Conformational changes during pore formation by the perforin-related protein pleurotolysin - Test2 - elhamkhani - TriplyDB

Conformational changes during pore formation by the perforin-related protein pleurotolysin

Conformational changes during pore formation by the perforin-related protein pleurotolysin

http://www.wikidata.org/entity/Q27313232

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Killing of Microbes and Cancer by the Immune System with Three Mammalian Pore-Forming Killer Proteins Cryo-electron Microscopy Analysis of Structurally Heterogeneous Macromolecular Complexes Structure of the poly-C9 component of the complement membrane attack complex The Apicomplexan CDC/MACPF-like pore-forming proteins.Single-particle electron microscopy in the study of membrane protein structure Refinement of atomic models in high resolution EM reconstructions using Flex-EM and local assessment.TEMPy: a Python library for assessment of three-dimensional electron microscopy density fits Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death.Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.Stonefish toxin defines an ancient branch of the perforin-like superfamily.Statistical modeling and removal of lipid membrane projections for cryo-EM structure determination of reconstituted membrane proteins Outcome of the First wwPDB Hybrid/Integrative Methods Task Force Workshop Integrative modelling of cellular assemblies.Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms.Improved metrics for comparing structures of macromolecular assemblies determined by 3D electron-microscopy.Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins.Cryo-electron tomography: an ideal method to study membrane-associated proteins.The mystery behind membrane insertion: a review of the complement membrane attack complex Structure of astrotactin-2: a conserved vertebrate-specific and perforin-like membrane protein involved in neuronal development.Comparative and transcriptional analysis of the predicted secretome in the lignocellulose-degrading basidiomycete fungus Pleurotus ostreatus.Measuring kinetic drivers of pneumolysin pore structure.Real-time visualization of perforin nanopore assembly.Chimeric approach for narrowing a membrane-inserting region within human perforin.Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB.Structures of monomeric and oligomeric forms of the Toxoplasma gondii perforin-like protein 1.The first transmembrane region of complement component-9 acts as a brake on its self-assembly Mechanism of membrane pore formation by human gasdermin-D Advances in structure determination by cryo-EM to unravel membrane-spanning pore formation

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Conformational changes during pore formation by the perforin-related protein pleurotolysin

http://www.wikidata.org/entity/Q27313232

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2015 nî lūn-bûn

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2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2015 թվականի փետրվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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Essential role of membrane-attack protein in malarial transmission to mosquito host

Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation

A common fold mediates vertebrate defense and bacterial attack

Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense

The structural basis for membrane binding and pore formation by lymphocyte perforin

Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement.

Assembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9.

Structure of Complement C6 Suggests a Mechanism for Initiation and Unidirectional, Sequential Assembly of Membrane Attack Complex (MAC)

Crystal Structure of C5b-6 Suggests Structural Basis for Priming Assembly of the Membrane Attack Complex

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