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

An MHC-I Cytoplasmic Domain/HIV-1 Nef Fusion Protein Binds Directly to the μ Subunit of the AP-1 Endosomal Coat Complex

17 Dec 2009

Abstract excerpt

BACKGROUND: The down-regulation of the major histocompatibility complex class I (MHC-I) from the surface of infected cells by the Nef proteins of primate immunodeficiency viruses likely contributes to pathogenesis by providing evasion of cell-mediated immunity. HIV-1 Nef-induced down-regulation involves endosomal trafficking and a cooperative interaction between the cytoplasmic domain (CD) of MHC-I, Nef, and the...

Read the complete abstract on PubMed

Topics

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

Share to HIV Research and Treatment
Share to interferon and immune responses
Share to Viral-associated cancers and disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20020046
DOI: 10.1371/journal.pone.0008364

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An MHC-I Cytoplasmic Domain/HIV-1 Nef Fusion Protein Binds Directly to the μ Subunit of the AP-1 Endosomal Coat ComplexPMID 20020046Read ↗

HIV-1 Nef disrupts intracellular trafficking of major histocompatibility complex class I, CD4, CD8, and CD28 by distinct pathways that share common elements.Semantic proximity Read ↗

The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is necessary for Nef to recruit AP-1 to the major histocompatibility complex class I cytoplasmic tail.Semantic proximity Read ↗

HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tailSemantic proximity Read ↗

Mechanism of Nef-induced CD4 endocytosis: Nef connects CD4 with the mu chain of adaptor complexes.Semantic proximity Read ↗

Negative factor from SIV binds to the catalytic subunit of the V-ATPase to internalize CD4 and to increase viral infectivity.Semantic proximity Read ↗

HIV-1 Nef disrupts antigen presentation early in the secretory pathway.Semantic proximity Read ↗

Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3.Semantic proximity Read ↗

The downregulation of CD4 and MHC‐I by primate lentiviruses: a paradigm for the modulation of cell surface receptorsSemantic proximity Read ↗

An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I.Semantic proximity Read ↗

How HIV Nef Proteins Hijack Membrane Traffic To Promote InfectionSemantic proximity Read ↗

HIV ‐1 Nef: Taking Control of Protein TraffickingSemantic proximity Read ↗

HIV-1 Nef sequesters MHC-I intracellularly by targeting early stages of endocytosis and recyclingSemantic proximity Read ↗

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