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Circulating Pneumolysin Is a Potent Inducer of Cardiac Injury during Pneumococcal InfectionStructural basis of complement membrane attack complex formation.A Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipidStructure of the poly-C9 component of the complement membrane attack complexTrapping of Vibrio cholerae cytolysin in the membrane-bound monomeric state blocks membrane insertion and functional pore formation by the toxinGSDMD membrane pore formation constitutes the mechanism of pyroptotic cell deathIdentification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of ActinoporinsAssembling the puzzle: Oligomerization of α-pore forming proteins in membranesPerforin oligomers form arcs in cellular membranes: a locus for intracellular delivery of granzymes.The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.Serotype 1 and 8 Pneumococci Evade Sensing by Inflammasomes in Human Lung Tissue.Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores.More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes.Molecular mechanism of pore formation by aerolysin-like proteins.Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms.Biological activities of suilysin: role in Streptococcus suis pathogenesis.Bax and Bak Pores: Are We Closing the Circle?Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.Cryo-electron tomography: an ideal method to study membrane-associated proteins.The mystery behind membrane insertion: a review of the complement membrane attack complexStructure of astrotactin-2: a conserved vertebrate-specific and perforin-like membrane protein involved in neuronal development.Measuring kinetic drivers of pneumolysin pore structure.Real-time visualization of perforin nanopore assembly.Single molecule compression reveals intra-protein forces drive cytotoxin pore formation.Structures of monomeric and oligomeric forms of the Toxoplasma gondii perforin-like protein 1.Mechanism of membrane pore formation by human gasdermin-D
P2860
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P2860
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Incomplete pneumolysin oligomers form membrane pores.
@en
type
label
Incomplete pneumolysin oligomers form membrane pores.
@en
prefLabel
Incomplete pneumolysin oligomers form membrane pores.
@en
P2860
P356
P1433
P1476
Incomplete pneumolysin oligomers form membrane pores
@en
P2093
Andreas F-P Sonnen
P2860
P304
P356
10.1098/RSOB.140044
P577
2014-04-23T00:00:00Z