cellular Networks
Castrillo, J. I., & Oliver, S. G. (2016) · Methods in Molecular Biology · doi:10.1007/978-1-4939-2627-5_1 · Cited by 44
Endoplasmic Reticulum Stress and Tumor Microenvironment in Bladder Cancer: The Missing Link
Nie, Z., Chen, M., Wen, X., Gao, Y., Huang, D., Cao, H., Peng, Y., Guo, N., Ni, J., & Zhang, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.683940 · Cited by 43
The Role of the Hypoxia-Related Unfolded Protein Response (UPR) in the Tumor Microenvironment
Bartoszewska, S., Collawn, J. F., & Bartoszewski, R. (2022) · Cancers · doi:10.3390/cancers14194870 · Cited by 43
Masson, H., Tat, J., Di Giusto, P., Antonakoudis, A., Shamie, I., Baghdassarian, H., Samoudi, M., Robinson, C. M., Kuo, C.-C., Koga, N., et al. (2025) · Cell Systems · doi:10.1016/j.cels.2025.101453 · Cited by 6
Metadata
- Authors
- Braakman, I., & Bulleid, N. J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2011-07-07
- Volume
- 80
- Issue
- 1
- Pages
- 71-99
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2137559379
- Cited by
- 691
- References
- 6
- FWCI
- 2.90
- 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
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.
