Membrane interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs (original) (raw)

Mode of Action of an Antiviral Peptide from HIV-1. INHIBITION AT A POST-LIPID MIXING STAGE

Journal of Biological Chemistry, 2001

HIV-1 Membrane Fusion Mechanism: Structural Studies of the Interactions between Biologically-Active Peptides from gp41

Biochemistry, 1996

Fusion Peptides Derived from the HIV Type 1 Glycoprotein 41 Associate within Phospholipid Membranes and Inhibit Cell-Cell Fusion. STRUCTURE-FUNCTION STUDY

Yossef Kliger

Journal of Biological Chemistry, 1997

View PDFchevron_right

The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids

Cyril Curtain

European Biophysics Journal, 1999

View PDFchevron_right

Mode of Action of an Antiviral Peptide from HIV-1

Yossef Kliger

Journal of Biological Chemistry, 2001

View PDFchevron_right

Structural Analysis and Assembly of the HIV-1 Gp41 Amino-Terminal Fusion Peptide and the Pretransmembrane Amphipathic-At-Interface Sequence †

David Andreu

Biochemistry, 2006

View PDFchevron_right

Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using 13C-enhanced Fourier transform infrared spectroscopy

Mark Sherman

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2002

View PDFchevron_right

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

Cyril Curtain

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1992

View PDFchevron_right

Conformational Stability and Membrane Interaction of the Full-Length Ectodomain of HIV-1 gp41: Implication for Mode of Action †

Richard Epand

Biochemistry, 2009

View PDFchevron_right

Conformational Partitioning of the Fusion Peptide of HIV-1 gp41 and Its Structural Analogs in Bilayer Membranes

Marjorie Longo

Biophysical Journal, 2002

View PDFchevron_right

Biophysical Characterization of the Structure of the Amino-terminal Region of gp41 of HIV-1. IMPLICATIONS ON VIRAL FUSION MECHANISM

Ding-kwo Chang

Journal of Biological Chemistry, 1999

View PDFchevron_right

Membrane-induced conformational change during the activation of HIV-1 gp41 1 1 Edited by A. R. Fersht

Yossef Kliger

J Mol Biol, 2000

View PDFchevron_right

Effect of E1(64–81) hepatitis G peptide on the in vitro interaction of HIV-1 fusion peptide with membrane models

María Sánchez-martín, Ma Antònia Busquets

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2011

View PDFchevron_right

The N-terminal 12 Residue Long Peptide of HIV gp41 is the Minimal Peptide Sufficient to Induce Significant T-cell-like Membrane Destabilization in Vitro

Benoit Charloteaux

Journal of Molecular Biology, 2006

View PDFchevron_right

Adopted Conformations in Membranes by the HIV1 Fusion Peptide

Nerea Huarte A

2010

View PDFchevron_right

Comparative Analysis of Membrane-Associated Fusion Peptide Secondary Structure and Lipid Mixing Function of HIV gp41 Constructs that Model the Early Pre-Hairpin Intermediate and Final Hairpin Conformations

Richard Epand

Journal of Molecular Biology, 2010

View PDFchevron_right

Membranotropic effects of peptides from the V3 loop of HIV-1

Anna Petrukhina

Letters in Peptide Science, 1998

View PDFchevron_right

Structure and Interaction with Membrane Model Systems of a Peptide Derived from the Major Epitope Region of HIV Protein gp41: Implications on Viral Fusion Mechanism

Mariela Gavilan

Biochemistry, 2001

View PDFchevron_right

Characterization of the Interaction of Two Peptides from the N Terminus of the NHR Domain of HIV-1 gp41 with Phospholipid Membranes †

Jaime Guillen

Biochemistry, 2007

View PDFchevron_right

Physicochemical characterization of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide: interaction with model membranes

MONTSERRAT PUJOL, Antonio Cruz

International journal of pharmaceutics, 2012

View PDFchevron_right

Membrane-induced conformational change during the activation of HIV-1 gp41

Yossef Kliger

Journal of Molecular Biology, 2000

View PDFchevron_right

Crystal Structure of HIV-1 gp41 Including Both Fusion Peptide and Membrane Proximal External Regions

Winfried Weissenhorn

PLoS Pathogens, 2010

View PDFchevron_right

Study of the inhibition capacity of an 18-mer peptide domain of GBV-C virus on gp41-FP HIV-1 activity

Isabel Haro

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2011

View PDFchevron_right

Study of the inhibition capacity of a 18-mer peptide domain of GBV-C virus on gp41-FP HIV-1 activity

Victoria Girona

2011

View PDFchevron_right

A Peptide Pertaining to the Loop Segment of Human Immunodeficiency Virus gp41 Binds and Interacts with Model Biomembranes: Implications for the Fusion Mechanism

Roberto Pascual

Journal of Virology, 2005

View PDFchevron_right

The LLSGIV stretch of the N-terminal region of HIV-1 gp41 is critical for binding to a model peptide, T20

Ding-kwo Chang

Protein …, 2003

View PDFchevron_right

Membrane-Anchored Inhibitory Peptides Capture Human Immunodeficiency Virus Type 1 gp41 Conformations That Engage the Target Membrane prior to Fusion

dorothee von laer

Journal of Virology, 2006

View PDFchevron_right

HIV-1 fusion inhibitor peptides enfuvirtide and T-1249 interact with erythrocyte and lymphocyte membranes

Pedro Matos

PloS One, 2010

View PDFchevron_right

Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation 1 1 Edited by J. Karn

Yossef Kliger

J Mol Biol, 2000

View PDFchevron_right

Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation

Yossef Kliger

Journal of Molecular Biology, 2000

View PDFchevron_right

Both lipid environment and pH are critical for determining physiological solution structure of 3-D-conserved epitopes of the HIV-1 gp41-MPER peptide P1

Patrick Curmi

The FASEB Journal, 2008

View PDFchevron_right

Membrane interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs (original) (raw)

Related papers