The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.
Lipid-Dependent Membrane Protein Topogenesis
Open accessAbstract
The topology of polytopic membrane proteins is determined by topogenic sequences in the protein, protein-translocon interactions, and interactions during folding within the protein and between the protein and the lipid environment. Orientation of transmembrane domains is dependent on membrane phospholipid composition during initial assembly as well as on changes in lipid composition postassembly. The membrane translocation potential of negative amino acids working in opposition to the positive-inside rule is largely dampened by the normal presence of phosphatidylethanolamine, thus explaining the dominance of positive residues as retention signals. Phosphatidylethanolamine provides the appropriate charge density that permits the membrane surface to maintain a charge balance between membrane translocation and retention signals and also allows the presence of negative residues in the cytoplasmic face of proteins for other purposes.
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Cites
Structure and Mechanism of the Lactose Permease of Escherichia coli
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Self-citationRecognition of transmembrane helices by the endoplasmic reticulum translocon
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Protein Translocation Across the Bacterial Cytoplasmic Membrane
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Cited by
The Kennedy pathway—De novo synthesis of phosphatidylethanolamine and phosphatidylcholine
Gibellini, F., & Smith, T. K. (2010) · IUBMB Life · doi:10.1002/iub.337 · Cited by 830
Mechanisms of Integral Membrane Protein Insertion and Folding
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Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282
Structural Basis of Human CYP51 Inhibition by Antifungal Azoles
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Metadata
- Authors
- Dowhan, W., & Bogdanov, M.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2009-06-01
- Volume
- 78
- Issue
- 1
- Pages
- 515-540
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2126118567
- Cited by
- 263
- References
- 78
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- green
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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.