About: F NMR studies provide insights into lipid membrane interactions of listeriolysin O, a pore forming toxin from Listeria monocytogenes

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: F NMR studies provide insights into lipid membrane interactions of listeriolysin O, a pore forming toxin from Listeria monocytogenes Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published in Scientific Reports

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Scientific Reports (fr) наукова стаття, опублікована в травні 2018 (uk) im Mai 2018 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Scientific Reports (en)
publication date	wds:Q60201763-1BA3A4A6-8F4D-4181-88D5-8ED7A25CED22
publication date	2018-05-02 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q60201763-880C0A57-DC4A-48C4-A926-01FCC6B95E32
language of work or name	English
cites work	wds:Q60201763-00A380E2-A47E-41C5-A979-B57130A37417 wds:Q60201763-042FBBD5-A010-4A7D-8DED-A69F1AA027CD wds:Q60201763-058068A2-527D-4013-94ED-A5AB9549221D wds:Q60201763-06C6C1BA-DAB7-44C5-B842-A1CE569FC98F wds:Q60201763-10B9B477-025F-42A5-82DA-4D3FA689650D wds:Q60201763-1C996F06-48A4-44D6-B22D-E2898F476951 wds:Q60201763-21D3308E-B8EB-4817-9E90-9FFA0CDC8527 wds:Q60201763-235E124A-009B-4329-955E-D18243466A72 wds:Q60201763-299E09DA-09D5-4FAE-A172-635EF8755967 wds:Q60201763-29A7778D-6E52-47D7-8734-70ED2972514C wds:Q60201763-2A6C7FCD-8C6D-461B-A138-C092D33647B2 wds:Q60201763-2E330974-CDA9-47AA-AB03-B2E4385EBC93 wds:Q60201763-377694B3-DE68-4D44-B9CF-23CBA2109AC4 wds:Q60201763-3B4B5A30-4A0B-47EB-B2C0-8B0F2EF26DEC wds:Q60201763-43E800C2-7169-4B3D-B4D7-5BA32B383072 wds:Q60201763-4C3C1F06-FE43-4C2B-8C1B-48B4A23A7B41 wds:Q60201763-58093B34-E095-4D0D-AEF1-E3F67BBEE4C5 wds:Q60201763-59EC188D-F6BC-4F73-9727-7C1A26F0E3B7 wds:Q60201763-5B0B5432-223B-49EC-A979-AA93F2AD17D8 wds:Q60201763-5D79D915-8248-4A4B-8FEC-37B722C56C4E wds:Q60201763-5E1F3B50-E115-40C9-A9C6-6E05BAAEDECA wds:Q60201763-5EEAE8CC-34E9-46A0-95C7-85E6C7D69311 wds:Q60201763-68A3DD3A-8C27-4216-8D32-EB0761AAD4D9 wds:Q60201763-703F2056-B64C-40C9-B32A-E065782CA908 wds:Q60201763-760AC8BB-C339-4EBC-916F-D7B4856FBCA1 wds:Q60201763-7F6142C6-096C-4EC9-8D10-B87DB03EDE45 wds:Q60201763-81FD3BD1-5F75-4362-B40B-BE607E78D39F wds:Q60201763-9BC1A376-66E7-4023-987F-1C1D2DE52506 wds:Q60201763-9F370147-904C-4334-81C6-0F904EC1E115 wds:Q60201763-9F3ACD2F-0290-40B4-AA08-17A34C130EA8 wds:Q60201763-A4AFD73E-74D1-4F20-ADDA-EE804C967B4B wds:Q60201763-B0478DE3-787C-4F70-B59C-3C1605FD8CC8 wds:Q60201763-BDD01292-983E-445A-A516-5FA4DECF759E wds:Q60201763-C1841161-315F-46AB-9A7C-D3970ACE1EE5 wds:Q60201763-C4C3B8E6-EFA3-4250-A368-8C6835BA7229 wds:Q60201763-C5390A8E-FE82-46B9-B608-627FE3F1FFCC wds:Q60201763-D31D10AB-AEA5-4591-B332-521B263EDADA wds:Q60201763-E3D857C6-B235-4770-94D5-BA105ACFCD63 wds:Q60201763-E9AF7E13-6D47-4538-BA88-294272E7387C wds:Q60201763-F087F1E8-9590-45C0-89C7-AD6665734BE5 wds:Q60201763-FAAAF405-EA12-4BA5-93F8-E76C4E1A491D
cites work	pH dependence of listeriolysin O aggregation and pore-forming ability Listeria monocytogenes: a multifaceted model Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins Molecular determinants of Listeria monocytogenes pathogenesis Perspectives on NMR in drug discovery: a technique comes of age Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA. The cell biology of Listeria monocytogenes infection (escape from a vacuole) The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytes Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form Membrane assembly of the cholesterol-dependent cytolysin pore complex Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface Molecular basis of listeriolysin O pH dependence pH-dependent perforation of macrophage phagosomes by listeriolysin O from Listeria monocytogenes. Listeriolysin O: the Swiss army knife of Listeria Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles Listeriolysin O: cholesterol inhibits cytolysis but not binding to cellular membranes. Sterol and pH Interdependence in the Binding, Oligomerization, and Pore Formation of Listeriolysin O† CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin The Unique Molecular Choreography of Giant Pore Formation by the Cholesterol-Dependent Cytolysins of Gram-Positive Bacteria Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes Use of 19F NMR to probe protein structure and conformational changes Applications of (19)F-NMR in Fragment-Based Drug Discovery 19F NMR as a probe of ligand interactions with the iNOS binding site of SPRY domain-containing SOCS box protein 2. Interaction of the eukaryotic pore-forming cytolysin equinatoxin II with model membranes: 19F NMR studies Cellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracis Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us. Membrane pore formation at protein-lipid interfaces Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol. Plasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected]. A cytolysin, theta-toxin, preferentially binds to membrane cholesterol surrounded by phospholipids with 18-carbon hydrocarbon chains in cholesterol-rich region The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin. Structural characteristics of tetanolysin and its binding to lipid vesicles Structure-based functional studies for the cellular recognition and cytolytic mechanism of pneumolysin from Streptococcus pneumoniae Modifications in perfringolysin O domain 4 alter the cholesterol concentration threshold required for binding Actin dynamics studied by solid-state NMR spectroscopy Effect of streptolysin O and digitonin on egg lecithin/cholesterol vesicles Listeriolysin O Membrane Damaging Activity Involves Arc Formation and Lineaction -- Implication for Listeria monocytogenes Escape from Phagocytic Vacuole Transmembrane protein (perfringolysin o) association with ordered membrane domains (rafts) depends upon the raft-associating properties of protein-bound sterol
author name string	wds:Q60201763-3E421D7F-A6CB-409A-B110-A7E879C7963B wds:Q60201763-5431B150-9258-4394-A905-8DA628695F1B wds:Q60201763-B1DF19E1-9926-4D93-8BC3-3F6A8B467DAC
author name string	Vesna Hodnik Gregor Ilc Martina Lenarčič Živković
rdfs:label	F NMR studies provide insights into lipid membrane interactions of listeriolysin O, a pore forming toxin from Listeria monocytogenes (en)

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 183 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software