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

Hydrophobic interactions dominate the recognition of a KRAS G12V neoantigen

21 Aug 2023

Abstract excerpt

Abstract Specificity remains a major challenge to current therapeutic strategies for cancer. Mutation associated neoantigens (MANAs) are products of genetic alterations, making them highly specific therapeutic targets. MANAs are HLA-presented (pHLA) peptides derived from intracellular mutant proteins that are otherwise inaccessible to antibody-based therapeutics. Here, we describe the cryo-EM structure of an...

Read the complete abstract on PubMed

Topics

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

Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research
Share to T-cell and B-cell Immunology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 37604828
DOI: 10.1038/s41467-023-40821-w

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

Hydrophobic interactions dominate the recognition of a KRAS G12V neoantigenPMID 37604828Read ↗

Identification and structural characterization of a mutant KRAS-G12V specific TCR restricted by HLA-A3.Semantic proximity Read ↗

Identification and Structural Characterization of a mutant KRAS-G12V specific TCR restricted by HLA-A3Semantic proximity Read ↗

Overcoming immune evasion from post-translational modification of a mutant KRAS epitope to achieve TCR-T cell-mediated antitumor activitySemantic proximity Read ↗

Identification and affinity enhancement of T-cell receptor targeting a KRASG12V cancer neoantigen.Semantic proximity Read ↗

Natural TCRs targeting KRASG12V display fine specificity and sensitivity to human solid tumorsSemantic proximity Read ↗

An integrated in silico-in vitro workflow for discovering high-affinity, selective antibodies to the KRAS(G12D)-MHC I complexSemantic proximity Read ↗

Molecular mechanism of phosphopeptide neoantigen immunogenicitySemantic proximity Read ↗

Dual-degenerate TCRs target multiple KRAS hotspot and HLA-A3 family combinationsSemantic proximity Read ↗

Functional avidity enhancement of a T-cell receptor targeting the KRASG12D cancer neoantigen.Semantic proximity Read ↗

Role of in silico structural modeling in predicting immunogenic neoepitopes for cancer vaccine development.Semantic proximity Read ↗

KRAS G12V neoantigen specific T cell receptor for adoptive T cell therapy against tumorsSemantic proximity Read ↗

Structural principles of peptide-centric chimeric antigen receptor recognition guide therapeutic expansionSemantic proximity Read ↗

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