Line-tension controlled mechanism for influenza fusion (Q34325691)

1 August 2017

title

Line-tension controlled mechanism for influenza fusion (English)

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1 August 2017

author name string

Herre Jelger Risselada

1

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1 August 2017

Giovanni Marelli

2

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1 August 2017

Marc Fuhrmans

3

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1 August 2017

Yuliya G Smirnova

4

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1 August 2017

Helmut Grubmüller

5

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1 August 2017

Siewert Jan Marrink

6

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1 August 2017

Marcus Müller

7

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1 August 2017

language of work or name

English

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publication date

28 June 2012

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1 August 2017

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1 August 2017

volume

7

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1 August 2017

issue

6

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1 August 2017

page(s)

e38302

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Creative Commons Attribution 4.0 International

1 August 2017

copyright license

start time

28 June 2012

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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6 July 2018

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Mechanics of membrane fusion

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Membranes of the world unite!

6 July 2018

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6 July 2018

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6 July 2018

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Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion

6 July 2018

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6 July 2018

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6 July 2018

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Membrane permeability changes at early stages of influenza hemagglutinin-mediated fusion

6 July 2018

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6 July 2018

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6 July 2018

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6 July 2018

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6 July 2018

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6 July 2018

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6 July 2018

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A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion.

6 July 2018

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

6 July 2018

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Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion. A new model for fusion

6 July 2018

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

6 July 2018

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Tension of membranes expressing the hemagglutinin of influenza virus inhibits fusion

6 July 2018

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Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion

6 July 2018

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6 July 2018

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Interaction of the influenza hemagglutinin fusion peptide with lipid bilayers: area expansion and permeation

6 July 2018

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Lysis of Large Unilamellar Vesicles Induced by Analogs of the Fusion Peptide of Influenza Virus Hemagglutinin

6 July 2018

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Influenza-virus-liposome lipid mixing is leaky and largely insensitive to the material properties of the target membrane

6 July 2018

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Energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms

6 July 2018

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6 July 2018

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Single mutation effects on conformational change and membrane deformation of influenza hemagglutinin fusion peptides

6 July 2018

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Molecular view of the role of fusion peptides in promoting positive membrane curvature.

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21 January 2018

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Molecular dynamics with coupling to an external bath

21 January 2018

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12 December 2020

Comment on "On using a too large integration time step in molecular dynamics simulations of coarse-grained molecular models" by M. Winger, D. Trzesniak, R. Baron and W. F. van Gunsteren, Phys. Chem. Chem. Phys., 2009, 11, 1934

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12 December 2020

The protein coat in membrane fusion: lessons from fission

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12 December 2020

A single bicontinuous cubic phase induced by fusion peptides

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12 December 2020

Nucleation free energy of pore formation in an amphiphilic bilayer studied by molecular dynamics simulations

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12 December 2020

Application of mean field boundary potentials in simulations of lipid vesicles

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12 December 2020

Influenza hemagglutinin-mediated membrane fusion does not involve inverted phase lipid intermediates

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12 December 2020

Dependence of the energies of fusion on the intermembrane separation: optimal and constrained

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12 December 2020

Insights into the molecular mechanism of membrane fusion from simulation: evidence for the association of splayed tails

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12 December 2020

[Possible mechanism of membrane fusion]

1 reference

12 December 2020

10.1371/JOURNAL.PONE.0038302

Identifiers

DOI

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1 August 2017

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1 August 2017

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