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

Disparate folding and stability of the ankylosing spondylitis-associated HLA-B1403 and B2705 proteins.

Arthritis and rheumatism - 1 Dec 2008

Merino Elena, Galocha Begoña, Vázquez Miriam N, López de Castro José A

Abstract excerpt

OBJECTIVE: To investigate the folding, assembly, maturation, and stability of HLA-B*1402 and B*1403, which differ by 1 amino acid change and are differentially associated with ankylosing spondylitis (AS), and to compare these features with those of B*2705. METHODS: Stable transfectants expressing...

Read the complete abstract on PubMed

Topics

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

Share to Antigens, Surface
Share to Dimerization
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HLA-B Antigens

Share to HLA-B27 Antigen

Share to Hot Temperature

Share to Immunoprecipitation

Share to Spondylitis, Ankylosing

Source

Identifiers

PMID: 19035480
DOI: 10.1002/art.24045

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19035480-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disparate folding and stability of the ankylosing spondylitis-associated HLA-B*1403 and B*2705 proteins.PMID 19035480Read ↗

HLA-B*2704, an allotype associated with ankylosing spondylitis, is critically dependent on transporter associated with antigen processing and relatively independent of tapasin and immunoproteasome for maturation, surface expression, and T cell recognition: relationship to B*2705 and B*2706.Semantic proximity Read ↗

Differences in Cellular Clearing Mechanisms of Aggregates of Two Subtypes of HLA-B27.Semantic proximity Read ↗

HLA-B27 misfolding and ankylosing spondylitis.Semantic proximity Read ↗

Peptide handling by HLA-B27 subtypes influences their biological behavior, association with ankylosing spondylitis and susceptibility to endoplasmic reticulum aminopeptidase 1 (ERAP1).Semantic proximity Read ↗

HLA-B27Semantic proximity Read ↗

Distinct mechanisms survey the structural integrity of HLA-B*27:05 intracellularly and at the surface.Semantic proximity Read ↗

Dominant role of the ERAP1 polymorphism R528K in shaping the HLA-B27 Peptidome through differential processing determined by multiple peptide residues.Semantic proximity Read ↗

Assembly and intracellular trafficking of HLA-B*3501 and HLA-B*3503.Semantic proximity Read ↗

HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading.Semantic proximity Read ↗

Separate effects of the ankylosing spondylitis associated ERAP1 and ERAP2 aminopeptidases determine the influence of their combined phenotype on the HLA-B*27 peptidome.Semantic proximity Read ↗

The immunobiology of HLA-B27: variations on a theme.Semantic proximity Read ↗

Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27.Semantic proximity Read ↗

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