The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structure and function of bacterial outer membrane proteins: barrels in a nutshell
Open accessAbstract
The outer membrane protects Gram‐negative bacteria against a harsh environment. At the same time, the embedded proteins fulfil a number of tasks that are crucial to the bacterial cell, such as solute and protein translocation, as well as signal transduction. Unlike membrane proteins from all other sources, integral outer membrane proteins do not consist of transmembrane α‐helices, but instead fold into antiparallel β‐barrels. Over recent years, the atomic structures of several outer membrane proteins, belonging to six families, have been determined. They include the OmpA membrane domain, the OmpX protein, phospholipase A, general porins (OmpF, PhoE), substrate‐specific porins (LamB, ScrY) and the TonB‐dependent iron siderophore transporters FhuA and FepA. These crystallographic studies have yielded invaluable insight into and decisively advanced the understanding of the functions of these intriguing proteins. Our review is aimed at discussing their common principles and peculiarities as well as open questions associated with them.
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Cites
Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide
Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W. (1998) · Science · doi:10.1126/science.282.5397.2215 · Cited by 787
Cited by
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Nikaido, H. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.593-656.2003 · Cited by 4,316
The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria
Pagès, J.-M., James, C. E., & Winterhalter, M. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1994 · Cited by 939
Recombinant protein secretion in Escherichia coli
Mergulhão, F. J. M., Summers, D. K., & Monteiro, G. A. (2005) · Biotechnology Advances · doi:10.1016/j.biotechadv.2004.11.003 · Cited by 485
Emerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Mesa-Galloso, H., Abdizadeh, H., Noskov, S. Y., Marrink, S. J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 459
Similarities and Differences between Silver Ions and Silver in Nanoforms as Antibacterial Agents
Kędziora, A., Speruda, M., Krzyżewska, E., Rybka, J., Łukowiak, A., & Bugla-Płoskońska, G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020444 · Cited by 452
Metadata
- Authors
- Koebnik, R., Locher, K. P., & Van Gelder, P.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2000-07
- Volume
- 37
- Issue
- 2
- Pages
- 239-253
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2004696942
- Cited by
- 1,202
- References
- 1
- FWCI
- 20.41
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Koebnik, R., Locher, K. P., & Van Gelder, P. (2000). Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Molecular Microbiology. https://doi.org/10.1046/j.1365-2958.2000.01983.x
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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).
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