Goettle, Martin and Dove, Stefan and Seifert, Roland (2012) Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action. TOXINS, 4 (7). pp. 505-535. ISSN 2072-6651
Full text not available from this repository. (Request a copy)Abstract
Since the isolation of Bacillus anthracis exotoxins in the 1960s, the detrimental activity of edema factor (EF) was considered as adenylyl cyclase activity only. Yet the catalytic site of EF was recently shown to accomplish cyclization of cytidine 5'-triphosphate, uridine 5'-triphosphate and inosine 5'-triphosphate, in addition to adenosine 5'-triphosphate. This review discusses the broad EF substrate specificity and possible implications of intracellular accumulation of cyclic cytidine 3':5'-monophosphate, cyclic uridine 3': 5'-monophosphate and cyclic inosine 3': 5'-monophosphate on cellular functions vital for host defense. In particular, cAMP-independent mechanisms of action of EF on host cell signaling via protein kinase A, protein kinase G, phosphodiesterases and CNG channels are discussed.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ADENYLATE-CYCLASE TOXIN; NUCLEOTIDE-GATED CHANNELS; BOMBARDMENT MASS-SPECTROMETRY; DEPENDENT PROTEIN-KINASE; LETHAL FACTOR CLEAVES; CYTIDINE 3'-5'-CYCLIC MONOPHOSPHATE; CYCLIC CMP PHOSPHODIESTERASE; HUMAN MONOCLONAL-ANTIBODY; SOLUBLE GUANYLYL CYCLASE; PROTECTIVE ANTIGEN; adenylyl cyclase toxin; anthrax; Bacillus anthracis; edema factor; edema toxin |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 600 Technology > 615 Pharmacy |
| Divisions: | Chemistry and Pharmacy > Institute of Pharmacy > Alumni or Retired Professors > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer) |
| Depositing User: | Petra Gürster |
| Date Deposited: | 18 May 2020 06:45 |
| Last Modified: | 18 May 2020 06:45 |
| URI: | https://pred.uni-regensburg.de/id/eprint/18474 |
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