The DOI matches its Crossref record; 72 of the 72 references it cites were found in a registry or an index.
Secretion and Membrane Localization of Proteins in Escherichia Coli
Abstract
The envelope of Escherichia coli consists of two distinct membranes, the outer membrane and the cytoplasmic membrane. The space between the two membranes is called the periplasmic space, and each fraction contains its own specific proteins. In this review, it is discussed how proteins are localized in their final locations in the envelope. Proteins localized in the outer membrane and the periplasmic space as well as transmembranous proteins in the cytoplasmic membranes appear to be produced from their precursors which have peptide extensions of about 20 amino acid residues at the amino terminal ends. General features for the peptide extension are deduced from the known sequences of the peptide extensions, and, based on their known properties, a hypothesis (loop model) is proposed to explain the possible functions of the peptide extension during the mechanism of secretion across the cytoplasmic membrane.
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Citations
Cites
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Transfer of Proteins Across Membranes
Kreil, G. (1981) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.50.070181.001533 · Cited by 866
Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322.
Sutcliffe, J. G. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.8.3737 · Cited by 782
Characterization of the Major Envelope Protein from Escherichia coli
Rosenbusch, J. P. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42066-8 · Cited by 729
A Possible Precursor of Immunoglobulin Light Chains
MILSTEIN, C., BROWNLEE, G. G., HARRISON, T. M., & MATHEWS, M. B. (1972) · Nature New Biology · doi:10.1038/newbio239117a0 · Cited by 603
The Outer Membrane of Gram-negative Bacteria
Nikaido, H., & Nakae, T. (1980) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60208-8 · Cited by 587
Nucleotide sequence and amplification in bacteria of structural gene for rat growth hormone
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The Outer Membrane Proteins of Gram-Negative Bacteria: Biosynthesis, Assembly, and Functions
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Self-citation
Cited by
Lugtenberg, B., & Van Alphen, L. (1983) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(83)90014-x · Cited by 759
Randall, L. L. (1983) · Cell · doi:10.1016/0092-8674(83)90352-5 · Cited by 234
Optimisation of signal peptide for recombinant protein secretion in bacterial hosts
Low, K. O., Muhammad Mahadi, N., & Md. Illias, R. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-4831-z · Cited by 130
Genetic Mutations Affecting Human Lipoprotein Metabolism
Zannis, V. I., & Breslow, J. L. (1985) · Advances in Human Genetics 14 · doi:10.1007/978-1-4615-9400-0_3 · Cited by 65
Mode of Action of the Tetracyclines and the Nature of Bacterial Resistance to Them
Chopra, I. (1985) · Handbook of Experimental Pharmacology · doi:10.1007/978-3-642-70304-1_6 · Cited by 44
Metadata
- Authors
- Inouye, M., Halegoua, S., & Beckwith, J.
- Venue
- Critical Reviews in Biochemistry
- Publisher
- Informa UK Limited
- Published
- 1980-01
- Volume
- 7
- Issue
- 4
- Pages
- 339-371
- ISSN
- 0045-6411 (ISSN-L)
- 1040-8355
- OpenAlex
- W2215100787
- Cited by
- 401
- References
- 72
- FWCI
- 8.75
- Type
- journal article
- Language
- en
- Open access
- closed
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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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.