Zobrazeno 1 - 5
of 5
pro vyhledávání: '"William A. Furin"'
Autor:
D Joseph Sexton, Ausaf Ahmad, Judith Noble-Wang, Kaitlin Forsberg, Anastasia P. Litvintseva, William A Furin, Stephanie R. Black, Tristan D. McPherson, Gordana Derado, Massimo Pacilli, Meghan L Bentz, Brendan R Jackson, Rory M. Welsh, Sarah K Kemble, Owen Herzegh, Laura J. Rose
Publikováno v:
Clinical Infectious Diseases: An Official Publication of the Infectious Diseases Society of America
Background Candida auris is an emerging multidrug-resistant yeast that contaminates healthcare environments causing healthcare-associated outbreaks. The mechanisms facilitating contamination are not established. Methods C. auris was quantified in res
Autor:
Judith Noble-Wang, Laura J. Rose, Lisa H Tran, William A Furin, Monica Y Chan, Amanda K Lyons
Publikováno v:
Infection Control & Hospital Epidemiology. 43:1492-1494
Sponges and swabs were evaluated for their ability to recover Candida auris dried 1 hour on steel and plastic surfaces. Culture recovery ranged from 50% recovery (swabs), indicating that cells may enter a viable but nonculturable state.
Autor:
William A, Furin, Lisa H, Tran, Monica Y, Chan, Amanda K, Lyons, Judith, Noble-Wang, Laura J, Rose
Publikováno v:
Infection control and hospital epidemiology. 43(10)
Sponges and swabs were evaluated for their ability to recover
A protocol for the production of recombinant spider silk-like proteins for artificial fiber spinning
Autor:
Randolph V. Lewis, Daniela Bittencourt, William A. Furin, Elíbio L. Rech, Amanda E. Brooks, Florence Teulé, Alyssa R. Cooper
Publikováno v:
Nature Protocols. 4:341-355
The extreme strength and elasticity of spider silks originate from the modular nature of their repetitive proteins. To exploit such materials and mimic spider silks, comprehensive strategies to produce and spin recombinant fibrous proteins are necess
Publikováno v:
Journal of Materials Science. 42:8974-8985
Bacteria were genetically engineered to produce two spider silk protein variants composed of basic repeat units combining a flagelliform elastic motif ([GPGGX]4) and a major ampullate silk strength motif ([linker/poly-alanine]. The secondary structur