Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin. (Q41064610)

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15 October 2019

title

Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin (English)

1 reference

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15 October 2019

main subject

transmembrane protein

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author

Hagan Bayley

5

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15 October 2019

author name string

Valeva A

1

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15 October 2019

Weisser A

2

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15 October 2019

Walker B

3

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15 October 2019

Kehoe M

4

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15 October 2019

Bhakdi S

6

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15 October 2019

Palmer M

7

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15 October 2019

language of work or name

English

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publication date

1 April 1996

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15 October 2019

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15 October 2019

volume

15

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15 October 2019

issue

8

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15 October 2019

page(s)

1857-1864

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A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes

15 October 2019

cites work

1 reference

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Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation

26 September 2017

1 reference

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Triggers and switches in a self-assembling pore-forming protein

26 September 2017

1 reference

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Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore

26 September 2017

1 reference

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Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis

26 September 2017

1 reference

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Primary sequence of the alpha-toxin gene from Staphylococcus aureus wood 46.

26 September 2017

1 reference

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Correlation between toxin binding and hemolytic activity in membrane damage by staphylococcal alpha-toxin.

26 September 2017

1 reference

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Expression of a cloned Staphylococcus aureus alpha-hemolysin determinant in Bacillus subtilis and Staphylococcus aureus

26 September 2017

1 reference

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Staphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles

26 September 2017

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On the mechanism of membrane damage by Staphylococcus aureus alpha-toxin

26 September 2017

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Calculation of protein extinction coefficients from amino acid sequence data

26 September 2017

1 reference

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Alpha-toxin of Staphylococcus aureus

26 September 2017

1 reference

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Solubilization of membranes by detergents

26 September 2017

1 reference

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A pore-forming protein with a metal-actuated switch.

26 September 2017

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Lipid-induced polymerization of staphylococcal -toxin.

14 June 2018

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Fluorescence energy transfer distance measurements using site-directed single cysteine mutants. The membrane insertion of colicin A.

14 June 2018

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Colicin E1 binding to membranes: time-resolved studies of spin-labeled mutants

14 June 2018

1 reference

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Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification.

19 August 2018

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Synthesis, spectral properties, and use of 6-acryloyl-2-dimethylaminonaphthalene (Acrylodan). A thiol-selective, polarity-sensitive fluorescent probe

19 August 2018

1 reference

12 December 2020

Secondary structure and assembly mechanism of an oligomeric channel protein

1 reference

12 December 2020

Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis

1 reference

12 December 2020

Functional complementation of staphylococcal alpha-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loop

1 reference

12 December 2020

Staphylococcus aureus alpha-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cysteine at positions 69, 130, and 186

1 reference

12 December 2020

Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin

1 reference

12 December 2020

Identification of a putative membrane-inserted segment in the alpha-toxin of Staphylococcus aureus

1 reference

12 December 2020

Surface labeling of key residues during assembly of the transmembrane pore formed by staphylococcal alpha-hemolysin

1 reference

12 December 2020

Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal alpha-toxin into the lipid bilayer

1 reference

12 December 2020

10.1002/J.1460-2075.1996.TB00536.X

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8617232%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8617232%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

PubMed publication ID

8617232

1 reference