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

A long N-terminal-extended nested set of abundant and antigenic major histocompatibility complex class I natural ligands from HIV envelope protein.

The Journal of biological chemistry - 10 Mar 2006

Samino Yolanda, López Daniel, Guil Sara, Saveanu Loredana, van Endert Peter M, Del Val Margarita

Abstract excerpt

Viral antigens complexed with major histocompatibility complex (MHC) class I molecules are recognized by cytotoxic T lymphocytes on infected cells. Assays with synthetic peptides identify optimal MHC class I ligands often used for vaccines. However, when natural peptides are analyzed, more complex mixtures including long peptides bulging in the middle of the binding site or with carboxyl extensions are found,...

Read the complete abstract on PubMed

Topics

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

Share to Endoplasmic Reticulum
Share to Epitopes, T-Lymphocyte

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

Share to Histocompatibility Antigens Class I

Share to HIV Envelope Protein gp160

Share to L Cells

Share to Lipoproteins

Share to Peptide Fragments

Share to T-Lymphocytes, Cytotoxic

Source

Identifiers

PMID: 16407287
DOI: 10.1074/jbc.M512263200

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A long N-terminal-extended nested set of abundant and antigenic major histocompatibility complex class I natural ligands from HIV envelope protein.PMID 16407287Read ↗

The C-terminal extension landscape of naturally presented HLA-I ligandsSemantic proximity Read ↗

Toxoplasma gondii peptide ligands open the gate of the HLA class I binding grooveSemantic proximity Read ↗

Comprehensive Analysis of the Naturally Processed Peptide Repertoire: Differences between HLA-A and B in the Immunopeptidome.Semantic proximity Read ↗

ERAP1 enzyme-mediated trimming and structural analyses of MHC I–bound precursor peptides yield novel insights into antigen processing and presentationSemantic proximity Read ↗

HLA-B15 peptide ligands are preferentially anchored at their C termini.Semantic proximity Read ↗

The polymorphism at residue 156 determines the HLA-B*35 restricted peptide repertoire during HCMV infection.Semantic proximity Read ↗

Analysis of the structure of naturally processed peptides bound by class I and class II major histocompatibility complex molecules.Semantic proximity Read ↗

Identification of the Cryptic HLA-I ImmunopeptidomeSemantic proximity Read ↗

A subset of HLA-I peptides are not genomically templated: Evidence for cis- and trans-spliced peptide ligandsSemantic proximity Read ↗

MHC-I peptides get out of the groove and enable a novel mechanism of HIV-1 escape.Semantic proximity Read ↗

Baculoviral expressed HLA class I heavy chains used to screen a synthetic peptide library for allele-specific peptide binding motifs.Semantic proximity Read ↗

Variations in MHC class I antigen presentation and immunopeptidome selection pathwaysSemantic proximity Read ↗

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