Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217. (Q30160110)

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English	Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.	scientific article

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217. (English)

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

object named as

Hagan Bayley

3

0 references

author name string

Lakmal Jayasinghe

1

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

George Miles

2

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

language of work or name

0 references

publication date

14 October 2005

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Europe PubMed Central

PubMed publication ID

8 June 2017

number of pages

10

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

8 June 2017

281

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

4

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

2195-2204

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

Beta-barrel membrane protein folding and structure viewed through the lens of alpha-hemolysin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Bacterial two-component and hetero-heptameric pore-forming cytolytic toxins: structures, pore-forming mechanism, and organization of the genes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Cooperative assembly of beta-barrel pore-forming toxins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

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

1 reference

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21 January 2018

Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Assembly of alpha-hemolysin on A431 cells leads to clustering of Caveolin-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Functional form of Caveolin-1 is necessary for the assembly of alpha-hemolysin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Caveolin-1 binding motif of alpha-hemolysin: its role in stability and pore formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions.

1 reference

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21 January 2018

The staphylococcal leukocidin bicomponent toxin forms large ionic channels

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Single-molecule imaging of cooperative assembly of -hemolysin on erythrocyte membranes

1 reference

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21 January 2018

Prepore for a breakthrough

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Arresting and releasing Staphylococcal α‐hemolysin at intermediate stages of pore formation by engineered disulfide bonds

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Staphylococcal alpha-toxin: the role of the N-terminus in formation of the heptameric pore -- a fluorescence study

1 reference

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21 January 2018

Functional engineered channels and pores (Review).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Stochastic sensors inspired by biology.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Single-molecule covalent chemistry with spatially separated reactants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Kinetics of a three-step reaction observed at the single-molecule level

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

A functional protein pore with a "retro" transmembrane domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Anthrax protective antigen: prepore-to-pore conversion

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Controlling pore assembly of staphylococcal gamma-haemolysin by low temperature and by disulphide bond formation in double-cysteine LukF mutants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Structural basis of pore formation by the bacterial toxin pneumolysin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Membrane insertion of the heptameric staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Natural-like function in artificial WW domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Directed evolution of a thermostable esterase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

A structural view of evolutionary divergence

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M510841200

21 January 2018

The heptameric prepore of a staphylococcal alpha-hemolysin mutant in lipid bilayers imaged by atomic force microscopy

1 reference

2 April 2022

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

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2 April 2022

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An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch

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2 April 2022

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Improved protocol for high-throughput cysteine scanning mutagenesis

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2 April 2022

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Restoration of pore-forming activity in staphylococcal alpha-hemolysin by targeted covalent modification

1 reference

2 April 2022

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Designed protein pores as components for biosensors

1 reference

2 April 2022

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Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus alpha-toxin in planar lipid bilayers

1 reference

2 April 2022

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Staphylococcal alpha-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages

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2 April 2022

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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

2 April 2022

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Kinetics of a reversible covalent-bond-forming reaction observed at the single-molecule level

1 reference

2 April 2022

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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

1 reference

2 April 2022

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Site-directed mutagenesis of the alpha-toxin gene of Staphylococcus aureus: role of histidines in toxin activity in vitro and in a murine model

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2 April 2022

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Stepwise growth of a single polymer chain

2 references

2 April 2022

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2 April 2022

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The role of the amino terminus in the kinetics and assembly of alpha-hemolysin of Staphylococcus aureus

1 reference

2 April 2022

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Identifiers

10.1074/JBC.M510841200

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

8 June 2017

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