A Virulence Locus of Pseudomonas aeruginosa Encodes a Protein Secretion Apparatus
By J. D. Mougous, M. Cuff, S. Raunser, A. Shen, Min Zhou, Casey A. Gifford, A. Goodman, G. Joachimiak, C. Ordoñez, S. Lory and 3 more. Science, 2006
1,122 citations recorded by the source corpus.
Subfields: Endocrinology, Molecular Biology, Molecular Medicine
View Paper: https://www.semanticscholar.org/paper/74ded404b081da04b84489576fd411ecbb0c6e13
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In Endocrinology
In Molecular Biology
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- Jung Hun Lee
- Jinhu Huang
- Chang-Ro Lee
- Stephen K. Burley
In Molecular Medicine
Citations in the corpus
- A Type VI Secretion System of Pseudomonas aeruginosa Targets a Toxin to Bacteria (2010, positive): “Western blotting was performed as described previously (Mougous et al., 2006), with the exception that detection of the Tse proteins required primary antibody incubation in 5% BSA in Tris-buffered saline containing 0.05% v/v Tween 20 (TBST).”
- Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin (2009, background): “The ClpV protein channel as well as other proteins in the T6SS machine are responsible for translocation of Hcp across the bacterial cell envelope to the external milieu (4).”
- Biology of Acinetobacter baumannii: Pathogenesis, Antibiotic Resistance Mechanisms, and Prospective Treatment Options (2017, background): “Many bacteria use the T6SS to inject effector proteins, providing a colonization advantage during infection of eukaryotic hosts (Mougous et al., 2006) or to kill competing bacteria (Basler et al.”
- Protein Injection Machines in Bacteria (2018, positive): “The inner tube is primarily composed of a stack of Hcp hexamers forming a 1,000 nm tubular structure capped at its membrane-proximal end by a trimer of VgrG, a structure equivalent to the bacteriophage T4 cell-puncturing device (Leiman et al., 2009; Mougous et al., 2006).”
- Type VI secretion requires a dynamic contractile phage tail-like structure (2012, positive): “cholerae , VipA and VipB, form tubular structures that can be depolymerized by another T6SS gene product, Clp”
- The Hcp proteins fused with diverse extended-toxin domains represent a novel pattern of antibacterial effectors in type VI secretion systems (2017, background): “for both the assembly of a functional T6SS and the export of its effectors.(22,23,26,43) Crystallographic data of Hcp homologs showed that the protein forms hexameric rings, which can stack into a tube.”
- Bacterial Secretion Systems – An overview (2016, background): “T6SSs are the most recent bacterial secretion systems to be discovered (99), and therefore, there is still much to learn about their structure and functions.”