Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin.
about
The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyCholesterol-dependent cytolysins, a family of versatile pore-forming toxinsRapid assembly of a multimeric membrane protein poreRedefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysinsDisentangling the roles of cholesterol and CD59 in intermedilysin pore formation.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.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.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunitRole of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membraneAssembly and topography of the prepore complex in cholesterol-dependent cytolysins.Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of ActinoporinsStructures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysinsInsights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O.Development of a single-gene, signature-tag-based approach in combination with alanine mutagenesis to identify listeriolysin O residues critical for the in vivo survival of Listeria monocytogenes.Construction and immunological characterization of a novel nontoxic protective pneumolysin mutant for use in future pneumococcal vaccines.Conformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.Perfringolysin O: The Underrated Clostridium perfringens Toxin?Cloning, functional characterization, and mode of action of a novel insecticidal pore-forming toxin, sphaericolysin, produced by Bacillus sphaericus.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Antibody-mediated neutralization of perfringolysin o for intracellular protein delivery.Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity.Use of mutant 125I-perfringolysin O to probe transport and organization of cholesterol in membranes of animal cells.Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysinListeriolysin O as a strong immunogenic molecule for the development of new anti-tumor vaccinesThe influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O)Clostridial toxins.Insights into structure and activity of natural compound inhibitors of pneumolysin.Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose.Bacterial toxins and the nervous system: neurotoxins and multipotential toxins interacting with neuronal cells.Domain 4 (D4) of Perfringolysin O to Visualize Cholesterol in Cellular Membranes-The Update.Listeria monocytogenes impairs SUMOylation for efficient infection.Immunization with genetic toxoids of the Arcanobacterium pyogenes cholesterol-dependent cytolysin, pyolysin, protects mice against infection.Measuring kinetic drivers of pneumolysin pore structure.Incomplete pneumolysin oligomers form membrane pores.
P2860
Q21131398-F154B756-7AD8-4889-A55C-6B3A28F8222CQ24534721-1609E184-9DE0-4949-A901-33FC16B852C3Q24620804-A4229AEB-D8CD-4A84-BC29-8B7E478B1DD6Q24673155-E61D049E-1701-4195-A068-D7ADDAEA63F3Q30152693-A7C85CF7-6BA5-4D9F-A69D-234BD96830ECQ30152918-5E72D947-1B25-40EE-AF4F-4950954667DAQ30153240-FB00CC8A-F8C1-4E32-B916-5EAC36E0B3A0Q30153348-3F936E6F-86C4-4F51-A956-ED3B6CCCCE87Q30155306-7307FFA5-7F38-4ACF-8163-A535C0557585Q30155494-946F96E3-0158-4694-A3AF-633045687185Q30157689-D3104B1A-5680-405C-AB2F-237EB78FF394Q30160110-369F10C4-97ED-4132-B973-E407BA58520CQ30163889-F369EC85-805A-4C42-AFBB-A0A8B331FC7EQ30164706-22C8255F-672D-4B80-8B2E-B90AB14837E0Q30390842-3190AB3B-2EE2-492F-B0C8-E77F42A450EDQ33343788-D3662FE4-BD74-4E85-9094-7EE463A6B68BQ33755934-C7FE9B7F-BFBD-4EB3-9B32-96863D18FD53Q34134769-D29AE32C-B187-47B8-8DDD-1EF1C19E9C9EQ34186321-9BB3A06F-3710-4A25-816C-BD3B9479DD97Q34208868-408F0E2D-2252-4B52-9A38-CAAB403DF39FQ34301234-CFD37164-69FC-412E-A7F0-61560CA5CD4AQ34635171-ED8AD99B-063E-4609-991C-FD116F85966CQ35662926-4EBEB4CC-2F7A-4968-BE6B-1F0DB21D5C68Q35869675-9A53DCC9-0554-4EB9-BC92-23E8506BDA93Q36059050-5C07955A-5610-4DF7-B685-A55A6B645ED4Q36926959-AED6B8C3-4C3D-4D2C-973F-3D71ADD0D183Q36954090-0A371843-7DFF-4787-9277-74466754912DQ36967619-9A67799F-224E-42CF-B1C1-59FDCDC0814CQ37102350-26523D98-7ACD-4983-8D6A-F0BC66B5886AQ37505374-2A27952D-06A7-4C53-9E11-479320F39264Q37608423-EA866AE6-66AD-4951-93C9-AC3F59650FF0Q37613674-056628E1-5F98-415D-82C5-EAC7756E9E6FQ37625776-3D42CC5A-FBA9-4F8D-9504-67197A896E1BQ37807985-EF0022EE-E86A-4269-B6F0-202F6D973FDFQ37954286-F2D288CC-8EB7-4E7A-8EB1-6D739C85A9FAQ39168764-29475C12-8D72-494E-8E05-8064B7B7AE5FQ39711579-6BF2D0A2-52FD-4440-A2DE-01FFD88554DBQ39746198-5DCECE9F-4F86-40A3-BD8B-81E8D747F676Q39931955-FE7E1BEB-6DF4-45E3-8BF7-A8DC240DE895Q40223553-5ED03C49-1EA1-4011-9F2A-76B0450D89AC
P2860
Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Monomer-monomer interactions d ...... olesterol-dependent cytolysin.
@ast
Monomer-monomer interactions d ...... olesterol-dependent cytolysin.
@en
type
label
Monomer-monomer interactions d ...... olesterol-dependent cytolysin.
@ast
Monomer-monomer interactions d ...... olesterol-dependent cytolysin.
@en
prefLabel
Monomer-monomer interactions d ...... olesterol-dependent cytolysin.
@ast
Monomer-monomer interactions d ...... olesterol-dependent cytolysin.
@en
P2093
P2860
P356
P1476
Monomer-monomer interactions d ...... olesterol-dependent cytolysin.
@en
P2093
Arthur E Johnson
Daniel M Czajkowsky
Eileen M Hotze
Rodney K Tweten
Zhifeng Shao
P2860
P304
11597-11605
P356
10.1074/JBC.M111039200
P407
P577
2002-01-17T00:00:00Z