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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac

Retrovirology, 2012-06, Vol.9 (1), p.49-49, Article 49

2012

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Nuclear Import of the HIV-1 Core Precedes Reverse Transcription and Uncoating

Cell reports (Cambridge), 2020-09, Vol.32 (13), p.108201-108201, Article 108201

2020

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HIV-1 uncoating is facilitated by dynein and kinesin 1

Journal of virology, 2014-12, Vol.88 (23), p.13613-13625

2014

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Inhibition of Reverse Transcriptase Activity Increases Stability of the HIV-1 Core

Journal of Virology, 2013-01, Vol.87 (1), p.683-687

2013

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Bicaudal D2 facilitates the cytoplasmic trafficking and nuclear import of HIV-1 genomes during infection

Proceedings of the National Academy of Sciences - PNAS, 2017-12, Vol.114 (50), p.E10707-E10716

2017

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Structural basis of HIV-1 capsid recognition by PF74 and CPSF6

Proceedings of the National Academy of Sciences - PNAS, 2014-12, Vol.111 (52), p.18625-18630

2014

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Identification and characterization of naturally occurring splice variants of SAMHD1

Retrovirology, 2012-10, Vol.9 (1), p.86-86, Article 86

2012

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The ribonuclease activity of SAMHD1 is required for HIV-1 restriction

Nature medicine, 2014-08, Vol.20 (8), p.936-941

2014

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SAMHD1 Restricts Herpes Simplex Virus 1 in Macrophages by Limiting DNA Replication

Journal of Virology, 2013-12, Vol.87 (23), p.12949-12956

2013

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Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in Nondividing Cells

Journal of virology, 2018-10, Vol.92 (19), p.e00648-18

2018

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Cyclophilin A Prevents HIV-1 Restriction in Lymphocytes by Blocking Human TRIM5α Binding to the Viral Core

Cell reports (Cambridge), 2020-03, Vol.30 (11), p.3766-3777.e6

2020

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HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus

Nature communications, 2015-03, Vol.6 (1), p.6660-6660, Article 6660

2015

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The fate of HIV-1 capsid: a biochemical assay for HIV-1 uncoating

Methods in molecular biology (Clifton, N.J.), 2014-01, Vol.1087, p.29

2014

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Formation of nuclear CPSF6/CPSF5 biomolecular condensates upon HIV-1 entry into the nucleus is important for productive infection

Scientific reports, 2023-07, Vol.13 (1), p.10974-10974, Article 10974

2023

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Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration

PloS one, 2012-09, Vol.7 (9), p.e46037-e46037

2012

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Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication

Virology (New York, N.Y.), 2013-05, Vol.440 (1), p.8-18

2013

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Specific Recognition and Accelerated Uncoating of Retroviral Capsids by the TRIM5α Restriction Factor

Proceedings of the National Academy of Sciences - PNAS, 2006-04, Vol.103 (14), p.5514-5519

2006

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Biochemical detection of capsid in the nucleus during HIV-1 infection

STAR protocols, 2021-03, Vol.2 (1), p.100323-100323, Article 100323

2021

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Ebselen, a Small-Molecule Capsid Inhibitor of HIV-1 Replication

Antimicrobial agents and chemotherapy, 2016-04, Vol.60 (4), p.2195-2208

2016

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The HIV-1 capsid core is an opportunistic nuclear import receptor

Nature communications, 2023-06, Vol.14 (1), p.3782-3782, Article 3782

2023

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Dephosphorylation of the HIV-1 restriction factor SAMHD1 is mediated by PP2A-B55α holoenzymes during mitotic exit

Nature communications, 2018-06, Vol.9 (1), p.2227-16, Article 2227

2018

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Role of lysosome rupture in controlling Nlrp3 signaling and necrotic cell death

Cell cycle (Georgetown, Tex.), 2013-06, Vol.12 (12), p.1868-1878

2013

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Contribution of SAM and HD domains to retroviral restriction mediated by human SAMHD1

Virology (New York, N.Y.), 2013-02, Vol.436 (1), p.81-90

2013

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MxB binds to the HIV-1 core and prevents the uncoating process of HIV-1

Retrovirology, 2014-08, Vol.11 (1), p.68-68, Article 68

2014

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Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification

Nature communications, 2021-02, Vol.12 (1), p.731-14, Article 731

2021

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Role of SAMHD1 nuclear localization in restriction of HIV-1 and SIVmac

Nuclear Import of the HIV-1 Core Precedes Reverse Transcription and Uncoating

HIV-1 uncoating is facilitated by dynein and kinesin 1

Inhibition of Reverse Transcriptase Activity Increases Stability of the HIV-1 Core

Bicaudal D2 facilitates the cytoplasmic trafficking and nuclear import of HIV-1 genomes during infection

Structural basis of HIV-1 capsid recognition by PF74 and CPSF6

Identification and characterization of naturally occurring splice variants of SAMHD1

The ribonuclease activity of SAMHD1 is required for HIV-1 restriction

SAMHD1 Restricts Herpes Simplex Virus 1 in Macrophages by Limiting DNA Replication

Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in Nondividing Cells

Cyclophilin A Prevents HIV-1 Restriction in Lymphocytes by Blocking Human TRIM5α Binding to the Viral Core

HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus

The fate of HIV-1 capsid: a biochemical assay for HIV-1 uncoating

Formation of nuclear CPSF6/CPSF5 biomolecular condensates upon HIV-1 entry into the nucleus is important for productive infection

Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration

Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication

Specific Recognition and Accelerated Uncoating of Retroviral Capsids by the TRIM5α Restriction Factor

Biochemical detection of capsid in the nucleus during HIV-1 infection

Ebselen, a Small-Molecule Capsid Inhibitor of HIV-1 Replication

The HIV-1 capsid core is an opportunistic nuclear import receptor

Dephosphorylation of the HIV-1 restriction factor SAMHD1 is mediated by PP2A-B55α holoenzymes during mitotic exit

Role of lysosome rupture in controlling Nlrp3 signaling and necrotic cell death

Contribution of SAM and HD domains to retroviral restriction mediated by human SAMHD1

MxB binds to the HIV-1 core and prevents the uncoating process of HIV-1

Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification

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