The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
Anthrax Toxin: Receptor Binding, Internalization, Pore Formation, and Translocation
Abstract
Anthrax toxin consists of three nontoxic proteins that self-assemble at the surface of receptor-bearing mammalian cells or in solution, yielding a series of toxic complexes. Two of the proteins, called Lethal Factor (LF) and Edema Factor (EF), are enzymes that act on cytosolic substrates. The third, termed Protective Antigen (PA), is a multifunctional protein that binds to receptors, orchestrates the assembly and internalization of the complexes, and delivers them to the endosome. There, the PA moiety forms a pore in the endosomal membrane and promotes translocation of LF and EF to the cytosol. Recent advances in understanding the entry process include insights into how PA recognizes its two known receptors and its ligands, LF and EF; how the PA:receptor interaction influences the pH-dependence of pore formation; and how the pore functions in promoting translocation of LF and EF across the endosomal membrane.
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Cites
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Identification of the cellular receptor for anthrax toxin
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Self-citationCrystal structure of the anthrax toxin protective antigen
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Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor
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Seidah, N. G., & Prat, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3699 · Cited by 759
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Metadata
- Authors
- Young, J. A. T., & Collier, R. J.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2007-06-07
- Volume
- 76
- Issue
- 1
- Pages
- 243-265
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2153738223
- Cited by
- 601
- References
- 60
- FWCI
- 2.64
- Type
- journal article
- Language
- en
- Open access
- closed
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- Young, J. A. T., & Collier, R. J. (2007). Anthrax Toxin: Receptor Binding, Internalization, Pore Formation, and Translocation. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.75.103004.142728
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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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