Kevin Young Microbiology and Immunology, University of Arkansas for Medical Sciences, USA
1 protocol

Gang Li
  • Microbiology and Immunology, University of Arkansas for Medical Sciences, USA
Research focus
  • Microbiology
  • 1 Author merit

Education

Ph.D. in Microbiology, University of Saskatchewan, Saskatoon, Canada, 2009

Current position

Postdoctoral Research Associate, Department of Microbiology & Immunology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA 72205-7199

Publications

  1. Li, G. and Young, K. D. (2012). Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol Microbiol 84(2): 276-295.
  2. Strozen, T. G., Li, G. and Howard, S. P. (2012). YghG (GspSbeta) is a novel pilot protein required for localization of the GspSbeta type II secretion system secretin of enterotoxigenic Escherichia coli. Infect Immun 80(8): 2608-2622.
  3. Li, G., Miller, A., Bull, H. and Howard, S. P. (2011). Assembly of the type II secretion system: identification of ExeA residues critical for peptidoglycan binding and secretin multimerization. J Bacteriol 193(1): 197-204.
  4. Li, G. and Howard, S. P. (2010). ExeA binds to peptidoglycan and forms a multimer for assembly of the type II secretion apparatus in Aeromonas hydrophila. Mol Microbiol 76(3): 772-781.
  5. Howard, S. P., Gebhart, C., Langen, G. R., Li, G. and Strozen, T. G. (2006). Interactions between peptidoglycan and the ExeAB complex during assembly of the type II secretin of Aeromonas hydrophila. Mol Microbiol 59(3): 1062-1072.
  6. Schoenhofen, I. C., Li, G., Strozen, T. G. and Howard, S. P. (2005). Purification and characterization of the N-terminal domain of ExeA: a novel ATPase involved in the type II secretion pathway of Aeromonas hydrophila. J Bacteriol 187(18): 6370-6378.
1 Protocol published
Isolation of Inner Membrane Vesicles from Escherichia coli by Using an Affinity Tag
Authors:  Gang Li and Kevin D. Young, date: 10/20/2012, view: 7347, Q&A: 0
This protocol was developed in a project aimed to identify the inner membrane proteins localizing to cell poles in Escherichia coli (E. coli). By using a known polar protein Tar as a tag, we isolated pole-derived inner membrane ...
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