The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Endoplasmic Reticulum Structure and Interconnections with Other Organelles
Open accessAbstract
The endoplasmic reticulum (ER) is a large, continuous membrane-bound organelle comprised of functionally and structurally distinct domains including the nuclear envelope, peripheral tubular ER, peripheral cisternae, and numerous membrane contact sites at the plasma membrane, mitochondria, Golgi, endosomes, and peroxisomes. These domains are required for multiple cellular processes, including synthesis of proteins and lipids, calcium level regulation, and exchange of macromolecules with various organelles at ER-membrane contact sites. The ER maintains its unique overall structure regardless of dynamics or transfer at ER-organelle contacts. In this review, we describe the numerous factors that contribute to the structure of the ER.
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Cites
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275
Li, Y., & Prinz, W. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407600200 · Cited by 144
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
Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions
Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625
Cellular Reorganization during Mitotic Entry
Champion, L., Linder, M. I., & Kutay, U. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.07.004 · Cited by 139
Marzook, A., Tomas, A., & Jones, B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678055 · Cited by 121
XBP1 links the 12-hour clock to NAFLD and regulation of membrane fluidity and lipid homeostasis
Meng, H., Gonzales, N. M., Lonard, D. M., Putluri, N., Zhu, B., Dacso, C. C., York, B., & O’Malley, B. W. (2020) · Nature Communications · doi:10.1038/s41467-020-20028-z · Cited by 67
Metadata
- Authors
- English, A. R., & Voeltz, G. K.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2013-04-01
- Volume
- 5
- Issue
- 4
- Pages
- a013227-a013227
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2105729094
- Cited by
- 330
- References
- 3
- Type
- posted content
- Language
- en
- Open access
- bronze
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