Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin. - Wikidata - awgldk - TriplyDB

Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin.

Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin.

http://www.wikidata.org/entity/Q36321226

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Lipid rafts, cholesterol, and the brain The Feat of Packaging Eight Unique Genome Segments Membrane microdomains: from seeing to understanding Insulin regulates Glut4 confinement in plasma membrane clusters in adipose cells Influenza Virus Induces Cholesterol-Enriched Endocytic Recycling Compartments for Budozone Formation via Cell Cycle-Independent Centrosome Maturation Formation of raft-like assemblies within clusters of influenza hemagglutinin observed by MD simulations Influenza viral membrane fusion is sensitive to sterol concentration but surprisingly robust to sterol chemical identity.Hemagglutinin Spatial Distribution Shifts in Response to Cholesterol in the Influenza Viral Envelope.Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1.Raft composition at physiological temperature and pH in the absence of detergents.Influenza A virus uses intercellular connections to spread to neighboring cells Kinetic disruption of lipid rafts is a mechanosensor for phospholipase D Spatial association of signaling proteins and F-actin effects on cluster assembly analyzed via photoactivation localization microscopy in T cells Dynamics of multicomponent vesicles in a viscous fluid.Polarized sorting and trafficking in epithelial cells Phase-field modeling of the dynamics of multicomponent vesicles: Spinodal decomposition, coarsening, budding, and fission."Entropic traps" in the kinetics of phase separation in multicomponent membranes stabilize nanodomains.Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories.Lipid peroxides promote large rafts: effects of excitation of probes in fluorescence microscopy and electrochemical reactions during vesicle formation.DC-SIGN and influenza hemagglutinin dynamics in plasma membrane microdomains are markedly different.Stochastic fusion simulations and experiments suggest passive and active roles of hemagglutinin during membrane fusion.Hemagglutinin clusters in the plasma membrane are not enriched with cholesterol and sphingolipids The role of cholesterol and sphingolipids in chemokine receptor function and HIV-1 envelope glycoprotein-mediated fusion.Quantitative analysis of the lipidomes of the influenza virus envelope and MDCK cell apical membrane In silico characterization of resonance energy transfer for disk-shaped membrane domains.Super-resolution imaging of C-type lectin and influenza hemagglutinin nanodomains on plasma membranes using blink microscopy Optical nanoscopy: from acquisition to analysis.Direct chemical evidence for sphingolipid domains in the plasma membranes of fibroblasts Have we become overly reliant on lipid rafts? Talking Point on the involvement of lipid rafts in T-cell activation.Domain formation in membranes caused by lipid wetting of protein.Actin mediates the nanoscale membrane organization of the clustered membrane protein influenza hemagglutinin Sphingolipid domains in the plasma membranes of fibroblasts are not enriched with cholesterol The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particles On the use of Ripley's K-function and its derivatives to analyze domain size Sphingolipid Organization in the Plasma Membrane and the Mechanisms That Influence It Fluorinated colloidal gold immunolabels for imaging select proteins in parallel with lipids using high-resolution secondary ion mass spectrometry.Lipid domain association of influenza virus proteins detected by dynamic fluorescence microscopy techniques.Alginate Biosynthesis Factories in Pseudomonas fluorescens: Localization and Correlation with Alginate Production Level.

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P2860

Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin.

http://www.wikidata.org/entity/Q36321226

description

2005 nî lūn-bûn

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Quantitative electron microsco ...... on of influenza hemagglutinin.

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Quantitative electron microsco ...... on of influenza hemagglutinin.

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Quantitative electron microsco ...... on of influenza hemagglutinin.

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Quantitative electron microsco ...... on of influenza hemagglutinin.

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Anil Verma

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Anne Kenworthy

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Jane Farrington

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Joshua Zimmerberg

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Mukesh Kumar

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Samuel T Hess

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P2860

Functional rafts in cell membranes

Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.

Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: nanoscopic domain formation driven by cholesterol

Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy

The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition

Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts.

Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines

The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation.

Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion

Dynamics of putative raft-associated proteins at the cell surface.

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