Team:IISER Bhopal/References

iGEM IISER Bhopal

References

  1. Ferrer et al. Chaperonins govern growth of Escherichia coli at low temperatures, Nat. Biotech. 21, 1266 - 1267 (2003). doi: 10.1038/nbt1103-1266

  2. Ferrer, M., Lünsdorf, H., Chernikova, T. N., Yakimov, M. , Timmis, K. N. and Golyshin, P. N. (2004), Functional consequences of single: double ring transitions in chaperonins: life in the cold. Molecular Microbiology, 53: 167-182. doi: 10.1111/j.1365-2958.2004.04077.x

  3. Strocchi, M., Ferrer, M., Timmis, K. and Golyshin, P. (2006), Low temperature‐induced systems failure in Escherichia coli: Insights from rescue by cold‐adapted chaperones. Proteomics, 6: 193-206. doi: 10.1002/pmic.200500031

  4. Team Amsterdam iGEM 2011

  5. Feller, Georges, and Charles Gerday. 2003. “Psychrophilic Enzymes: Hot Topics in Cold Adaptation.” Nature Reviews. Microbiology 1 (3): 200–208. doi: 10.1038/nrmicro773

  6. Feller, G., O. Le Bussy, and C. Gerday. 1998. “Expression of Psychrophilic Genes in Mesophilic Hosts: Assessment of the Folding State of a Recombinant Alpha-Amylase.” Applied and Environmental Microbiology 64 (3): 1163–65. PMCID: PMC106386

  7. Joseph, Babu, Vinod Kumar, and Pramod W. Ramteke. 2019. “Psychrophilic Enzymes: Potential Biocatalysts for Food Processing.” Enzymes in Food Biotechnology. doi: 10.1016/b978-0-12-813280-7.00047-5

  8. Cavicchioli R, Charlton T, Ertan H, Mohd Omar S, Siddiqui KS, Williams TJ. Biotechnological uses of enzymes from psychrophiles. Microb Biotechnol. 2011;4(4):449–460. doi: 10.1111/j.1751-7915.2011.00258.x

  9. Sarmiento F, Peralta R, Blamey JM. Cold and Hot Extremozymes: Industrial Relevance and Current Trends. Front Bioeng Biotechnol. 2015;3:148. Published 2015 Oct 20. doi: 10.3389/fbioe.2015.00148

  10. Bjerga GE, Lale R, Williamson AK. Engineering low-temperature expression systems for heterologous production of cold-adapted enzymes. Bioengineered. 2016;7(1):33–38. doi: 10.1080/21655979.2015.1128589

  11. Piette F1, D'Amico S, Struvay C, Mazzucchelli G, Renaut J, Tutino ML, Danchin A, Leprince P, Feller G; Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125; Mol Microbiol. 2010 Apr;76(1):120-32. doi: 10.1111/j.1365-2958.2010.07084.x

  12. Trigger Factor from the Psychrophilic Bacterium Psychrobacter frigidicola Is a Monomeric Chaperone; Sylvain Robin, Denisio M. Togashi, Alan G. Ryder, J. Gerard Wall; Journal of Bacteriology Jan 2009, 191 (4) 1162-1168. doi: 10.1128/JB.01137-08

  13. Structure and function of the molecular chaperone Trigger Factor; Anja Hoffmann, Bernd Bukau, and Günter Kramer; Biochimica et Biophysica Acta (BBA) - Molecular Cell Research Volume 1803, Issue 6, June 2010, Pages 650-661. doi: 10.1016/j.bbamcr.2010.01.017

  14. ArcticExpress Competent Cells and ArcticExpress (DE3) Competent Cells (Instruction Manual Catalog #230191) ArcticExpress Competent Cells #230192 ArcticExpress (DE3) Competent Cells; Agilent Technologies;

  15. Click here for the original gel images