The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement (Q35887194)

10 August 2017

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title

The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement (English)

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10 August 2017

F S Cohen

1

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PubMed ID

15366419

10 August 2017

G B Melikyan

series ordinal

2

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10 August 2017

1 May 2004

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10 August 2017

14

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Journal of Membrane Biology

inferred from page(s)

published in

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10 August 2017

199

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10 August 2017

1-14

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10 August 2017

1

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https://scigraph.springernature.com/pub.10.1007/s00232-004-0669-8

10 August 2017

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cites work

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A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype

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Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions

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Dynamics of fusion pores connecting membranes of different tensions

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Kinetically differentiating influenza hemagglutinin fusion and hemifusion machines.

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The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity

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Effect of chain length and unsaturation on elasticity of lipid bilayers

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A quantitative model for membrane fusion based on low-energy intermediates

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Leash in the groove mechanism of membrane fusion

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N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil

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Membrane anchorage brings about fusogenic properties in a short synthetic peptide

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Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin

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Measured effects of diacylglycerol on structural and elastic properties of phospholipid membranes

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Methodologies in the study of cell-cell fusion

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GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes

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Fusion of cells by flipped SNAREs

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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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Human Immunodeficiency Virus Type 1 Env with an Intersubunit Disulfide Bond Engages Coreceptors but Requires Bond Reduction after Engagement To Induce Fusion

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Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion

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Flickering fusion pores comparable with initial exocytotic pores occur in protein-free phospholipid bilayers

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Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion

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The influence of lysolipids on the spontaneous curvature and bending elasticity of phospholipid membranes

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Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation

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Lipids in biological membrane fusion

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The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion

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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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Membrane mechanics can account for fusion pore dilation in stages

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12 December 2020

Virus-cell and cell-cell fusion

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12 December 2020

Structure of influenza haemagglutinin at the pH of membrane fusion

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12 December 2020

Asymmetric membranes resulting from the fusion of two black lipid bilayers

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12 December 2020

Hemifusion between cells expressing hemagglutinin of influenza virus and planar membranes can precede the formation of fusion pores that subsequently fully enlarge

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12 December 2020

A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion

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12 December 2020

Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41

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12 December 2020

Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41.

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12 December 2020

The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein

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12 December 2020

Meta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin

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12 December 2020

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The 1-127 HA2 construct of influenza virus hemagglutinin induces cell-cell hemifusion

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12 December 2020

New phases of phospholipids and implications to the membrane fusion problem

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12 December 2020

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12 December 2020

Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide"

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12 December 2020

The electrical breakdown of cell and lipid membranes: the similarity of phenomenologies

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12 December 2020

Bilayer Mixing, Fusion, and Lysis Following the Interaction of Populations of Cationic and Anionic Phospholipid Bilayer Vesicles

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What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (review).

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Intermolecular forces in biology

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Protein-Lipid Interplay in Fusion and Fission of Biological Membranes

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12 December 2020

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Lessons for the study of membrane fusion from membrane interactions in phospholipid systems

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12 December 2020

Role of hydrophobic forces in bilayer adhesion and fusion

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12 December 2020

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12 December 2020

Conformational changes and fusion activity of vesicular stomatitis virus glycoprotein: [125I]iodonaphthyl azide photolabeling studies in biological membranes

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Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus

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12 December 2020

The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores

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12 December 2020

Thermodynamics of fusion peptide-membrane interactions

1 reference

12 December 2020

Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein

1 reference

12 December 2020

Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G

1 reference

12 December 2020

A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation

1 reference

12 December 2020

Multiple local contact sites are induced by GPI-linked influenza hemagglutinin during hemifusion and flickering pore formation.

1 reference

12 December 2020

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

1 reference

12 December 2020

Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity

1 reference

12 December 2020

Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein

1 reference

12 December 2020

Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection

1 reference

12 December 2020

GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity.

1 reference

12 December 2020

Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution

1 reference

12 December 2020

Progressive truncations C terminal to the membrane-spanning domain of simian immunodeficiency virus Env reduce fusogenicity and increase concentration dependence of Env for fusion

1 reference

12 December 2020

Protein-mediated membrane fusion

1 reference

12 December 2020

The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion

1 reference

12 December 2020

The hydrophobic interaction is long range, decaying exponentially with distance

1 reference

12 December 2020

Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy

1 reference

12 December 2020

Lipid intermediates in membrane fusion: formation, structure, and decay of hemifusion diaphragm

1 reference

12 December 2020

10.1007/S00232-004-0669-8

Identifiers

DOI

1 reference

10 August 2017

1 reference

PubMed ID

15366419