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Peptide Folding: When Simulation Meets Experiment
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Comparative Protein Modelling by Satisfaction of Spatial Restraints
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Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses 1 1Edited by P. E. Wright
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Multi-resolution contour-based fitting of macromolecular structures
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Clustering Rules: A Comparison of Partitioning and Hierarchical Clustering Algorithms
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Using Situs for the integration of multi-resolution structures
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VMD: Visual molecular dynamics
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Replica-exchange molecular dynamics method for protein folding
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Structure and self-association of the Rous sarcoma virus capsid protein
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Human Immunodeficiency Virus Type 1 Assembly, Release, and Maturation
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Three-Dimensional Analysis of Budding Sites and Released Virus Suggests a Revised Model for HIV-1 Morphogenesis
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Dimeric Rous Sarcoma Virus Capsid Protein Structure Relevant to Immature Gag Assembly
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January 2004 |
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Three-dimensional Structure of HIV-1 Virus-like Particles by Electron Cryotomography
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Cryo-electron Microscopy Reveals Conserved and Divergent Features of Gag Packing in Immature Particles of Rous Sarcoma Virus and Human Immunodeficiency Virus
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January 2006 |
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Interactions between HIV-1 Gag Molecules in Solution: An Inositol Phosphate-mediated Switch
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RSV Capsid Polymorphism Correlates with Polymerization Efficiency and Envelope Glycoprotein Content: Implications that Nucleation Controls Morphogenesis
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Retroviral Capsid Assembly: A Role for the CA Dimer in Initiation
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A Structural Model for the Generation of Continuous Curvature on the Surface of a Retroviral Capsid
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Molecular dynamics simulations of large macromolecular complexes
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April 2015 |
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Proton-Linked Dimerization of a Retroviral Capsid Protein Initiates Capsid Assembly
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HIV Gag polyprotein: processing and early viral particle assembly
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Elements in HIV-1 Gag contributing to virus particle assembly
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Exchange Often and Properly in Replica Exchange Molecular Dynamics
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Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone ϕ, ψ and Side-Chain χ 1 and χ 2 Dihedral Angles
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Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies
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A molecular switch required for retrovirus assembly participates in the hexagonal immature lattice
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April 2008 |
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Visualization of a missing link in retrovirus capsid assembly
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February 2009 |
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Atomic-level modelling of the HIV capsid
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January 2011 |
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Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy
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Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics
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Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution
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A de novo peptide hexamer with a mutable channel
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Maturation of the HIV-1 core by a non-diffusional phase transition
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January 2015 |
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The stoichiometry of Gag protein in HIV-1
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June 2004 |
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Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
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Hierarchical coarse-graining strategy for protein-membrane systems to access mesoscopic scales
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Structure and assembly of immature HIV
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An atomic-level mechanism for activation of the kinesin molecular motors
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Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly
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Direct measurement of Gag–Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy
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HIV Type 1 Gag as a Target for Antiviral Therapy
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Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
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Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: Implications for particle assembly and RNA packaging
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Flexibility in the P2 domain of the HIV-1 Gag polyprotein
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Structure of the Carboxyl-Terminal Dimerization Domain of the HIV-1 Capsid Protein
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On the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?
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Mutations in the Spacer Peptide and Adjoining Sequences in Rous Sarcoma Virus Gag Lead to Tubular Budding
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Potential Role for CA-SP in Nucleating Retroviral Capsid Maturation
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Overlapping Roles of the Rous Sarcoma Virus Gag p10 Domain in Nuclear Export and Virion Core Morphology
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July 2007 |
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Myristoylation Is Required for Human Immunodeficiency Virus Type 1 Gag-Gag Multimerization in Mammalian Cells
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A Two-Pronged Structural Analysis of Retroviral Maturation Indicates that Core Formation Proceeds by a Disassembly-Reassembly Pathway Rather than a Displacive Transition
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October 2013 |
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Conserved and Variable Features of Gag Structure and Arrangement in Immature Retrovirus Particles
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September 2010 |
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Higher-Order Structure of the Rous Sarcoma Virus SP Assembly Domain
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March 2014 |
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Genetic Determinants of Rous Sarcoma Virus Particle Size
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Roles of Matrix, p2, and N-Terminal Myristoylation in Human Immunodeficiency Virus Type 1 Gag Assembly
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Viral DNA Synthesis Defects in Assembly-Competent Rous Sarcoma Virus CA Mutants
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Characterization of Rous Sarcoma Virus Gag Particles Assembled In Vitro
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March 2001 |
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Rous Sarcoma Virus Gag Protein-Oligonucleotide Interaction Suggests a Critical Role for Protein Dimer Formation in Assembly
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June 2002 |
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Charged Assembly Helix Motif in Murine Leukemia Virus Capsid: an Important Region for Virus Assembly and Particle Size Determination
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June 2003 |
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A Structurally Disordered Region at the C Terminus of Capsid Plays Essential Roles in Multimerization and Membrane Binding of the Gag Protein of Human Immunodeficiency Virus Type 1
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February 2003 |
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Functional Surfaces of the Human Immunodeficiency Virus Type 1 Capsid Protein
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May 2003 |
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Nucleic Acid Binding-Induced Gag Dimerization in the Assembly of Rous Sarcoma Virus Particles In Vitro
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Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus gag protein.
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The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity.
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In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles.
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Protease Cleavage Leads to Formation of Mature Trimer Interface in HIV-1 Capsid
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Virus maturation as a new HIV-1 therapeutic target
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