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10.1186/s12977-021-00566-0 · 2021 · External reference

Structure, function, and interactions of the HIV-1 capsid protein

2021 · External reference

HIV-1 capsid stability and reverse transcription are finely balanced to minimize sensing of reverse transcription products via the cGAS-STING pathway

10.1128/mbio.00348-24 · 2024 · External reference

Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication

10.1128/jvi.76.11.5667-5677.2002 · 2002 · External reference

The secrets of the stability of the HIV-1 capsid

2018 · External reference

Capsid lattice destabilization leads to premature loss of the viral genome and integrase enzyme during HIV-1 infection

10.1128/jvi.00984-20 · 2020 · External reference

Pharmacologic hyperstabilisation of the HIV-1 capsid lattice induces capsid failure

2024 · External reference

Efficient HIV-1 in vitro reverse transcription: optimal capsid stability is required

10.1038/s41392-020-00458-3 · 2021 · External reference

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

10.1126/science.abc8420 · 2020 · External reference

The HIV-1 capsid serves as a nanoscale reaction vessel for reverse transcription

10.1371/journal.ppat.1011810 · 2024 · External reference

The host cell metabolite inositol hexakisphosphate promotes efficient endogenous HIV-1 reverse transcription by stabilizing the viral capsid

10.1128/mbio.02820-20 · 2020 · External reference

HIV-1 uncoating requires long double-stranded reverse transcription products

10.1126/sciadv.adn7033 · 2024 · External reference

HIV-1 cores retain their integrity until minutes before uncoating in the nucleus

2021 · External reference

Nuclear capsid uncoating and reverse transcription of HIV-1

10.1146/annurev-virology-020922-110929 · 2022 · External reference

Binding of host factors to stabilized HIV-1 capsid tubes

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A snapshot of HIV-1 capsid-host interactions

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Capsid-dependent host factors in HIV-1 infection

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Interactions of HIV-1 capsid with host factors and their implications for developing novel therapeutics

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HIV-1 uncoating occurs via a series of rapid biomechanical changes in the core related to individual stages of reverse transcription

10.1128/jvi.00166-21 · 2021 · External reference

Reverse transcription mechanically initiates HIV-1 capsid disassembly

10.1128/jvi.00289-17 · 2017 · External reference

HIV-1 capsid uncoating is a multistep process that proceeds through defect formation followed by disassembly of the capsid lattice

10.1021/acsnano.3c07678 · 2024 · External reference

Strain and rupture of HIV-1 capsids during uncoating

2022 · External reference

Revisiting HIV-1 uncoating

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Early cytoplasmic uncoating is associated with infectivity of HIV-1

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Teaching old dogmas new tricks: recent insights into the nuclear import of HIV-1

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HIV-1 replication complexes accumulate in nuclear speckles and integrate into speckle-associated genomic domains

10.1038/s41467-020-17256-8 · 2020 · External reference

HIV-1 requires capsid remodelling at the nuclear pore for nuclear entry and integration

10.1371/journal.ppat.1009484 · 2021 · External reference

Nuclear import of the HIV-1 core precedes reverse transcription and uncoating

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Nuclear import of HIV-1

10.3390/v13112242 · 2021 · External reference

Cone-shaped HIV-1 capsids are transported through intact nuclear pores

10.1016/j.cell.2021.01.025 · 2021 · External reference

Capsid-labelled HIV to investigate the role of capsid during nuclear import and integration

10.1128/jvi.01024-19 · 2020 · External reference

HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex

10.7554/elife.41800 · 2019 · External reference

Tough way In, tough way out: the complex interplay of host and viral factors in nucleocytoplasmic trafficking during HIV-1 infection

10.3390/v14112503 · 2022 · External reference

Correlative in situ cryo-ET reveals cellular and viral remodeling associated with selective HIV-1 core nuclear import

2025 · External reference

Passage of the HIV capsid cracks the nuclear pore

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Elasticity of the HIV-1 core facilitates nuclear entry and infection

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Analysis of the mechanical properties of wild type and hyperstable mutants of the HIV-1 capsid

10.1186/s12977-016-0250-4 · 2016 · External reference

PF74 Reinforces the HIV-1 Capsid to Impair Reverse Transcription-Induced Uncoating

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Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo

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Microtubule-associated proteins 1 (MAP1) promote human immunodeficiency virus type I (HIV-1) intracytoplasmic routing to the nucleus

10.1074/jbc.m114.613133 · 2015 · External reference

HIV-1 induces the formation of stable microtubules to enhance early infection

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

10.1038/s41564-020-0735-8 · 2020 · External reference