The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Disulfide Formation in the ER and Mitochondria: Two Solutions to a Common Process
Abstract
Two Ways to Redox Regulation: Eukaryotic cells control the redox environment within their cytoplasm to be generally reducing. However, the endoplasmic reticulum provides an oxidizing environment for secretory and membrane proteins. In addition, a subcompartment of mitochondria—the powerhouses of the cell—also generates an oxidizing environment for constituent and itinerant proteins. Riemer et al. (p. 1284 ) review the current understanding of both eukaryotic redox machineries and highlight their implications for the biogenesis and regulation of protein function, focusing on the impact of these systems on health and disease.
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Cites
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
The p66shc adaptor protein controls oxidative stress response and life span in mammals
Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712
A Disulfide Relay System in the Intermembrane Space of Mitochondria that Mediates Protein Import
Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., & Herrmann, J. M. (2005) · Cell · doi:10.1016/j.cell.2005.04.011 · Cited by 557
Self-citationMonitoring disulfide bond formation in the eukaryotic cytosol
Østergaard, H., Tachibana, C., & Winther, J. R. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200402120 · Cited by 333
Hu, J., Dong, L., & Outten, C. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803028200 · Cited by 273
Allen, S., Balabanidou, V., Sideris, D. P., Lisowsky, T., & Tokatlidis, K. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.049 · Cited by 235
A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1
Dabir, D. V., Leverich, E. P., Kim, S., Tsai, F. D., Hirasawa, M., Knaff, D. B., & Koehler, C. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601909 · Cited by 162
Cited by
Brigelius-Flohé, R., & Maiorino, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.020 · Cited by 1,904
Nguyen, V. D., Hatahet, F., Salo, K. E., Enlund, E., Zhang, C., & Ruddock, L. W. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-1 · Cited by 260
Reactive oxygen species and insulin resistance: the good, the bad and the ugly
Tiganis, T. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.11.006 · Cited by 256
Bien, M., Longen, S., Wagener, N., Chwalla, I., Herrmann, J. M., & Riemer, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.017 · Cited by 179
Self-citationHow do cilia organize signalling cascades?
Nachury, M. V. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0465 · Cited by 150
Metadata
- Authors
- Riemer, J., Bulleid, N., & Herrmann, J. M.
- Venue
- Science
- Published
- 2009-06-05
- Volume
- 324
- Issue
- 5932
- Pages
- 1284-1287
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2016980705
- Cited by
- 252
- References
- 7
- FWCI
- 11.04
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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