about
Human perforin employs different avenues to damage membranesInerolysin, a cholesterol-dependent cytolysin produced by Lactobacillus inersBiological effects of listeriolysin O: implications for vaccinationA new model for pore formation by cholesterol-dependent cytolysinsBrinp1(-/-) mice exhibit autism-like behaviour, altered memory, hyperactivity and increased parvalbumin-positive cortical interneuron densityStructure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicronCellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracisStructures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin RecognitionStructure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC)Defining the interaction of perforin with calcium and the phospholipid membraneCalcium-dependent permeabilization of erythrocytes by a perforin-like protein during egress of malaria parasitesA Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipidKilling of Microbes and Cancer by the Immune System with Three Mammalian Pore-Forming Killer ProteinsInflammasome-activated gasdermin D causes pyroptosis by forming membrane poresNovel animal defenses against predation: a snail egg neurotoxin combining lectin and pore-forming chains that resembles plant defense and bacteria attack toxinsThe Chlamydia psittaci genome: a comparative analysis of intracellular pathogensPerforin-like protein PPLP2 permeabilizes the red blood cell membrane during egress of Plasmodium falciparum gametocytesAn intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Resolved single-molecule detection of individual species within a mixture of anti-biotin antibodies using an engineered monomeric nanopore.Functional truncated membrane pores.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.Structural and functional analysis of perforin mutations in association with clinical data of familial hemophagocytic lymphohistiocytosis type 2 (FHL2) patients.Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells.Statins protect against fulminant pneumococcal infection and cytolysin toxicity in a mouse model of sickle cell diseaseBetaSearch: a new method for querying β-residue motifsA Nonpolycationic Fully Proteinaceous Multiagent System for Potent Targeted Delivery of siRNA.Topology of the membrane-bound form of complement protein C9 probed by glycosylation mapping, anti-peptide antibody binding, and disulfide modification.Biological characterization of Chlamydia trachomatis plasticity zone MACPF domain family protein CT153.Apicomplexan perforin-like proteins.Transcriptome of American oysters, Crassostrea virginica, in response to bacterial challenge: insights into potential mechanisms of disease resistancePerforin evolved from a gene duplication of MPEG1, followed by a complex pattern of gene gain and loss within EuteleostomiEffects of MACPF/CDC proteins on lipid membranes.Functional assessment of perforin C2 domain mutations illustrates the critical role for calcium-dependent lipid binding in perforin cytotoxic functionPerforin deficiency and susceptibility to cancer.Perforin: structure, function, and role in human immunopathology.Structure of the essential Plasmodium host cell traversal protein SPECT1.Staphylococcal enterotoxin H induced apoptosis of bovine mammary epithelial cells in vitro.Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9Reconstitution of cholesterol-dependent vaginolysin into tethered phospholipid bilayers: implications for bioanalysis.
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The MACPF/CDC family of pore-forming toxins.
@ast
The MACPF/CDC family of pore-forming toxins.
@en
type
label
The MACPF/CDC family of pore-forming toxins.
@ast
The MACPF/CDC family of pore-forming toxins.
@en
prefLabel
The MACPF/CDC family of pore-forming toxins.
@ast
The MACPF/CDC family of pore-forming toxins.
@en
P2093
P2860
P50
P1476
The MACPF/CDC family of pore-forming toxins.
@en
P2093
Carlos J Rosado
Ilia Voskoboinik
Michael J Kuiper
Michelle A Dunstone
Ruby H P Law
Stephanie Kondos
Tara E Bull
P2860
P304
P356
10.1111/J.1462-5822.2008.01191.X
P577
2008-06-28T00:00:00Z
2008-09-01T00:00:00Z