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The American Society for Microbiology honors Marc Torrent
Date:6/18/2013

er, he showed that these results could be generalized to include other proteins and developed computational tools to identify antimicrobial domains. These studies revealed, once more, that aggregation properties could modulate the activity of antimicrobial peptides. Hence, he directed his efforts to understand whether antimicrobial peptides could be related to amyloid-prone proteins. Surprisingly, his results suggested that antimicrobial peptides might have arisen during evolution after cationization of amyloid-prone sequences.

Presently, Torrent is a Marie Curie fellow at the Medical Research Council, Laboratory of Molecular Biology in Cambridge, England, where he is investigating the regulatory roles of tRNAs. These studies can help to understand, among other questions, how viruses manipulate tRNA populations to favor translation of their own proteins.


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Contact: Garth Hogan
ghogan@asmusa.org
202-942-9389
American Society for Microbiology
Source:Eurekalert

Page: 1 2

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Mouse polyclonal antibody raised against a partial recombinant IFNA13. NCBI Entrez Gene ID = 3447...
Mouse polyclonal antibody raised against a partial recombinant NCLN. NCBI Entrez Gene ID = 56926...
...
Mouse monoclonal antibody raised against a partial recombinant WDR5. NCBI Entrez Gene ID = WDR5...
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