Naturally processed peptides from rheumatoid arthritis associated and non-associated HLA-DR alleles.

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

Back to search

Article

Naturally processed peptides from rheumatoid arthritis associated and non-associated HLA-DR alleles.

Journal of immunology (Baltimore, Md. : 1950) - 15 Dec 1995

Kirschmann D A, Duffin K L, Smith C E, Welply J K, Howard S C, Schwartz B D, Woulfe S L

Abstract excerpt

Naturally processed peptides from immunoaffinity-purified HLA-DRB1*0401, -DRB1*0404 (rheumatoid arthritis (RA)-associated), and -DRB1*0402 (non-RA-associated) molecules were analyzed by capillary liquid chromatography and mass spectrometry. The molecular weights observed for more than 60 eluted p...

Topics

Alleles
Amino Acid Sequence
Antigen Presentation
Arthritis, Rheumatoid
B-Lymphocytes
Cell Line, Transformed
HLA-DR Antigens
HLA-DRB1 Chains
Humans
Mass Spectrometry
Molecular Sequence Data

Source

Open in PubMed

Identifiers

PMID: 7499850

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7499850-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics