Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism - Wikidata - wikimedia - TriplyDB

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

http://www.wikidata.org/entity/Q27685330

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Binary Toxin Subunits of Lysinibacillus sphaericus Are Monomeric and Form Heterodimers after In Vitro Activation Lectin domains at the frontiers of plant defense Conformational changes during pore formation by the perforin-related protein pleurotolysin Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.A new model for pore formation by cholesterol-dependent cytolysins Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process.In situ structural analysis of the Yersinia enterocolitica injectisome Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure Prepore Stability Controls Productive Folding of the BAM-independent Multimeric Outer Membrane Secretin PulD.X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form.Towards an integrative structural biology approach: combining Cryo-TEM, X-ray crystallography, and NMR.Structural basis for self-assembly of a cytolytic pore lined by protein and lipid Disentangling constraints using viability evolution principles in integrative modeling of macromolecular assemblies Comparative transcriptomics of the model mushroom Coprinopsis cinerea reveals tissue-specific armories and a conserved circuitry for sexual development Channel-forming bacterial toxins in biosensing and macromolecule delivery Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxins Conformational States of macromolecular assemblies explored by integrative structure calculation.Site-specific chemoenzymatic labeling of aerolysin enables the identification of new aerolysin receptors The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Soluble Oligomers of the Pore-forming Toxin Cytolysin A from Escherichia coli Are Off-pathway Products of Pore Assembly.Temperature Effect on Ionic Current and ssDNA Transport through Nanopores A prodrug-doped cellular Trojan Horse for the potential treatment of prostate cancer.Revealing Assembly of a Pore-Forming Complex Using Single-Cell Kinetic Analysis and Modeling.Dynamics and Energy Contributions for Transport of Unfolded Pertactin through a Protein Nanopore.Outcome of the First wwPDB Hybrid/Integrative Methods Task Force Workshop Pore-forming toxins from pathogenic amoebae.Single molecule analysis by biological nanopore sensors.Construction of an aerolysin nanopore in a lipid bilayer for single-oligonucleotide analysis.Integrative modelling of cellular assemblies.Molecular mechanism of pore formation by aerolysin-like proteins.Electron Cryo-microscopy as a Tool for Structure-Based Drug Development.Nanopore Sensing.Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform.Single molecule atomic force microscopy of aerolysin pore complexes reveals unexpected star-shaped topography.Amaranthin-Like Proteins with Aerolysin Domains in Plants.Nanopore sensing of botulinum toxin type B by discriminating an enzymatically cleaved Peptide from a synaptic protein synaptobrevin 2 derivative.Structural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family.

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P2860

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

http://www.wikidata.org/entity/Q27685330

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2013 nî lūn-bûn

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2013 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

@zh-hans

2013年学术文章

@zh-my

2013年学术文章

@zh-sg

2013年學術文章

@yue

name

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@ast

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@en

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@nl

type

label

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@ast

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@en

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@nl

prefLabel

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@ast

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@en

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

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Nature Chemical Biology

P1476

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

@en

P2093

Ioan Iacovache

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Lucile Pernot

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Matteo Dal Peraro

http://www.w3.org/2001/XMLSchema#string

Mohamed Chami

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P2860

Functional organization of the yeast proteome by systematic analysis of protein complexes

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

MolProbity: all-atom structure validation for macromolecular crystallography

Improved methods for building protein models in electron density maps and the location of errors in these models

Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin

Crystal structure of the parasporin-2 Bacillus thuringiensis toxin that recognizes cancer cells

The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism

Structural insight into nascent polypeptide chain-mediated translational stalling.

Biological and structural characterization of the Mycobacterium smegmatis nitroreductase NfnB, and its role in benzothiazinone resistance

Structures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin Recognition

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623-629

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scholarly article

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511702

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10.1038/NCHEMBIO.1312

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10

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9

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Henning Stahlberg

Matteo T. Degiacomi

Misha Kudryashev

Gisou van der Goot

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2013-08-04T00:00:00Z

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255177181

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1040348007

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23912165

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