(Q24634854)

English

Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components

scientific article

Crystal structure of the octameric pore of staphylococcal -hemolysin reveals the -barrel pore formation mechanism by two components
Crystal structure of the octameric pore of staphylococcal -hemolysin reveals the -barrel pore formation mechanism by two components

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scholarly article

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Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components (English)

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crystal structure

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Keitaro Yamashita

object named as

Keitaro Yamashita

1

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object named as

Makoto Ohta

7

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author name string

Yuka Kawai

2

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Yoshikazu Tanaka

3

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Nagisa Hirano

4

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Jun Kaneko

5

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Noriko Tomita

6

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Yoshiyuki Kamio

8

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Min Yao

9

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Isao Tanaka

10

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language of work or name

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publication date

18 October 2011

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Proceedings of the National Academy of Sciences of the United States of America

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108

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42

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17314-9

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Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

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://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

7 April 2017

Pore formation: an ancient yet complex form of attack.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Toward single molecule DNA sequencing: direct identification of ribonucleoside and deoxyribonucleoside 5'-monophosphates by using an engineered protein nanopore equipped with a molecular adapter

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Cooperative assembly of beta-barrel pore-forming toxins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Pore-forming protein toxins: from structure to function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Retrieving biological activity from LukF-PV mutants combined with different S components implies compatibility between the stem domains of these staphylococcal bicomponent leucotoxins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Assembly of macromolecular pores by immune defense systems

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

27 September 2017

Analysis of the specificity of Panton-Valentine leucocidin and gamma-hemolysin F component binding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

30 May 2018

Engineered covalent leucotoxin heterodimers form functional pores: insights into S-F interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

30 May 2018

Protein engineering modulates the transport properties and ion selectivity of the pores formed by staphylococcal gamma-haemolysins in lipid membranes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

30 May 2018

Channel-forming toxins: tales of transformation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3198349

30 May 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/10.1073%2FPNAS.1110402108

21 January 2018

Single-molecule visualization of environment-sensitive fluorophores inserted into cell membranes by staphylococcal gamma-hemolysin

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

Essential residues, W177 and R198, of LukF for phosphatidylcholine-binding and pore-formation by staphylococcal gamma-hemolysin on human erythrocyte membranes

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

The influence of membrane lipids in Staphylococcus aureus gamma-hemolysins pore formation

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

Membrane-protein structure: Piercing insights.

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

A molecular pin to study the dynamics of beta-barrel formation in pore-forming toxins on erythrocytes: a sliding model.

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

Uni-molecular detection and quantification of selected β-lactam antibiotics with a hybrid α-hemolysin protein pore.

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

Membrane Protein Stoichiometry Determined from the Step-Wise Photobleaching of Dye-Labelled Subunits

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1110402108

21 January 2018

Assembly of Staphylococcus aureus leukocidin into a pore-forming ring-shaped oligomer on human polymorphonuclear leukocytes and rabbit erythrocytes

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Tyrosine72 residue at the bottom of rim domain in LukF crucial for the sequential binding of the staphylococcal gamma-hemolysin to human erythrocytes

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Essential binding of LukF of staphylococcal gamma-hemolysin followed by the binding of H gamma II for the hemolysis of human erythrocytes

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Sequential binding of Staphylococcal gamma-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

An N-terminal region of LukF of staphylococcal leukocidin/gamma-hemolysin crucial for the biological activity of the toxin

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Roll out the barrel

1 reference

https://pubmed.ncbi.nlm.nih.gov/21969538

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.1110402108

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2011PNAS..10817314Y

0 references

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PMC publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

ResearchGate publication ID

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