Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes (Q30168584)

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English	Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes (English)

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

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author name string

A P Heuck

1

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

E M Hotze

2

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

R K Tweten

3

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

A E Johnson

4

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Europe PubMed Central

PubMed publication ID

9 June 2017

publication date

1 November 2000

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Europe PubMed Central

PubMed publication ID

9 June 2017

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Europe PubMed Central

PubMed publication ID

9 June 2017

6

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Europe PubMed Central

PubMed publication ID

9 June 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

1233-1242

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Extension of the parallax analysis of membrane penetration depth to the polar region of model membranes: use of fluorescence quenching by a spin-label attached to the phospholipid polar headgroup

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Cholesterol-dependent tetanolysin damage to liposomes

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Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids

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Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel.

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Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore.

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Streptolysin O: inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation

1 reference

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Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae.

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Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae

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The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane

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Fluoresceinthiocarbamyl-insulin: a potential analytical tool for the assay of disulfide bond reduction

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Effect of isolated C-terminal fragment of theta-toxin (perfringolysin O) on toxin assembly and membrane lysis

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Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes

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Structure and mechanism of carbonic anhydrase

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Interaction of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion

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Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel

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Kinetics of Streptolysin O Self-Assembly

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Crystal structure of the anthrax toxin protective antigen

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Interaction of streptolysin O with sterols

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Effect of streptolysin O and digitonin on egg lecithin/cholesterol vesicles

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Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form

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The Mechanism of Membrane Insertion for a Cholesterol-Dependent Cytolysin

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Identification of a Membrane-Spanning Domain of the Thiol-Activated Pore-Forming ToxinClostridium perfringensPerfringolysin O: An α-Helical to β-Sheet Transition Identified by Fluorescence Spectroscopy†

1 reference

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The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins

1 reference

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Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: significant homology with the genes for streptolysin O and pneumolysin

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Identifiers

10.1016/S1097-2765(00)00119-2

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

ResearchGate publication ID

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