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.
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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
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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
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
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- Braakman, I., & Bulleid, N. J. (2011). Protein Folding and Modification in the Mammalian Endoplasmic Reticulum. Annual Review of Biochemistry. https://doi.org/10.1146/annurev-biochem-062209-093836
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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.
