Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular Determinants for Recognition of Divergent SAMHD1 Proteins by the Lentiviral Accessory Protein Vpx

1 Apr 2015

Abstract excerpt

The SAMHD1 triphosphohydrolase inhibits HIV-1 infection of myeloid and resting T cells by depleting dNTPs. To overcome SAMHD1, HIV-2 and some SIVs encode either of two lineages of the accessory protein Vpx that bind the SAMHD1 N or C terminus and redirect the host cullin-4 ubiquitin ligase to target SAMHD1 for proteasomal degradation. We present the ternary complex of Vpx from SIV that infects mandrills...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytomegalovirus and herpesvirus research
Share to HIV Research and Treatment
Share to interferon and immune responses

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25856754
DOI: 10.1016/j.chom.2015.03.004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular Determinants for Recognition of Divergent SAMHD1 Proteins by the Lentiviral Accessory Protein VpxPMID 25856754Read ↗

Evolutionary Toggling of Vpx/Vpr Specificity Results in Divergent Recognition of the Restriction Factor SAMHD1Semantic proximity Read ↗

HIV/Simian Immunodeficiency Virus (SIV) Accessory Virulence Factor Vpx Loads the Host Cell Restriction Factor SAMHD1 onto the E3 Ubiquitin Ligase Complex CRL4DCAF1Semantic proximity Read ↗

Vpx overcomes a SAMHD1-independent block to HIV reverse transcription that is specific to resting CD4 T cellsSemantic proximity Read ↗

SAMHD1-Dependent and -Independent Functions of HIV-2/SIV Vpx ProteinSemantic proximity Read ↗

SAMHD1: a new insight into HIV-1 restriction in myeloid cellsSemantic proximity Read ↗

The Ability of Primate Lentiviruses to Degrade the Monocyte Restriction Factor SAMHD1 Preceded the Birth of the Viral Accessory Protein VpxSemantic proximity Read ↗

Functional analysis of the relationship between Vpx and the restriction factor SAMHD1.Semantic proximity Read ↗

Evolutionary and Functional Analyses of the Interaction between the Myeloid Restriction Factor SAMHD1 and the Lentiviral Vpx ProteinSemantic proximity Read ↗

Interplay of ancestral non-primate lentiviruses with the virus-restricting SAMHD1 proteins of their hostsSemantic proximity Read ↗

Co-Evolution of Primate SAMHD1 and Lentivirus Vpx Leads to the Loss of the vpx Gene in HIV-1 AncestorSemantic proximity Read ↗

The Human Immunodeficiency Virus Type 2 Vpx Protein Usurps the CUL4A-DDB1 DCAF1 Ubiquitin Ligase To Overcome a Postentry Block in Macrophage InfectionSemantic proximity Read ↗

Tetramerization of SAMHD1 Is Required for Biological Activity and Inhibition of HIV InfectionSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.