The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers.
Open accessAbstract
The three separate proteins that make up anthrax toxin--protective antigen (PA), edema factor (EF), and lethal factor (LF)--act in binary combinations to produce two distinct reactions in experimental animals: edema (PA + EF) and death (PA + LF). PA is believed to interact with a membrane receptor, and after proteolytic processing, to mediate endocytosis and subsequent translocation of EF or LF into the cytosol. PA can be separated, after mild trypsinolysis, into two fragments, PA65 (65 kDa) and PA20 (20 kDa). We demonstrate that trypsin-cleaved PA is capable of forming cation-selective channels in planar phospholipid bilayer membranes and that this activity is confined to the PA65 fragment; PA20, LF, and EF are devoid of channel-forming activity. These PA65 channels exhibit pH-dependent and voltage-dependent activity--a property reminiscent of the channels formed by the two-chain proteins diphtheria, tetanus, and botulinum toxins.
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process.
Friedlander, A. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38364-3 · Cited by 612
Molecular Pharmacology of Botulinum Toxin and Tetanus Toxin
Simpson, L. L. (1986) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.26.040186.002235 · Cited by 468
Diphtheria toxin fragment forms large pores in phospholipid bilayer membranes.
Kagan, B. L., Finkelstein, A., & Colombini, M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.8.4950 · Cited by 334
Self-citationLeppla, S. H. (1984) · PubMed · Cited by 165
Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis
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[50] Formation of bimolecular membranes from lipid monolayers
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Anthrax Toxin: Receptor Binding, Internalization, Pore Formation, and Translocation
Young, J. A. T., & Collier, R. J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142728 · Cited by 601
Self-citationPore-forming protein toxins: from structure to function
Parker, M. W., & Feil, S. C. (2005) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2004.01.009 · Cited by 468
Anthrax protective antigen forms oligomers during intoxication of mammalian cells.
Milne, J. C., Furlong, D., Hanna, P. C., Wall, J. S., & Collier, R. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32036-7 · Cited by 395
Self-citationBacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria
Chakroun, M., Banyuls, N., Bel, Y., Escriche, B., & Ferré, J. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00060-15 · Cited by 305
Bacterial pore-forming toxins: The (w)hole story?
Gonzalez, M. R., Bischofberger, M., Pernot, L., van der Goot, F. G., & Frêche, B. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7434-y · Cited by 262
Metadata
- Authors
- Blaustein, R. O., Koehler, T. M., Collier, R. J., & Finkelstein, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1989-04
- Volume
- 86
- Issue
- 7
- Pages
- 2209-2213
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2054027422
- Cited by
- 270
- References
- 10
- FWCI
- 1.49
- Type
- journal article
- Language
- en
- Open access
- green
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- Blaustein, R. O., Koehler, T. M., Collier, R. J., & Finkelstein, A. (1989). Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.86.7.2209
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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.