Extracellular ATP acts on P2Y2 purinergic receptors to facilitate HIV-1 infection.

doi:10.1084/jem.20101805

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

Community

Back to search

Article

Extracellular ATP acts on P2Y2 purinergic receptors to facilitate HIV-1 infection.

The Journal of experimental medicine - 29 Aug 2011

Séror Claire, Melki Marie-Thérèse, Subra Frédéric, Raza Syed Qasim, Bras Marlène, Saïdi Héla, Nardacci Roberta, Voisin Laurent, Paoletti Audrey, Law Frédéric, Martins Isabelle, Amendola Alessandra, Abdul-Sater Ali A, Ciccosanti Fabiola, Delelis Olivier, Niedergang Florence, Thierry Sylvain, Said-Sadier Najwane, Lamaze Christophe, Métivier Didier, Estaquier Jérome, Fimia Gian Maria, Falasca Laura, Casetti Rita, Modjtahedi Nazanine, Kanellopoulos Jean, Mouscadet Jean-François, Ojcius David M, Piacentini Mauro, Gougeon Marie-Lise, Kroemer Guido, Perfettini Jean-Luc

Abstract excerpt

Extracellular adenosine triphosphate (ATP) can activate purinergic receptors of the plasma membrane and modulate multiple cellular functions. We report that ATP is released from HIV-1 target cells through pannexin-1 channels upon interaction between the HIV-1 envelope protein and specific target cell receptors. Extracellular ATP then acts on purinergic receptors, including P2Y2, to activate proline-rich tyrosine...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Antiretroviral Therapy, Highly Active

Share to Cell Membrane

Share to Connexins

Share to Drug Resistance, Viral

Share to Enzyme Activation

Share to Focal Adhesion Kinase 2

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 21859844
DOI: 10.1084/jem.20101805
PMCID: PMC3171090

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Extracellular ATP acts on P2Y2 purinergic receptors to facilitate HIV-1 infection.PMID 21859844Read ↗

P2X1 Selective Antagonists Block HIV-1 Infection through Inhibition of Envelope Conformation-Dependent Fusion.Semantic proximity Read ↗

P2Y11 Receptors: Properties, Distribution and Functions.Semantic proximity Read ↗

Molecular dissection of purinergic P2X receptor channels.Semantic proximity Read ↗

Overview of the P2 receptors.Semantic proximity Read ↗

Circulating levels of ATP is a biomarker of HIV cognitive impairmentSemantic proximity Read ↗

HIV-Tat Protein Forms Phosphoinositide-dependent Membrane Pores Implicated in Unconventional Protein Secretion.Semantic proximity Read ↗

Allosteric modulation of ATP-gated P2X receptor channels.Semantic proximity Read ↗

Signal transduction due to HIV-1 envelope interactions with chemokine receptors CXCR4 or CCR5.Semantic proximity Read ↗

Endothelial pannexin 1 channels control inflammation by regulating intracellular calciumSemantic proximity Read ↗

P2X7 receptor activation regulates rapid unconventional export of transglutaminase-2.Semantic proximity Read ↗

“Host Tissue Damage” Signal ATP Promotes Non-directional Migration and Negatively Regulates Toll-like Receptor Signaling in Human MonocytesSemantic proximity Read ↗

[Structual and functional dynamics of the ATP receptor channel P2X(2)].Semantic proximity Read ↗

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