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  • 1
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    Supramolecular structure of the Salmonella typhimurium type III protein secretion system (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: The type III secretion system of Salmonella typhimurium directs the translocation of proteins into host cells. Evolutionarily related to the flagellar assembly machinery, this system is also present in other pathogenic bacteria, but its organization is unknown. Electron microscopy revealed supramolecular structures spanning the inner and outer membranes of flagellated and nonflagellated strains; such structures were not detected in strains carrying null mutations in components of the type III apparatus. Isolated structures were found to contain at least three proteins of this secretion system. Thus, the type III apparatus of S. typhimurium, and presumably other bacteria, exists as a supramolecular structure in the bacterial envelope.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kubori, T -- Matsushima, Y -- Nakamura, D -- Uralil, J -- Lara-Tejero, M -- Sukhan, A -- Galan, J E -- Aizawa, S I -- New York, N.Y. -- Science. 1998 Apr 24;280(5363):602-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biosciences, Teikyo University, 1-1 Toyosatodai, Utsunomiya 320, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9554854" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/analysis ; Bacterial Proteins/*analysis/chemistry/*metabolism/ultrastructure ; Cell Membrane/chemistry/ultrastructure ; Centrifugation, Density Gradient ; Macromolecular Substances ; Membrane Proteins/*analysis/chemistry/ultrastructure ; *Membrane Transport Proteins ; Microscopy, Electron ; Microscopy, Immunoelectron ; Porins/analysis ; Salmonella typhimurium/*chemistry/metabolism/*ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Structural insights into the assembly of the type III secretion needle complex (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-06
    Description: Type III secretion systems (TTSSs) mediate translocation of virulence factors into host cells. We report the 17-angstrom resolution structures of a central component of Salmonella typhimurium TTSS, the needle complex, and its assembly precursor, the bacterial envelope-anchored base. Both the base and the fully assembled needle complex adopted multiple oligomeric states in vivo, and needle assembly was accompanied by recruitment of the protein PrgJ as a structural component of the base. Moreover, conformational changes during needle assembly created scaffolds for anchoring both PrgJ and the needle substructure and may provide the basis for substrate-specificity switching during type III secretion.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1459965/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1459965/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marlovits, Thomas C -- Kubori, Tomoko -- Sukhan, Anand -- Thomas, Dennis R -- Galan, Jorge E -- Unger, Vinzenz M -- AI30492/AI/NIAID NIH HHS/ -- GM35433/GM/NIGMS NIH HHS/ -- GM66145/GM/NIGMS NIH HHS/ -- P42 RR-01081/RR/NCRR NIH HHS/ -- R01 GM066145/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 5;306(5698):1040-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520-8024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528446" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/*ultrastructure ; Cryoelectron Microscopy ; Macromolecular Substances ; Membrane Transport Proteins/chemistry/ultrastructure ; Salmonella typhimurium/chemistry/*ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
    Electronic Resource
    Electronic Resource
    The invasion-associated type III secretion system of Salmonella typhimurium: common and unique features (2000)
    Springer
    Cellular and molecular life sciences 57 (2000), S. 1033-1049 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Type III secretion; S. typhimurium; bacterial invasion; bacterial pathogenicity.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Several bacterial pathogens make use of a specialized protein secretion system to inject effector proteins into host cells. This system, commonly referred to as type III secretion, is always associated with phenotypes related to intimate interactions between the pathogen and its respective host cells. The enteric pathogen Salmonella typhimurium utilizes a type III secretion system to invade nonphagocytic intestinal epithelial cells. Whereas the invasion-associated type III system of S. typhimurium has evolved to perform a specific function, many of the components of this system are conserved among the type III systems of other bacterial pathogens. This review will discuss the common and unique features of the S. typhimurium system in relation to the type III systems of other human pathogens. Topics discussed include the phenotypes associated with various type III systems, the genetic loci encoding these systems, the components of the type III secretion apparatus, the effector proteins and the mechanisms by which they enter host cells as well as the mechanisms used to regulate the expression of type III systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00000743
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  • 4
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    Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system (2000)
    National Academy of Sciences
    Details
    Publication Date: 2000-08-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 5
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    The invasion-associated type III secretion system of Salmonella typhimurium: common and unique features (2000)
    Springer
    Details
    Publication Date: 2000-07-01
    Print ISSN: 1420-682X
    Electronic ISSN: 1420-9071
    Topics: Biology , Medicine
    Published by Springer
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