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Write 1 page thesis on the topic assigment. Annotated Bibliography Botello-Morte L., Bes, M. T., Heras, B., Fernández-Otal, Á., Peleato, M. L & Fillat, M.F. (March 20, . Unraveling theRedox Proper

Write 1 page thesis on the topic assigment. Annotated Bibliography Botello-Morte L., Bes, M. T., Heras, B., Fernández-Otal, Á., Peleato, M. L & Fillat, M.F. (March 20, . Unraveling theRedox Properties of the Global Regulator FurA from Anabaena sp. PCC 7120: Disulfide Reductase Activity Based on Its CXXC Motifs. Antioxidants & Redox Signaling, 20(9): 1396-1406.

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This is a scientific article written by Botello-Morte, Bes, Heras, Fernández-Otal, Peleato, and Fillat. The aim of this scholarly work is to critically evaluate the supposed contribution of CXXC motifs to FurA’s redox properties. This research work also intends to obtain understanding of the potential interacting partners of Cyanobacterial FurA. The authors say that the function of the Cyanobacterial FurA is to act as a global regulator that links “iron homeostasis to photosynthetic metabolism and the responses to different environmental stresses” (Botello-Morte, et al). According to the scholars, FurA regulates various genes involved in redox homeostasis and works to meet the characteristics of a heme-sensor protein, whose interaction with this cofactor can have a negative impact on its DNA binding ability.

2. Heras, B., Scanlon, M. J & Martin, J. L. (Feb 19, 2014). Targeting Virulence not Viability in the Search for Future Antibacterials. Br J ClinPharmacol. doi: 10.1111/bcp.12356.

Targeting Virulence not Viability in the Search for Future Antibacterials is a research paper written by Heras, Scanlon, and Martin. In this article, the authors give particular focus to the subject ‘rapid antibiotic resistance’. The writers assert that improved approaches need to be developed for new antibacterials to overcome the issue of rapid antibiotic resistance. For this purpose, the researchers examine the development of improved new antibacterial drugs that do not either kill bacteria or hinder their growth but fight disease through targeting bacterial virulence. This research work gives readers a clear view of why existing approaches or techniques are not capable of addressing the issue of rapid antibiotic resistance in antibacterials. The study leaves further scope for experiments in the field of medical research.

List of All References

Botello-Morte L., Bes, M. T., Heras, B., Fernández-Otal, Á., Peleato, M. L & Fillat, M.F. (March 20, 2014). Unraveling the Redox Properties of the Global Regulator FurA from Anabaena sp. PCC 7120: Disulfide Reductase Activity Based on Its CXXC Motifs. Antioxidants & Redox Signaling, 20(9): 1396-1406.

Heras, B., Scanlon, M. J & Martin, J. L. (Feb 19, 2014). Targeting Virulence not Viability in the Search for Future Antibacterials. Br J ClinPharmacol. doi: 10.1111/bcp.12356.

Nagpal, J., Tan, J. L., Truscott, K. N., Heras, B & Dougan, D. A. (2013). Control of protein function through regulated protein degradation: biotechnological and biomedical applications. J MolMicrobiolBiotechnol 23(4-5):335-44.

Daly, N. L., Thorstholm, L., Greenwood, K. P., King, G. J.,&nbsp.Rosengren, K. J & Heras, B et al. (2013). Structural Insights into the Role of the Cyclic Backbone in a Squash Trypsin Inhibitor. J Biol Chem, 288(50):36141-8.

Kurth, F., Rimmer, K., Premkumar, L., Mohanty, B., Duprez, W & Halili, M et al. (2013). Comparative Sequence, Structure and Redox Analyses of&nbsp.KlebsiellapneumoniaeDsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct Classes. PLoS ONE 8(11): e80210. doi:10.1371/journal.pone.0080210.

Shepherd, M. 1., Heras, B., Achard, M. E., King, G. J., Argente, M. P., Kurth, F & Taylor, S. et al. (2013). Structural and Functional Characterization of ScsC, a PeriplasmicThioredoxin-Like Protein from&nbsp.Salmonella enterica&nbsp.SerovarTyphimurium. Antioxidants & Redox Signaling. 19(13): 1494-1506.

Heras, B., Totsika, M., Peters, K. M., Paxman, J. J., Gee, C. L., Jarrott, R. J & Perugini, M. A et al. (2013). The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping. Proceedings of the National Academy of Sciences of the United States of America, 111(1):457-62.