IndraLab

Statements



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"First, SLO binds to membrane cholesterol and then it is oligomerized to form a pre-pore state and inserted into the lipid bilayer [33-35]."

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"SLO monomers bind to cholesterol on the plasma membrane, followed by oligomerization, insertion into the lipid bilayer, and formation of a protein lined pore of about 30 nm in diameter."

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"This indicates that the enzymatic oxidation of cholesterol in the lipid bilayer did not progress during 30 min, probably because DTT-activate SLO interacted with cholesterol more strongly than cholest[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The pore forming toxin SLO binds to cholesterol molecules present on the eukaryotic cell membrane to create pores and cause cell lysis [XREF_BIBR]."

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"The SLO and cholesterol complex induced the chemokine production in proportion to the residual hemolytic activity of the complex."

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"Our observation of YFP-GPI partitioning into SLO induced endosomes (XREF_FIG) and the fact that SLO interacts with membrane cholesterol during pore formation suggested a role for cholesterol rich membrane domains in this endocytic mechanism."

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"Like other thiol activated cytolysins, SLO binds to cholesterol present in eukaryotic cell membranes, where it oligomerizes to form transmembrane pores (Sekiya et al., 1993; Palmer et al. 1998)."

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"SLO binds to cholesterol in cell membranes, forms large 30 nm diameter pores (versus 1-2 nm pores for Cry PFTs), and is an important virulence factor of human-pathogenic streptococci XREF_BIBR."

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"The effect of the delivery method using streptolysin O (SLO), however, needs to be determined, since SLO binds to cholesterol molecules on cell plasma membrane which may cause damages to cell membrane [XREF_BIBR, XREF_BIBR]."

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"SLO can bind cholesterol in the plasma membrane at low temperature (4°C) and form pores in the membrane to allow the permeabilization of biomolecules into cells at high temperature (37°C)."

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"In this study we explore the role for cholesterol binding by SLO in CMT by extracting it from the membrane and by mutating SLO 's cholesterol recognition motif."

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"At 4degreesC, SLO binds to cholesterol in the plasma membrane."

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"Removal of the maltose binding protein from the SLO fusion products increases the order of the monolayer array of biotinylated SLO bound to cholesterol crystals."

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"SLO binds to cholesterol in the plasma membrane and oligomerizes to form ~ 30-nm-diameter pores."
| PMC

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"The rate of SLO diffusion is suggested to be slower than that of SLO binding to cholesterol."

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"Cholesterol binding to BK channel-forming proteins involves the central tyrosine of a CRAC domain located at the channel core-cytosolic tail interface."

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"A possible explanation for these findings is that cholesterol enriched microdomains containing glycosphingolipids in the erythrocyte membrane become occupied by tightly stacked lectin molecules, blocking the interaction between cholesterol and SLO that would otherwise result in penetration of the membrane."

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"Since a linear relationship between P 30 min and the fraction of cholesterol in a lipid bilayer is maintained as far as P 30 min is above 0.3, the leveling off of P 30 min after 30 min can not be expl[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"