The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The Bacterial Cell Envelope
Open accessAbstract
The bacteria cell envelope is a complex multilayered structure that serves to protect these organisms from their unpredictable and often hostile environment. The cell envelopes of most bacteria fall into one of two major groups. Gram-negative bacteria are surrounded by a thin peptidoglycan cell wall, which itself is surrounded by an outer membrane containing lipopolysaccharide. Gram-positive bacteria lack an outer membrane but are surrounded by layers of peptidoglycan many times thicker than is found in the gram-negatives. Threading through these layers of peptidoglycan are long anionic polymers, called teichoic acids. The composition and organization of these envelope layers and recent insights into the mechanisms of cell envelope assembly are discussed.
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Cites
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
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“Because of this, the periplasm has been called an evolutionary precursor of the lysosomes of eukaryotic cells (De Duve and Wattiaux, 1966).”
BackgroundProtein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.
Rapoport, T. A. (2007) · Nature · doi:10.1038/nature06384 · Cited by 977
Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J. M., & Engelhardt, H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709530105 · Cited by 596
Covalent lipoprotein from the outer membrane of Escherichia coli
Braun, V. (1975) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(75)90013-1 · Cited by 580
Structure of a complex of the ATPase SecA and the protein-translocation channel.
Zimmer, J., Nam, Y., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07335 · Cited by 459
Direct Visualization of the Outer Membrane of Mycobacteria and Corynebacteria in Their Native State
Zuber, B., Chami, M., Houssin, C., Dubochet, J., Griffiths, G., & Daffé, M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01919-07 · Cited by 458
Anchor Structure of Staphylococcal Surface Proteins
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Localization of Protein A in the Bacteria
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“Some of these surface proteins, called adhesins, are attached via noncovalent ionic interactions to peptidoglycan or teichoic acids, but many are attached covalently to stem peptides within the peptidoglycan layers (Dramsi et al. 2008; Sjoquist et al. 1972; Fischetti et al. 1990).”
Background
Cited by
Outer-membrane vesicles from Gram-negative bacteria: biogenesis and functions
Schwechheimer, C., & Kuehn, M. J. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3525 · Cited by 1,922
Silver nanoparticles: A new view on mechanistic aspects on antimicrobial activity
Durán, N., Durán, M., de Jesus, M. B., Seabra, A. B., Fávaro, W. J., & Nakazato, G. (2016) · Nanomedicine: Nanotechnology, Biology and Medicine · doi:10.1016/j.nano.2015.11.016 · Cited by 1,542
Wall Teichoic Acids of Gram-Positive Bacteria
Brown, S., Santa Maria, J. P., & Walker, S. (2013) · Annual Review of Microbiology · doi:10.1146/annurev-micro-092412-155620 · Cited by 966
Self-citationPorphyromonas gingivalis: An Overview of Periodontopathic Pathogen below the Gum Line
How, K. Y., Song, K. P., & Chan, K. G. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00053 · Cited by 858
Function and Biogenesis of Lipopolysaccharides
Bertani, B., & Ruiz, N. (2018) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0001-2018 · Cited by 742
Metadata
- Authors
- Silhavy, T. J., Kahne, D., & Walker, S.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-04-14
- Volume
- 2
- Issue
- 5
- Pages
- a000414-a000414
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2102906662
- Cited by
- 3,798
- References
- 9
- Type
- posted content
- Language
- en
- Open access
- bronze
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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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