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

Modulation of Cellular Protein Trafficking by Human Immunodeficiency Virus Type 1 Nef: Role of the Acidic Residue in the ExxxLL Motif

26 Jan 2006

Abstract excerpt

The nef gene contributes to the replication of primate lentiviruses by altering the trafficking of cellular proteins involved in adaptive immunity (class I and II major histocompatibility complex [MHC]) and viral transmission (CD4 and DC-SIGN). A conserved acidic leucine-based sequence (E(160)xxxLL) within human immunodeficiency virus type 1 (HIV-1) Nef binds to the cellular adaptor protein (AP) complexes, which...

Read the complete abstract on PubMed

Topics

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

Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment
Share to Immune Cell Function and Interaction

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 16439540
DOI: 10.1128/jvi.80.4.1837-1849.2006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Modulation of Cellular Protein Trafficking by Human Immunodeficiency Virus Type 1 Nef: Role of the Acidic Residue in the ExxxLL MotifPMID 16439540Read ↗

Human Immunodeficiency Virus Type 1 Nef: Adapting to Intracellular Trafficking PathwaysSemantic proximity Read ↗

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 ↗

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

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

Functional characterization of the human immunodeficiency virus type 1 Nef acidic domain.Semantic proximity Read ↗

Maintenance of AP-2-Dependent Functional Activities of Nef Restricts Pathways of Immune Escape from CD8 T Lymphocyte Responses.Semantic proximity Read ↗

One Protein to Rule them All: Modulation of Cell Surface Receptors and Molecules by HIV NefSemantic 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 ↗

Identification of a novel binding site between HIV type 1 Nef C-terminal flexible loop and AP2 required for Nef-mediated CD4 downregulation.Semantic 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 ↗

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