Quantitative analysis of the lipidomes of the influenza virus envelope and MDCK cell apical membrane - Wikidata - wikimedia - TriplyDB

Quantitative analysis of the lipidomes of the influenza virus envelope and MDCK cell apical membrane

Quantitative analysis of the lipidomes of the influenza virus envelope and MDCK cell apical membrane

http://www.wikidata.org/entity/Q35694152

about

A mechanistic paradigm for broad-spectrum antivirals that target virus-cell fusion Flexibility of a eukaryotic lipidome--insights from yeast lipidomics Counterion-mediated pattern formation in membranes containing anionic lipids Diacylglycerol Kinases: Shaping Diacylglycerol and Phosphatidic Acid Gradients to Control Cell Polarity Computational virology: From the inside out Formation of raft-like assemblies within clusters of influenza hemagglutinin observed by MD simulations Morphology and Molecular Composition of Purified Bovine Viral Diarrhea Virus Envelope Methodologies for the analysis of instantaneous lipid diffusion in MD simulations of large membrane systems.Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel 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.Influenza A induced cellular signal transduction pathways.Involvement of an Arginine Triplet in M1 Matrix Protein Interaction with Membranes and in M1 Recruitment into Virus-Like Particles of the Influenza A(H1N1)pdm09 Virus.Membrane Fusion and Infection of the Influenza Hemagglutinin.Multiphasic effects of cholesterol on influenza fusion kinetics reflect multiple mechanistic roles.The composition of West Nile virus lipid envelope unveils a role of sphingolipid metabolism in flavivirus biogenesis.Influenza A virus uses intercellular connections to spread to neighboring cells Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.Membrane raft association is a determinant of plasma membrane localization Lipidomics identifies a requirement for peroxisomal function during influenza virus replication Domain Stability in Biomimetic Membranes Driven by Lipid Polyunsaturation Influenza A virus survival in water is influenced by the origin species of the host cell.Trafficking of epidermal growth factor receptor ligands in polarized epithelial cells.Polarized sorting and trafficking in epithelial cells Tracking cholesterol/sphingomyelin-rich membrane domains with the ostreolysin A-mCherry protein.Nothing to sneeze at: a dynamic and integrative computational model of an influenza A virion.HIV-1 capture and transmission by dendritic cells: the role of viral glycolipids and the cellular receptor Siglec-1 Hemagglutinin clusters in the plasma membrane are not enriched with cholesterol and sphingolipids Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes Identification of mumps virus protein and lipid composition by mass spectrometry.A molecular tweezer antagonizes seminal amyloids and HIV infection.Sphingosine-1-Phosphate Lyase Deficient Cells as a Tool to Study Protein Lipid Interactions Hexagonal Substructure and Hydrogen Bonding in Liquid-Ordered Phases Containing Palmitoyl Sphingomyelin.Effects of diet and development on the Drosophila lipidome pH-Dependent Formation and Disintegration of the Influenza A Virus Protein Scaffold To Provide Tension for Membrane Fusion Hemagglutinin-esterase-fusion (HEF) protein of influenza C virus.Inhibition of Acid Sphingomyelinase Depletes Cellular Phosphatidylserine and Mislocalizes K-Ras from the Plasma Membrane.Intact sphingomyelin biosynthetic pathway is essential for intracellular transport of influenza virus glycoproteins.Transformation of polarized epithelial cells by apical mistrafficking of epiregulin The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particles

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P2860

Quantitative analysis of the lipidomes of the influenza virus envelope and MDCK cell apical membrane

http://www.wikidata.org/entity/Q35694152

description

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name

Quantitative analysis of the l ...... and MDCK cell apical membrane

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Quantitative analysis of the l ...... and MDCK cell apical membrane

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Quantitative analysis of the l ...... and MDCK cell apical membrane

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Quantitative analysis of the l ...... and MDCK cell apical membrane

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Quantitative analysis of the l ...... and MDCK cell apical membrane

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Quantitative analysis of the l ...... and MDCK cell apical membrane

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Journal of Cell Biology

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Quantitative analysis of the l ...... and MDCK cell apical membrane

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Andrej Shevchenko

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Beth Binnington

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Clifford A Lingwood

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Cornelia Schroeder

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Jean-Marc Verbavatz

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Lucie Kalvodova

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Severino Urban

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P2860

A comprehensive classification system for lipids

Influenza virus M2 protein mediates ESCRT-independent membrane scission

Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry

Update of the LIPID MAPS comprehensive classification system for lipids

Membrane lipids: where they are and how they behave

Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells

Progressive ordering with decreasing temperature of the phospholipids of influenza virus

Virus entry by endocytosis

Lipid domain structure of the plasma membrane revealed by patching of membrane components

Membrane proteins diffuse as dynamic complexes with lipids.

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10.1083/JCB.201108175

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2

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196

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Jean-Marc Verbavatz

Julio L Sampaio

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2012-01-16T00:00:00Z

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221751434

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3265945

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