A cholesterol consensus motif is required for efficient intracellular transport and raft association of a group 2 HA from influenza virus (Q42183262)

18 October 2017

title

A cholesterol consensus motif is required for efficient intracellular transport and raft association of a group 2 HA from influenza virus (English)

1 reference

18 October 2017

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25330796%20AND%20SRC:MED&resulttype=core&format=json

6 June 2020

Michael Veit

series ordinal

3

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6 June 2020

author name string

Andreas Herrmann

series ordinal

2

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6 June 2020

language of work or name

English

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publication date

1 January 2015

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18 October 2017

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25330796%20AND%20SRC:MED&resulttype=core&format=json

6 June 2020

volume

465

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6 June 2020

issue

2

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6 June 2020

page(s)

305-314

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Revitalizing membrane rafts: new tools and insights

6 June 2020

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

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Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories

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Greasing their way: lipid modifications determine protein association with membrane rafts

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Palmitoylation regulates raft affinity for the majority of integral raft proteins.

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Requirement of transmembrane domain for CD154 association to lipid rafts and subsequent biological events

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The transmembrane domain of podoplanin is required for its association with lipid rafts and the induction of epithelial-mesenchymal transition.

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Identification of a lysine-rich region of Fas as a raft nanodomain targeting signal necessary for Fas-mediated cell death.

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Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly

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S acylation of the hemagglutinin of influenza viruses: mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine.

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Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity

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Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain

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

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Lipid domain association of influenza virus proteins detected by dynamic fluorescence microscopy techniques.

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FLIM-FRET and FRAP reveal association of influenza virus haemagglutinin with membrane rafts.

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Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi.

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Membrane raft association is a determinant of plasma membrane localization

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Lipids and cholesterol as regulators of traffic in the endomembrane system

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Transport through the Golgi apparatus by rapid partitioning within a two-phase membrane system

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Domain coupling in asymmetric lipid bilayers

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Linker and/or transmembrane regions of influenza A/Group-1, A/Group-2, and type B virus hemagglutinins are packed differently within trimers

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Identification of novel sphingolipid-binding motifs in mammalian membrane proteins.

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Complilation of detailed protocols needed to detect and analyze the most important co- and post translational modifications of protein. Preface

21 January 2018

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Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide

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Identifiers

DOI

10.1042/BJ20141114

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25330796%20AND%20SRC:MED&resulttype=core&format=json

6 June 2020

1 reference