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Structural Insights into Ail-Mediated Adhesion in Yersinia pestis
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title
Structural Insights into Ail-Mediated Adhesion in Yersinia pestis
(English)
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main subject
structural biology
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Yersinia pestis
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author
Nicholas Noinaj
series ordinal
4
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Susan K Buchanan
series ordinal
9
object named as
Susan K Buchanan
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author name string
Satoshi Yamashita
series ordinal
1
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Petra Lukacik
series ordinal
2
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Travis J Barnard
series ordinal
3
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Suleyman Felek
series ordinal
5
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Tiffany M Tsang
series ordinal
6
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Eric S Krukonis
series ordinal
7
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B Joseph Hinnebusch
series ordinal
8
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publication date
9 November 2011
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published in
Structure
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volume
19
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issue
11
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page(s)
1672-82
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cites work
Crystal Structure of Neisserial Surface Protein A (NspA), a Conserved Outer Membrane Protein with Vaccine Potential
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The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence
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A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein
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20 March 2017
DaliLite workbench for protein structure comparison
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Outer Membrane Protein X (Ail) Contributes to Yersinia pestis Virulence in Pneumonic Plague and Its Activity Is Dependent on the Lipopolysaccharide Core Length
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Three Yersinia pestis Adhesins Facilitate Yop Delivery to Eukaryotic Cells and Contribute to Plague Virulence
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29 September 2017
Ail binding to fibronectin facilitates Yersinia pestis binding to host cells and Yop delivery
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Temperature and growth phase influence the outer-membrane proteome and the expression of a type VI secretion system in Yersinia pestis
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29 September 2017
The Yersinia pestis Ail protein mediates binding and Yop delivery to host cells required for plague virulence
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Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein
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29 September 2017
Human dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells.
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Resistance of Yersinia pestis to complement-dependent killing is mediated by the Ail outer membrane protein.
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29 September 2017
Phenotypic characterization of OmpX, an Ail homologue of Yersinia pestis KIM.
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29 September 2017
Resistance of Yersinia pestis to antimicrobial agents
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Adaptive response of Yersinia pestis to extracellular effectors of innate immunity during bubonic plague.
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29 September 2017
Attachment of Yersinia pestis to human respiratory cell lines is inhibited by certain oligosaccharides
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29 September 2017
Identification of regions of Ail required for the invasion and serum resistance phenotypes.
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29 September 2017
Characterization of the lipopolysaccharide of Yersinia pestis
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PubMed Central
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29 September 2017
Expression of plasminogen activator pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix.
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PubMed Central
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29 September 2017
Microbial adherence to and invasion through proteoglycans
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29 September 2017
Identification and characterization of an outer membrane protein, OmpX, in Escherichia coli that is homologous to a family of outer membrane proteins including Ail of Yersinia enterocolitica
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Structure and function of laminin: anatomy of a multidomain glycoprotein
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Mechanism of resistance to complement-mediated killing of bacteria encoded by the Salmonella typhimurium virulence plasmid gene rck
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29 September 2017
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29 September 2017
Modulation of virulence factor expression by pathogen target cell contact
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2 June 2018
On the mutations responsible for the rough phenotype of Escherichia coli B
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2 June 2018
Binding of extracellular matrix laminin to Escherichia coli expressing the Salmonella outer membrane proteins Rck and PagC.
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27 November 2018
Protease resistance and conformation of laminin.
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reference URL
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retrieved
27 November 2018
Identifiers
DOI
10.1016/J.STR.2011.08.010
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
820539
OpenCitations bibliographic resource ID
820539
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
820539
PMC publication ID
3217190
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
820539
PubMed publication ID
22078566
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
820539
ResearchGate publication ID
51794164
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