Membrane assembly of the cholesterol-dependent cytolysin pore complex.
about
Interactions between Autophagy and Bacterial Toxins: Targets for Therapy?Obstructing toxin pathways by targeted pore blockageBiological effects of listeriolysin O: implications for vaccinationMultifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenesMore than a pore: the cellular response to cholesterol-dependent cytolysinsConformational changes during pore formation by the perforin-related protein pleurotolysinListeriolysin O Membrane Damaging Activity Involves Arc Formation and Lineaction -- Implication for Listeria monocytogenes Escape from Phagocytic VacuoleCrystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assemblyA new model for pore formation by cholesterol-dependent cytolysinsManipulating the Lewis antigen specificity of the cholesterol-dependent cytolysin lectinolysinStructure and secretion of CofJ, a putative colonization factor of enterotoxigenic Escherichia coliCryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.The Apicomplexan CDC/MACPF-like pore-forming proteins.Decreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size.An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Crucial role of perfringolysin O D1 domain in orchestrating structural transitions leading to membrane-perforating pores: a hydrogen-deuterium exchange study.Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.Cysteine-scanning mutagenesis supports the importance of Clostridium perfringens enterotoxin amino acids 80 to 106 for membrane insertion and pore formationMonomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Assembling the puzzle: Oligomerization of α-pore forming proteins in membranesInduction of endoplasmic reticulum stress and unfolded protein response constitutes a pathogenic strategy of group A streptococcusMouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Effects of MACPF/CDC proteins on lipid membranes.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin OThe cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cellsThe cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.Reconstitution of cholesterol-dependent vaginolysin into tethered phospholipid bilayers: implications for bioanalysis.Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.Protective role of the dynamin inhibitor Dynasore against the cholesterol-dependent cytolysin of Trueperella pyogenesPerfringolysin O: The Underrated Clostridium perfringens Toxin?Listeriolysin O Affects the Permeability of Caco-2 Monolayer in a Pore-Dependent and Ca2+-Independent Manner.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Dual modes of membrane binding direct pore formation by Streptolysin O.Identification and characterization of the first cholesterol-dependent cytolysins from Gram-negative bacteriaAltering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O.Antibody-mediated neutralization of perfringolysin o for intracellular protein delivery.Vaginolysin drives epithelial ultrastructural responses to Gardnerella vaginalis.Insights into structure and activity of natural compound inhibitors of pneumolysin.
P2860
Q26801464-CE242721-2A04-44B4-83B3-2FAAA79B29BBQ26827489-7D897C3C-DEC7-4F58-BE37-E6C9E8FDDFD0Q26853146-56264429-D4F6-4D2C-82A5-C527632A5D39Q26864252-08D4A6A9-E2B2-4C48-ABB0-E16A5102B3BBQ27023593-A362D579-0489-4E21-B66D-9B9B11FBD4FAQ27313232-D5BE2681-8D6E-454E-8B99-9F28187ED8E0Q27314335-F72B9DCC-9A77-44DF-BCCB-AA0A16258102Q27316710-AF068DA1-EEC3-485E-924C-C62AB4C84D56Q27321259-24E8905D-EB0B-4300-B766-22FAB4BF5907Q27675238-CE75E6EF-0EC2-414C-A271-3F2BDBABDDFDQ27687046-CBC27661-BAF3-48FD-9B51-BD4BC6A126F7Q30152651-2FC51CC3-D1AD-4674-AEFF-EDD164537A23Q30152918-46C09539-18F2-4D68-94B7-5CFC7754EAD9Q30152922-04E698FD-ABBD-42AE-98F3-BCC721646B29Q30152956-41C3A0CC-697D-4A79-A7C8-9BE96AD3577BQ30153240-7742B36D-0B27-4334-849B-D37F12108F38Q30153348-A8F2A4A8-2FEC-4BC5-A8E5-2AC4D2293E5AQ30155117-8515A40D-56EE-47AD-8F27-4F9D45DDF3B0Q30155232-6EBD1596-F4BB-4D69-98E6-0941273F7D83Q30155306-FE11A9E1-A615-4BEB-98D5-BB3934088562Q33361524-2D1B21AA-35C2-44AF-9E37-4ADCAC5B6306Q33997843-BB609A66-210A-47FE-AA18-DB858E7EDAFFQ34134769-7422E464-9B82-4C8E-BF1E-E0D2B521610DQ34300045-EFC6826C-1F58-42B3-A23D-A9C83CC04406Q34422117-9A22EAA6-BF3F-4493-AA25-055BF73C5B81Q34664198-14592C54-9C52-42C6-A0E9-D45FC34D826AQ35003661-C0BEC0BA-B794-4370-AD04-636BF9CBA783Q35068926-D246589F-F3E3-46F0-88A4-96D484900805Q35070351-A328F583-7CD3-4D5D-895A-1511974F652FQ35240727-DDC9B980-B51A-41E2-8688-90D3514D4BA5Q35410523-DC3801EC-62B1-4FCD-8B38-219ECB2FB1ADQ35662926-12AA6DEF-8469-473F-B667-A3E3F0C0FE53Q35667526-859549C2-C900-4B06-9EA8-4A0124D03703Q36059050-E04159B4-A292-4803-804C-B1D377D65143Q36407452-5CC94E56-0C62-43E8-B85A-BD0EB1079CC2Q36506035-5CF633DD-1DA0-416D-8FE5-F34243630CB7Q36526328-FDEBA8E4-F88E-44BE-BF91-220485E8FFB8Q36926959-AE2B433A-2E37-459D-80A0-89E53C80A3F8Q37335989-3E092D64-DF6F-4749-B405-0DCF0D0E92C6Q37625776-A9077CD9-E99E-440F-ABAF-F3EE2083753F
P2860
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
@ast
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
@en
type
label
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
@ast
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
@en
prefLabel
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
@ast
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
@en
P2860
P1476
Membrane assembly of the cholesterol-dependent cytolysin pore complex.
@en
P2093
Eileen M Hotze
Rodney K Tweten
P2860
P304
P356
10.1016/J.BBAMEM.2011.07.036
P407
P577
2011-07-31T00:00:00Z