Sequential unfolding of the hemolysin two-partner secretion domain from P roteus mirabilis
Author:
Affiliation:
1. Department of Chemistry and Biochemistry; University Wisconsin - La Crosse; La Crosse Wisconsin 54601
2. Department of Chemistry; Wabash College; Crawfordsville Indiana 47933
Funder
National Science Foundation Grants
University Wisconsin - La Crosse Faculty Research Grant
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2791/fullpdf
Reference58 articles.
1. Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins;Jacob-Dubuisson;Mol Microbiol,2001
2. Activation of Serratia marcescens hemolysin through a conformational change;Walker;Infect Immun,2004
3. The filamentous haemagglutinin, a multifaceted adhesion produced by virulent Bordetella spp;Locht;Mol Microbiol,1993
4. A prototype two-partner secretion pathway: the Haemophilus influenzae HMW1 and HMW2 adhesin systems;Geme;Trends Microbiol,2009
5. Cytotoxic activity of the Proteus hemolysin HpmA;Swihart;Infect Immun,1990
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1. Corrigendum to “Sequential unfolding of the hemolysin two‐partner secretion domain from Proteus mirabilis ”;Protein Science;2019-08-21
2. Pathogenesis of Proteus mirabilis Infection;EcoSal Plus;2018-02-08
3. Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions;Frontiers in Cellular and Infection Microbiology;2017-05-09
4. Proteolysis of truncated hemolysin A yields a stable dimerization interface;Acta Crystallographica Section F Structural Biology Communications;2017-02-21
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