The influenza virus hemagglutinin: a model protein in the study of membrane fusion (Q45754803)

15 December 2017

review article

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title

The influenza virus hemagglutinin: a model protein in the study of membrane fusion (English)

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15 December 2017

author

João Ramalho-Santos

series ordinal

1

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15 December 2017

author name string

M C de Lima

series ordinal

2

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15 December 2017

publication date

1 June 1998

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15 December 2017

number of pages

8

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Biochimica et Biophysica Acta

inferred from page(s)

published in

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15 December 2017

volume

1376

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15 December 2017

issue

1

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15 December 2017

page(s)

147-154

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15 December 2017

Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism

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Partial fusion activity of influenza virus toward liposomes and erythrocyte ghosts is distinct from viral inactivation

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The structure and function of the hemagglutinin membrane glycoprotein of influenza virus

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Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin

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Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin

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Intermediates in influenza virus PR/8 haemagglutinin-induced membrane fusion

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Target cell membrane sialic acid modulates both binding and fusion activity of influenza virus

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Influenza hemagglutinin-mediated membrane fusion: influence of receptor binding on the lag phase preceding fusion

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Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density

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Membrane fusion. Anchors aweigh

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Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity

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Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin

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A spring-loaded mechanism for the conformational change of influenza hemagglutinin

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Structure of influenza haemagglutinin at the pH of membrane fusion

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Structure and topology of the influenza virus fusion peptide in lipid bilayers

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Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers

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Structural characterization of viral fusion proteins

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Mechanisms of membrane fusion

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Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers

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Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events

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Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion

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Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion

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Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion

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The exocytotic fusion pore

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An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids

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Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusion

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Virus-cell and cell-cell fusion

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Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg.

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7 January 2021

Synaptic vesicle biogenesis, docking, and fusion: a molecular description

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Evidence that synaptobrevin is involved in fusion between synaptic vesicles and synaptic plasma membrane vesicles.

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7 January 2021

Lysolipids reversibly inhibit Ca(2+)-, GTP- and pH-dependent fusion of biological membranes.

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Identifiers

DOI

1 reference

15 December 2017

PubMed ID

9666108

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15 December 2017