Andrew J. Darwin
Affiliations: | Biology | New York University, New York, NY, United States |
Area:
Microbiology BiologyGoogle:
"Andrew Darwin"Children
Sign in to add trainee| Michelle Maxson | research assistant | 2001-2005 | NYU Langone (ImmunoTree) |
| Grace L. Axler-DiPerte | grad student | 2007 | NYU |
| Nancy K. Horstman | grad student | 2011 | NYU |
| Saori Yamaguchi | grad student | 2013 | NYU |
| Josue Flores-Kim | grad student | 2014 | NYU |
| Erwan Gueguen | post-doc | 2008-2012 | NYU |
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Publications
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| Hsu HC, Wang M, Kovach A, et al. (2022) Pseudomonas aeruginosa C-Terminal Processing Protease CtpA Assembles into a Hexameric Structure That Requires Activation by a Spiral-Shaped Lipoprotein-Binding Partner. Mbio. e0368021 |
| Chung S, Darwin AJ. (2020) The C-terminus of substrates is critical but not sufficient for their degradation by the CtpA protease. Journal of Bacteriology |
| Srivastava D, Seo J, Rimal B, et al. (2018) A Proteolytic Complex Targets Multiple Cell Wall Hydrolases in Pseudomonas aeruginosa. Mbio. 9 |
| Srivastava D, Moumene A, Flores-Kim J, et al. (2017) Psp Stress Response Proteins Form a Complex with Mislocalized Secretins in the Yersinia enterocolitica Cytoplasmic Membrane. Mbio. 8 |
| Flores-Kim J, Darwin AJ. (2016) Interactions between the cytoplasmic domains of PspB and PspC silence the Yersinia enterocolitica phage shock protein response. Journal of Bacteriology |
| Flores-Kim J, Darwin AJ. (2016) The Phage Shock Protein Response. Annual Review of Microbiology |
| Rajkovic A, Witzky A, Navarre W, et al. (2015) Elongation factor-P at the crossroads of the host-endosymbiont interface. Microbial Cell (Graz, Austria). 2: 360-362 |
| Rau R, Darwin AJ. (2015) Identification of YsaP, the Pilotin of the Yersinia enterocolitica Ysa Type III Secretion System. Journal of Bacteriology. 197: 2770-9 |
| Rajkovic A, Erickson S, Witzky A, et al. (2015) Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa. Mbio. 6: e00823 |
| Flores-Kim J, Darwin AJ. (2015) Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners. The Journal of Biological Chemistry. 290: 11417-30 |