A lysine ring in HIV capsid pores coordinates IP6 to drive mature capsid assembly

HIV-1 uncoats in the nucleus near sites of integration

(2020) Ryan C. Burdick et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Self-Assembly of Fluorescent HIV Capsid Spheres for Detection of Capsid Binders

(2020) Derrick Lau et al.   LANGMUIR

Nuclear pore blockade reveals that HIV-1 completes reverse transcription and uncoating in the nucleus

(2020) Adarsh Dharan et al.   Nature Microbiology

Reconstitution and visualization of HIV-1 capsid-dependent replication and integration in vitro

(2020) Devin E. Christensen et al.   SCIENCE

Novel Intersubunit Interaction Critical for HIV-1 Core Assembly Defines a Potentially Targetable Inhibitor Binding Pocket

(2019) Pierrick Craveur et al.   mBio

Structure-based insights into the mechanism of nucleotide import by HIV-1 capsid

(2019) Guang Song   JOURNAL OF STRUCTURAL BIOLOGY

Fluorescence Biosensor for Real-Time Interaction Dynamics of Host Proteins with HIV-1 Capsid Tubes

(2019) Derrick Lau et al.   ACS Applied Materials & Interfaces

Cellular IP6 Levels Limit HIV Production while Viruses that Cannot Efficiently Package IP6 Are Attenuated for Infection and Replication

(2019) Donna L. Mallery et al.   Cell Reports

Kinetics of HIV-1 capsid uncoating revealed by single-molecule analysis

(2018) Chantal L Márquez et al.   eLife

IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis

(2018) Donna L Mallery et al.   eLife

Inositol phosphates are assembly co-factors for HIV-1

(2018) Robert A. Dick et al.   NATURE

HIV-1 uses dynamic capsid pores to import nucleotides and fuel encapsidated DNA synthesis

(2016) David A. Jacques et al.   NATURE

HIV-1 capsid uncoating initiates after the first strand transfer of reverse transcription

(2016) Ophélie Cosnefroy et al.   Retrovirology

The structure and flexibility of conical HIV-1 capsids determined within intact virions

(2016) Simone Mattei et al.   SCIENCE

Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5α

(2016) Jonathan M Wagner et al.   eLife

HIV-1 uncoating: connection to nuclear entry and regulation by host proteins

(2014) Zandrea Ambrose et al.   VIROLOGY

Host Cofactors and Pharmacologic Ligands Share an Essential Interface in HIV-1 Capsid That Is Lost upon Disassembly

(2014) Amanda J. Price et al.   PLoS Pathogens

In Vitro Assembly of Retroviruses

(2014) Di L. Bush et al.   Annual Review of Virology

How good are my data and what is the resolution?

(2013) Philip R. Evans et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Retrovirus Restriction by TRIM5 Proteins Requires Recognition of Only a Small Fraction of Viral Capsid Subunits

(2013) J. Shi et al.   JOURNAL OF VIROLOGY

Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics

(2013) Gongpu Zhao et al.   NATURE

Extreme Genetic Fragility of the HIV-1 Capsid

(2013) Suzannah J. Rihn et al.   PLoS Pathogens

Second-site suppressors of HIV-1 capsid mutations: restoration of intracellular activities without correction of intrinsic capsid stability defects

(2012) Ruifeng Yang et al.   Retrovirology

Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating

(2011) Till Böcking et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Complementary assays reveal a relationship between HIV-1 uncoating and reverse transcription

(2011) A. E. Hulme et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Determinants of the HIV-1 core assembly pathway

(2011) Claudia S. López et al.   VIROLOGY

X-Ray Structures of the Hexameric Building Block of the HIV Capsid

(2009) Owen Pornillos et al.   CELL

The MORPHEUS protein crystallization screen

(2009) Fabrice Gorrec   JOURNAL OF APPLIED CRYSTALLOGRAPHY

Active site remodeling switches HIV specificity of antiretroviral TRIMCyp

(2009) Amanda J Price et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY