Asp2 and Asp3 Interact Directly with GspB, the Export Substrate of the Streptococcus gordonii Accessory Sec System
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Title
Asp2 and Asp3 Interact Directly with GspB, the Export Substrate of the Streptococcus gordonii Accessory Sec System
Authors
Keywords
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Journal
JOURNAL OF BACTERIOLOGY
Volume 193, Issue 13, Pages 3165-3174
Publisher
American Society for Microbiology
Online
2011-04-30
DOI
10.1128/jb.00057-11
References
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- (2009) Nina M. van Sorge et al. JOURNAL OF INFECTIOUS DISEASES
- Glycosylation and biogenesis of a family of serine-rich bacterial adhesins
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- SecB—A chaperone dedicated to protein translocation
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- Protein structure prediction on the Web: a case study using the Phyre server
- (2009) Lawrence A Kelley et al. Nature Protocols
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- (2008) A Keith Dunker et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- A Conserved C-Terminal 13-Amino-Acid Motif of Gap1 Is Required for Gap1 Function and Necessary for the Biogenesis of a Serine-Rich Glycoprotein of Streptococcus parasanguinis
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- Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis
- (2008) Yan Q. Xiong et al. MICROBIAL PATHOGENESIS
- A conserved domain of previously unknown function in Gap1 mediates protein-protein interaction and is required for biogenesis of a serine-rich streptococcal adhesin
- (2008) Yirong Li et al. MOLECULAR MICROBIOLOGY
- A new twist on an old pathway – accessory secretion systems
- (2008) Nathan W. Rigel et al. MOLECULAR MICROBIOLOGY
- Protein Translocation Across the Bacterial Cytoplasmic Membrane
- (2007) Arnold J.M. Driessen et al. Annual Review of Biochemistry
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