Archaeal cell surface biogenesis
Author:
Affiliation:
1. Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA
2. Computational Biology Group, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
Funder
University of Pennsylvania Research Foundation
National Science Foundation
Deutsche Forschungsgemeinschaft
Max Planck Society
Publisher
Oxford University Press (OUP)
Subject
Infectious Diseases,Microbiology
Link
http://academic.oup.com/femsre/article-pdf/42/5/694/25886320/fuy027.pdf
Reference279 articles.
1. Permuting the PGF signature motif blocks both archaeosortase-dependent C-terminal cleavage and prenyl lipid attachment for the Haloferax volcanii S-layer glycoprotein;Abdul Halim;J Bacteriol,2016
2. Haloferax volcanii archaeosortase is required for motility, mating, and C-terminal processing of the S-layer glycoprotein;Abdul Halim;Mol Microbiol,2013
3. Conserved residues are critical for Haloferax volcanii archaeosortase catalytic activity: Implications for convergent evolution of the catalytic mechanisms of non-homologous sortases from archaea and bacteria;Abdul Halim;Mol Microbiol,2018
4. ArtA-dependent processing of a tat substrate containing a conserved tripartite structure that is not localized at the C terminus;Abdul Halim;J Bacteriol,2017
5. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer;Abu-Qarn;J Mol Biol,2007
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