about
Crystal structure of a complex between anthrax toxin and its host cell receptorStructure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formationEvidence against a human cell-specific role for LRP6 in anthrax toxin entryReceptor-specific requirements for anthrax toxin delivery into cellsSusceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factorCholesterol-dependent cytolysins, a family of versatile pore-forming toxinsOnset of anthrax toxin pore formationBinary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteinsAnthrax vaccine design: strategies to achieve comprehensive protection against spore, bacillus, and toxinRatcheting up protein translocation with anthrax toxinThe Protective Antigen Component of Anthrax Toxin Forms Functional Octameric ComplexesDomain 4 of the anthrax protective antigen maintains structure and binding to the host receptor CMG2 at low pHEvidence That Histidine Protonation of Receptor-Bound Anthrax Protective Antigen Is a Trigger for Pore FormationAnthrax toxin protective antigen integrates poly- -D-glutamate and pH signals to sense the optimal environment for channel formationDomain Flexibility Modulates the Heterogeneous Assembly Mechanism of Anthrax Toxin Protective AntigenAlternative pre-approved and novel therapies for the treatment of anthraxInhibition of axotomy-induced neuronal apoptosis by extracellular delivery of a Bcl-XL fusion proteinCathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasmRole of N-terminal His6-Tags in binding and efficient translocation of polypeptides into cells using anthrax protective antigen (PA)The Disulfide Bond Cys255-Cys279 in the Immunoglobulin-Like Domain of Anthrax Toxin Receptor 2 Is Required for Membrane Insertion of Anthrax Protective Antigen PoreA protective antigen mutation increases the pH threshold of anthrax toxin receptor 2-mediated pore formationMonitoring the kinetics of the pH-driven transition of the anthrax toxin prepore to the pore by biolayer interferometry and surface plasmon resonance.Membrane damage by an α-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered stepsGRP78(BiP) facilitates the cytosolic delivery of anthrax lethal factor (LF) in vivo and functions as an unfoldase in vitro.Solubilization and characterization of the anthrax toxin pore in detergent micellesPreventing voltage-dependent gating of anthrax toxin channels using engineered disulfides.Identification of a prepore large-complex stage in the mechanism of action of Clostridium perfringens enterotoxinRole of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membraneMonomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin.Point mutations in anthrax protective antigen that block translocation.GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore.Anthrax sub-unit vaccine: the structural consequences of binding rPA83 to Alhydrogel®.Thermodynamic measurements of bilayer insertion of a single transmembrane helix chaperoned by fluorinated surfactants.Designing a polyvalent inhibitor of anthrax toxin.Anthrax toxin receptor 2 determinants that dictate the pH threshold of toxin pore formationOptimization of protease-inhibitor interactions by randomizing adventitious contactsImmunogenicity of Bacillus anthracis protective antigen domains and efficacy of elicited antibody responses depend on host genetic background.Neutralizing monoclonal antibodies directed against defined linear epitopes on domain 4 of anthrax protective antigenDisulfide bonds in the ectodomain of anthrax toxin receptor 2 are required for the receptor-bound protective-antigen pore to function.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Anthrax protective antigen: prepore-to-pore conversion.
@ast
Anthrax protective antigen: prepore-to-pore conversion.
@en
type
label
Anthrax protective antigen: prepore-to-pore conversion.
@ast
Anthrax protective antigen: prepore-to-pore conversion.
@en
prefLabel
Anthrax protective antigen: prepore-to-pore conversion.
@ast
Anthrax protective antigen: prepore-to-pore conversion.
@en
P356
P1433
P1476
Anthrax protective antigen: prepore-to-pore conversion.
@en
P2093
C J Miller
J L Elliott
P304
10432-10441
P356
10.1021/BI990792D
P407
P577
1999-08-01T00:00:00Z