The molecular area characteristics of the HIV-1 gp41-fusion peptide at the air/water interface. Effect of pH. (Q34432095)

2 August 2017

title

The molecular area characteristics of the HIV-1 gp41-fusion peptide at the air/water interface. Effect of pH. (English)

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2 August 2017

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S E Taylor

1

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2 August 2017

G Schwarz

series ordinal

2

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2 August 2017

language of work or name

English

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publication date

1 June 1997

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Biochimica et Biophysica Acta

2 August 2017

published in

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2 August 2017

volume

1326

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2 August 2017

issue

2

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2 August 2017

page(s)

257-264

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

2 August 2017

cites work

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7 January 2021

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Are fusion peptides really "sided" insertional helices?

7 January 2021

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Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41.

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The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation

7 January 2021

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The nature of the accessible and buried surfaces in proteins

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The amino-terminal peptide of HIV-1 glycoprotein 41 lyses human erythrocytes and CD4+ lymphocytes

7 January 2021

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Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage

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Preferential partitioning of melittin into the air/water interface: structural and thermodynamic implications

7 January 2021

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Inhibition of Human Immunodeficiency Virus Type 1 (HIV-1) Penetration into Target Cells by Synthetic Peptides Mimicking the N-Terminus of the HIV-1 Transmembrane Glycoprotein

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7 January 2021

Identifiers

DOI

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2 August 2017

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