A peptide inhibitor of HIV-1 assembly in vitro (original) (raw)
Assembly and Architecture of HIV
Mark Yeager
Viral Molecular Machines, 2011
View PDFchevron_right
The structural biology of HIV assembly
Mark Yeager
Current Opinion in Structural Biology, 2008
View PDFchevron_right
HIV-1 Gag Processing Intermediates Trans-dominantly Interfere with HIV-1 Infectivity
Krisztina Nikovics
Journal of Biological Chemistry, 2009
View PDFchevron_right
The Conserved Carboxy Terminus of the Capsid Domain of Human Immunodeficiency Virus Type 1 Gag Protein Is Important for Virion Assembly and Release
M. Mark-Danieli, Nir Ben-tal
Journal of Virology, 2004
View PDFchevron_right
Proteasome inhibition interferes with Gag polyprotein processing, release, and maturation of HIV-1 and HIV-2
Elena Chertova
Proceedings of the National Academy of Sciences, 2000
View PDFchevron_right
Peptide Inhibitors of HIV-1 Egress
Abdul Waheed
ACS Chemical Biology, 2008
View PDFchevron_right
Crystal structure of an HIV assembly and maturation switch
Mark Yeager
eLife, 2016
View PDFchevron_right
HIV-1 Assembly, Release and Maturation
Nathalie Chazal
World Journal of AIDS, 2011
View PDFchevron_right
Analysis of the initiating events in HIV-1 particle assembly and genome packaging
Sebla Döner
PLoS pathogens, 2010
View PDFchevron_right
Preparation of recombinant HIV-1 gag protein and assembly of virus-like particles in vitro
Siddhartha Datta
Methods in molecular biology (Clifton, N.J.), 2009
View PDFchevron_right
Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly …
Timothy Stemmler
The EMBO Journal, 1998
View PDFchevron_right
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
Chun Tang
Nature structural biology, 2002
View PDFchevron_right
The isolated major homology region of the HIV capsid protein is mainly unfolded in solution and binds to the intact protein
Adrian Velazquez-Campoy
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2011
View PDFchevron_right
Time Course of Gag Protein Assembly in HIV-1-Infected Cells: A Study by Immunoelectron Microscopy
Fedor Ciampor
Virology, 2003
View PDFchevron_right
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles
Etienne Decroly
Biochemical and Biophysical Research Communications, 2004
View PDFchevron_right
Identification of a host protein essential for assembly of immature HIV-1 capsids
Aalok Singh
Nature, 2002
View PDFchevron_right
Electrostatic repulsion between HIV-1 capsid proteins modulates hexamer plasticity and in vitro assembly
Bernard Gay
Proteins: Structure, Function, and Bioinformatics, 2010
View PDFchevron_right
Immature HIV-1 assembles from Gag dimers leaving partial hexamers at lattice edges as substrates for proteolytic maturation
aaron tan
2020
View PDFchevron_right
Plasma membrane is the site of productive HIV-1 particle assembly
Nolwenn Jouvenet
PLoS biology, 2006
View PDFchevron_right
Residues in the HIV-1 Capsid Assembly Inhibitor Binding Site Are Essential for Maintaining the Assembly-competent Quaternary Structure of the Capsid Protein
Peter Sehr
Journal of Biological Chemistry, 2008
View PDFchevron_right
Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells
Volker Brinkmann
Virology, 1992
View PDFchevron_right
Efficient support of virus-like particle assembly by the HIV-1 packaging signal
Siddhartha Datta
eLife, 2018
View PDFchevron_right
Assembly of Immature HIV-1 Capsids Using a Cell-Free System
Beth Thielen
Methods in Molecular Biology, 2009
View PDFchevron_right
On the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?
Siddhartha Datta
Journal of Virology, 2011
View PDFchevron_right
The effect of purification method on the completeness of the immature HIV-1 Gag shell
L. Hevroni, Nitzan Kol
Journal of Virological Methods, 2010
View PDFchevron_right
Conformation of the HIV-1 Gag Protein in Solution
Joseph Curtis
Journal of Molecular Biology, 2007
View PDFchevron_right
The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles
Fu-der Wang
Virology, 2004
View PDFchevron_right
Vif Is Largely Absent from Human Immunodeficiency Virus Type 1 Mature Virions and Associates Mainly with Viral Particles Containing Unprocessed Gag
David Volsky
Journal of Virology, 2001
View PDFchevron_right
Flexibility in HIV1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid Protein
Francisco Barrera
Biophysical Journal, 2007
View PDFchevron_right
Removal of human immunodeficiency virus type 1 (HIV-1) protease inhibitors from preparations of immature HIV-1 virions does not result in an increase in infectivity or the appearance of mature morphology
TOMINAGA FUKAZAWA
Antimicrobial Agents and Chemotherapy, 1997
View PDFchevron_right
Characterization of the In Vitro HIV-1 Capsid Assembly Pathway
Claudia López
Journal of Molecular Biology, 2009
View PDFchevron_right