Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation (original) (raw)
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
Mode of Action of an Antiviral Peptide from HIV-1
Yossef Kliger
Journal of Biological Chemistry, 2001
View PDFchevron_right
Mode of Action of an Antiviral Peptide from HIV-1. INHIBITION AT A POST-LIPID MIXING STAGE
Yossef Kliger
Journal of Biological Chemistry, 2001
View PDFchevron_right
Conformational Changes in HIV-1 gp41 in the Course of HIV-1 Envelope Glycoprotein-Mediated Fusion and Inactivation †
G. Marius Clore FRS
Biochemistry, 2005
View PDFchevron_right
Inhibiting HIV-1 Entry
Debra Eckert
Cell, 1999
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
Propensity for a Leucine Zipper-Like Domain of Human Immunodeficiency Virus Type 1 gp41 to Form Oligomers Correlates with a Role in Virus-Induced Fusion Rather than Assembly of the Glycoprotein Complex
Terrence Hunter
Proceedings of The National Academy of Sciences, 1994
View PDFchevron_right
Structural Investigation of the HIV-1 Envelope Glycoprotein gp160 Cleavage Site, 2: Relevance of an N-Terminal Helix
L. Falcigno, Gabriella D'Auria
ChemBioChem, 2003
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 interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs
Mark Sherman
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1999
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
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
HIV-1 Membrane Fusion Mechanism: Structural Studies of the Interactions between Biologically-Active Peptides from gp41
Kelly Guthrie
Biochemistry, 1996
View PDFchevron_right
Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide
Sonu Kumar
Nature Communications, 2019
View PDFchevron_right
A Covalent Inhibitor Targeting an Intermediate Conformation of the Fusogenic Subunit of the HIV-1 Envelope Complex
Xicai Huang
Journal of Biological Chemistry, 2007
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
Biophysical evidence of two docking sites of the carboxyl heptad repeat region within the amino heptad repeat region of gp41 of human immunodeficiency virus type 1
Ding-kwo Chang
Antiviral Research, 2007
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
Structural Mechanism of Trimeric HIV-1 Envelope Glycoprotein Activation
Gabriel Frank
PLoS Pathogens, 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
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
HIV gp41 C-terminal Heptad Repeat Contains Multifunctional Domains: RELATION TO MECHANISMS OF ACTION OF ANTI-HIV PEPTIDES
Byron Cheung
Journal of Biological Chemistry, 2007
View PDFchevron_right
Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: Functional complementation of specific defects in gp120 and gp41
Edward Berger
Proceedings of the National Academy of Sciences, 2000
View PDFchevron_right
Temperature-Dependent Intermediates in HIV-1 Envelope Glycoprotein-Mediated Fusion Revealed by Inhibitors that Target N- and C-Terminal Helical Regions of HIV-1 gp41
G. Marius Clore FRS
Biochemistry, 2004
View PDFchevron_right
Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion
Stephen Harrison
Proceedings of the National Academy of Sciences, 2006
View PDFchevron_right
Structural and Functional Roles of HIV-1 gp41 Pretransmembrane Sequence Segmentation
Ibon Iloro
Biophysical Journal, 2003
View PDFchevron_right
The Conserved Residue Arg46 in the N-Terminal Heptad Repeat Domain of HIV-1 gp41 Is Critical for Viral Fusion and Entry
lu lu
PLoS ONE, 2012
View PDFchevron_right
Non-peptide entry inhibitors of HIV-1 that target the gp41 coiled coil pocket
Steve Anderson
Bioorganic & Medicinal Chemistry Letters, 2010
View PDFchevron_right
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
Debra Eckert
Proceedings of the National Academy of Sciences of the United States of America, 2001
View PDFchevron_right
Prediction and validation of HIV-1 gp41 ecto-transmembrane domain post-fusion trimeric structure using molecular modeling
biswajit gorai
Journal of Biomolecular Structure and Dynamics, 2019
View PDFchevron_right
Conformational Differences Between Functional Human Immunodeficiency Virus (HIV-1) Envelope Glycoprotein Trimers and Stabilized Soluble Trimers
Hanh Nguyen
Journal of Virology, 2018
View PDFchevron_right
Role for the Terminal Clasp of HIV-1 gp41 Glycoprotein in the Initiation of Membrane Fusion
David Stapleton
Journal of Biological Chemistry, 2011
View PDFchevron_right
Identification of membrane-active regions of the HIV-1 envelope glycoprotein gp41 using a 15-mer gp41-peptide scan
Roberto Pascual
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2004
View PDFchevron_right
A Peptide from the Heptad Repeat of Human Immunodeficiency Virus gp41 Shows both Membrane Binding and Coiled-Coil Formation
Mark Rabenstein
Biochemistry, 1995
View PDFchevron_right
Computational study of bindings of HL9, a nonapeptide fragment of human lysozyme, to HIV1 fusion protein gp41
Dwi Angelina
Bioorganic & Medicinal Chemistry Letters, 2011
View PDFchevron_right