Structure-function analysis of invasion plasmid antigen C (IpaC) from Shigella flexneri.

scientific article published on 8 November 2002

Structure-function analysis of invasion plasmid antigen C (IpaC) from Shigella flexneri. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M208383200
P698PubMed publication ID12427760

P50authorLisa A KueltzoQ47653582
P2093author name stringJeff Barker
C Russell Middaugh
Wendy L Picking
William D Picking
Baran Ersoy
John Osiecki
P2860cites workIntrinsically disordered proteinQ28191444
Intrinsic disorder and protein functionQ29616415
Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri.Q32044872
The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cellsQ33552436
The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranesQ33878820
Interaction of Shigella flexneri IpaC with model membranes correlates with effects on cultured cellsQ39516559
Cdc42 facilitates invasion but not the actin-based motility of ShigellaQ40748370
Protein-protein interactions in the assembly of Shigella flexneri invasion plasmid antigens IpaB and IpaC into protein complexesQ40977835
IpaC from Shigella and SipC from Salmonella possess similar biochemical properties but are functionally distinctQ41474021
Interaction of partially structured states of acidic fibroblast growth factor with phospholipid membranesQ41666435
IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cellsQ42206130
Direct nucleation and bundling of actin by the SipC protein of invasive SalmonellaQ42680869
Shigella invasion of macrophage requires the insertion of IpaC into the host plasma membrane. Functional analysis of IpaC.Q43645358
Collective efforts to modulate the host actin cytoskeleton by Salmonella type III-secreted effector proteinsQ50112147
The Salmonella type III secretion translocon protein SspC is inserted into the epithelial cell plasma membrane upon infectionQ50119640
Estimation of globular protein secondary structure from circular dichroism.Q51259487
A self-consistent method for the analysis of protein secondary structure from circular dichroism.Q52400789
Cloning, expression, and affinity purification of recombinant Shigella flexneri invasion plasmid antigens IpaB and IpaC.Q54576324
Variable selection method improves the prediction of protein secondary structure from circular dichroism spectraQ68554855
Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopyQ72565266
Purification of IpaC, a protein involved in entry of Shigella flexneri into epithelial cells and characterization of its interaction with lipid membranesQ72991854
Preincubation of recombinant Ipa proteins of Shigella sonnei promotes entry of non-invasive Escherichia coli into HeLa cellsQ73031664
Identification of functional regions within invasion plasmid antigen C (IpaC) of Shigella flexneriQ73312849
Coiled-coil domains in proteins secreted by type III secretion systemsQ73663925
Characterization of the interaction of IpaB and IpaD, proteins required for entry of Shigella flexneri into epithelial cells, with a lipid membraneQ74261400
P433issue5
P407language of work or nameEnglishQ1860
P921main subjectShigella flexneriQ1644417
P304page(s)2792-2798
P577publication date2002-11-08
P1433published inJournal of Biological ChemistryQ867727
P1476titleStructure-function analysis of invasion plasmid antigen C (IpaC) from Shigella flexneri
P478volume278

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cites work (P2860)
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Q30481246Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella
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Q38853686Detergent Isolation Stabilizes and Activates the Shigella Type III Secretion System Translocator Protein IpaC.
Q41876888Evaluation of the physical stability of the EC5 domain of E-cadherin: effects of pH, temperature, ionic strength, and disulfide bonds
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Q27677178The Structures of Coiled-Coil Domains from Type III Secretion System Translocators Reveal Homology to Pore-Forming Toxins
Q37781063Uncivil engineers: Chlamydia, Salmonella and Shigella alter cytoskeleton architecture to invade epithelial cells.
Q41433693YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis

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