Hypothesis: spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion (Q30311060)

16 June 2017

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title

Hypothesis: spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion (English)

1 reference

16 June 2017

Lukas K Tamm

1

1 reference

PubMed ID

12873762

16 June 2017

language of work or name

English

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publication date

1 July 2003

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Biochimica et Biophysica Acta

16 June 2017

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16 June 2017

1614

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16 June 2017

1

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16 June 2017

14-23

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Coiled coils in both intracellular vesicle and viral membrane fusion

16 June 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Structure of influenza haemagglutinin at the pH of membrane fusion

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Structure of influenza virus haemagglutinin complexed with a neutralizing antibody.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Influenza hemagglutinin is spring-loaded by a metastable native conformation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

H+-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

pH-dependent membrane fusion activity of a synthetic twenty amino acid peptide with the same sequence as that of the hydrophobic segment of influenza virus hemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Membrane Fusion by Peptide Analogues of Influenza Virus Haemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Orientation of fusion-active synthetic peptides in phospholipid bilayers: determination by Fourier transform infrared spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

A host-guest system to study structure-function relationships of membrane fusion peptides

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Structure of an analog of fusion peptide from hemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Membrane protein folding and stability: physical principles

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Thermodynamics of fusion peptide-membrane interactions

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Titration calorimetry of lipid-peptide interactions

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Structural studies on membrane-embedded influenza hemagglutinin and its fragments

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

The mechanism for low-pH-induced clustering of phospholipid vesicles carrying the HA2 ectodomain of influenza hemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

The fusion kinetics of influenza hemagglutinin expressing cells to planar bilayer membranes is affected by HA density and host cell surface

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: probing the role of hydrophobic residue size in the central region of the fusion peptide

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

A transmembrane helix dimer: structure and implications

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Structure of dengue virus: implications for flavivirus organization, maturation, and fusion

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2736%2803%2900159-7

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0005-2736(03)00159-7

1 reference

16 June 2017

1 reference

PubMed ID

12873762