Toxin Instability and Its Role in Toxin Translocation from the Endoplasmic Reticulum to the Cytosol
Abstract
:1. AB Protein Toxins
2. Order–Disorder–Order Transitions for AB-Type, ER-Translocating Toxins
3. Holotoxin Disassembly
3.1. Cholera Toxin
3.2. Ricin Toxin
3.3. Pertussis Toxin
3.4. Shiga Toxin
3.5. Exotoxin A
3.6. Summary
4. Intrinsic Instability of the Isolated Toxin A Chain
4.1. Cholera Toxin
4.2. Ricin Toxin
4.3. Pertussis Toxin
4.4. Shiga Toxin
4.5. Exotoxin A
4.6. Cytolethal Distending Toxin
4.7. Summary
5. ERAD Processing of the Toxin A Chain
5.1. Cholera Toxin
5.2. Ricin Toxin
5.3. Shiga Toxin
5.4. Exotoxin A
5.5. Summary
6. Toxin Extraction from the ER
6.1. Cholera Toxin
6.2. Ricin Toxin
6.3. Shiga Toxin
6.4. Summary
7. Toxin Evasion of Efficient Degradation by the Ubiquitin-Proteasome System
7.1. Cholera Toxin
7.2. Ricin Toxin
7.3. Pertussis Toxin
7.4. Shiga Toxin
7.5. Cytolethal Distending Toxin
7.6. Summary
8. Refolding and Activation of the Cytosolic Toxin
8.1. Cholera Toxin
8.2. Ricin Toxin
8.3. Pertussis Toxin
8.4. Summary
9. Conclusions
Acknowledgments
Conflicts of Interest
References
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Teter, K. Toxin Instability and Its Role in Toxin Translocation from the Endoplasmic Reticulum to the Cytosol. Biomolecules 2013, 3, 997-1029. https://doi.org/10.3390/biom3040997
Teter K. Toxin Instability and Its Role in Toxin Translocation from the Endoplasmic Reticulum to the Cytosol. Biomolecules. 2013; 3(4):997-1029. https://doi.org/10.3390/biom3040997
Chicago/Turabian StyleTeter, Ken. 2013. "Toxin Instability and Its Role in Toxin Translocation from the Endoplasmic Reticulum to the Cytosol" Biomolecules 3, no. 4: 997-1029. https://doi.org/10.3390/biom3040997