The DOI matches its Crossref record; 118 of the 118 references it cites were found in a registry or an index.
Protein Folding in the Endoplasmic Reticulum
Open accessAbstract
In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, N-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline cis-trans isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.
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Cites
SignalP 4.0: discriminating signal peptides from transmembrane regions
Petersen, T. N., Brunak, S., von Heijne, G., & Nielsen, H. (2011) · Nature Methods · doi:10.1038/nmeth.1701 · Cited by 8,847
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
Precision Mapping of an In Vivo N-Glycoproteome Reveals Rigid Topological and Sequence Constraints
Zielinska, D. F., Gnad, F., Wiśniewski, J. R., & Mann, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.012 · Cited by 902
Peptide-binding specificity of the molecular chaperone BiP
Flynn, G. C., Pohl, J., Flocco, M. T., & Rothman, J. E. (1991) · Nature · doi:10.1038/353726a0 · Cited by 765
GHKL, an emergent ATPase/kinase superfamily
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The human protein disulphide isomerase family: substrate interactions and functional properties
Ellgaard, L., & Ruddock, L. W. (2005) · EMBO reports · doi:10.1038/sj.embor.7400311 · Cited by 755
Protein Folding and Modification in the Mammalian Endoplasmic Reticulum
Braakman, I., & Bulleid, N. J. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062209-093836 · Cited by 691
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Self-citationOS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD
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Cited by
The endoplasmic reticulum: structure, function and response to cellular signaling
Schwarz, D. S., & Blower, M. D. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2052-6 · Cited by 1,613
In vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,439
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
ER-associated degradation: Protein quality control and beyond
Ruggiano, A., Foresti, O., & Carvalho, P. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312042 · Cited by 607
Quality Control in the Endoplasmic Reticulum: Crosstalk between ERAD and UPR pathways
Hwang, J., & Qi, L. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.06.005 · Cited by 592
Metadata
- Authors
- Braakman, I., & Hebert, D. N.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2013-05-01
- Volume
- 5
- Issue
- 5
- Pages
- a013201-a013201
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2103644580
- Cited by
- 571
- References
- 118
- Type
- posted content
- Language
- en
- Open access
- bronze
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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.
