Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin.
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The role of hydrophobic interactions in positioning of peripheral proteins in membranesThe cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyObstructing toxin pathways by targeted pore blockagePerfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsMembrane assembly of the cholesterol-dependent cytolysin pore complex.Listeriolysin O as cytotoxic component of an immunotoxinStructures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysinsOnly two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.Listeria pathogenesis and molecular virulence determinantsSeeligeriolysin O, a cholesterol-dependent cytolysin of Listeria seeligeri, induces gamma interferon from spleen cells of mice.The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cellsStructural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family.Perfringolysin O: The Underrated Clostridium perfringens Toxin?Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions.Mini-review: novel therapeutic strategies to blunt actions of pneumolysin in the lungsSpecific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysinProtein arcs may form stable pores in lipid membranes.Clostridial toxins.Insights into structure and activity of natural compound inhibitors of pneumolysin.Biological activities of suilysin: role in Streptococcus suis pathogenesis.Dissociated linkage of cytokine-inducing activity and cytotoxicity to different domains of listeriolysin O from Listeria monocytogenes.Immunization with genetic toxoids of the Arcanobacterium pyogenes cholesterol-dependent cytolysin, pyolysin, protects mice against infection.Differential interaction of equinatoxin II with model membranes in response to lipid composition.The Crystal Structure of Pneumolysin at 2.0 Å Resolution Reveals the Molecular Packing of the Pre-pore Complex.Experimental design approach in recombinant protein expression: determining medium composition and induction conditions for expression of pneumolysin from Streptococcus pneumoniae in Escherichia coli and preliminary purification process.Structure-function studies of tryptophan mutants of equinatoxin II, a sea anemone pore-forming proteinThe conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding.The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains.The human-specific action of intermedilysin, a homolog of streptolysin O, is dictated by domain 4 of the protein.Molecular architecture of the bipartite fusion loops of vesicular stomatitis virus glycoprotein G, a class III viral fusion protein.A simple and rapid method to measure cholesterol binding to P450s and other proteins.Separation of a cholesterol-enriched microdomain involved in T-cell signal transduction.Interaction of Cholesterol with Perfringolysin O: What Have We Learned from Functional Analysis?Cysteine-scanning mutagenesis of an eukaryotic pore-forming toxin from sea anemone: topology in lipid membranes.A model for hydrophobic protrusions on peripheral membrane proteins
P2860
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P2860
Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Contribution of individual try ...... cholesterol-binding cytolysin.
@en
Contribution of individual try ...... cholesterol-binding cytolysin.
@nl
type
label
Contribution of individual try ...... cholesterol-binding cytolysin.
@en
Contribution of individual try ...... cholesterol-binding cytolysin.
@nl
prefLabel
Contribution of individual try ...... cholesterol-binding cytolysin.
@en
Contribution of individual try ...... cholesterol-binding cytolysin.
@nl
P2093
P2860
P1433
P1476
Contribution of individual try ...... cholesterol-binding cytolysin.
@en
P2093
K I Mitsui
M Nakamura
N Sekino-Suzuki
Y Ohno-Iwashita
P2860
P304
P356
10.1111/J.1432-1033.1996.00941.X
P407
P577
1996-11-01T00:00:00Z