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Journal ArticleDOI

Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor

TLDR
It is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway.
Abstract
Anthrax lethal toxin, produced by the bacterium Bacillus anthracis, is the major cause of death in animals infected with anthrax. One component of this toxin, lethal factor (LF), is suspected to be a metalloprotease, but no physiological substrates have been identified. Here it is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 (MAPKK1 and MAPKK2) and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway. The identification of a cleavage site for LF may facilitate the development of LF inhibitors.

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Citations
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Journal ArticleDOI

Bacillus anthracis edema but not lethal toxin challenge in rats is associated with depressed myocardial function in hearts isolated and tested in a Langendorff system

TL;DR: In vivo lethal LT challenge did not produce evidence of myocardial depression in isolated rat hearts, and while lethal ET challenge did depress isolated heart function, this may have resulted from prior hypotension and ischemia.
Journal ArticleDOI

Selective targeting of metastatic ovarian cancer using an engineered anthrax prodrug activated by membrane-anchored serine proteases

TL;DR: The basis for a transformative anticancer strategy based on anthrax toxin that has been engineered to be selectively activated by the catalytic power of zymogen-activating proteases on the surface of malignant tumor cells to induce cell death is developed.
Journal ArticleDOI

Cross-inhibition of pathogenic agents and the host proteins they exploit.

TL;DR: Two approved drugs are identified that effectively inhibited anthrax cytotoxic protease and demonstrated that they also block proteolytic activities of host furin, cathepsin B, and caspases that mediate toxin’s lethality in cells.
Journal ArticleDOI

Protein Kinase R in Bacterial Infections: Friend or Foe?

TL;DR: An overview of immune cell functions regulated by PKR is provided and the current knowledge on the role and functions of PKR in bacterial infections is summarized and existing pharmacological modulators of PKr that could be explored as novel treatment strategies for bacterial infections are provided.
Book ChapterDOI

Multivalent Inhibitors of Channel-Forming Bacterial Toxins.

TL;DR: Several prominent examples where the multivalent blockers were investigated for their ability to directly obstruct oligomeric channel-forming bacterial exotoxins, such as the pore-formingacterial toxins and B component of the binary bacterial toxins are described.
References
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Journal ArticleDOI

A synthetic inhibitor of the mitogen-activated protein kinase cascade.

TL;DR: Results indicate that the MAPK pathway is essential for growth and maintenance of the ras-transformed phenotype and PD 098059 is an invaluable tool that will help elucidate the role of theMAPK cascade in a variety of biological settings.
Journal ArticleDOI

Cyclin is degraded by the ubiquitin pathway

TL;DR: Cyclin degradation is the key step governing exit from mitosis and progress into the next cell cycle, and anaphase may be triggered by the recognition of cyclin by the ubiquitin-conjugating system.
Journal ArticleDOI

Transformation of mammalian cells by constitutively active MAP kinase kinase

TL;DR: It is found that constitutive activation of MAPKK is sufficient to promote cell transformation and is associated with highly tumorigenic in nude mice.
Journal ArticleDOI

Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells.

TL;DR: It is shown here that EF is an adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1] produced by Bacillus anthracis in an inactive form and nearly equals that of the most active known cyclase.
Journal ArticleDOI

Multiple Ras functions can contribute to mammalian cell transformation.

TL;DR: Results indicate that multiple cellular components, including Raf1, are activated by Ha-Ras and contribute to Ha- Ras-induced mammalian cell transformation.
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