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

Goodpasture Antigen-binding Protein, the Kinase That Phosphorylates the Goodpasture Antigen, Is an Alternatively Spliced Variant Implicated in Autoimmune Pathogenesis

1 Dec 2000

Abstract excerpt

The non-collagenous C-terminal domain of the alpha(3) chain of collagen IV is the autoantigen in Goodpasture disease, an autoimmune disorder described only in humans. Specific N-terminal phosphorylation is a biological feature unique to the human domain when compared with other homologous domains lacking immunopathogenic potential. We have recently cloned from a HeLa-derived cDNA library a novel serine/threonine...

Read the complete abstract on PubMed

Topics

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

Share to Diabetes and associated disorders
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: 11007769
DOI: 10.1074/jbc.m002769200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Goodpasture Antigen-binding Protein, the Kinase That Phosphorylates the Goodpasture Antigen, Is an Alternatively Spliced Variant Implicated in Autoimmune PathogenesisPMID 11007769Read ↗

Goodpasture antigen-binding protein and its spliced variant, ceramide transfer protein, have different functions in the modulation of apoptosis during zebrafish development.Semantic proximity Read ↗

Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains.Semantic proximity Read ↗

Nonsense mutations in AAGAB cause punctate palmoplantar keratoderma type Buschke-Fischer-Brauer.Semantic proximity Read ↗

Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon.Semantic proximity Read ↗

Identification of novel candidate genes in the diffuse panbronchiolitis critical region of the class I human MHC.Semantic proximity Read ↗

PKA Cβ: a forgotten catalytic subunit of cAMP-dependent protein kinase opens new windows for PKA signaling and disease pathologies.Semantic proximity Read ↗

The Goodpasture AutoantigenSemantic proximity Read ↗

Molecular cloning of the human Goodpasture antigen demonstrates it to be the alpha 3 chain of type IV collagen.Semantic proximity Read ↗

Temperature-dependent autoactivation associated with clinical variability of PDGFRB Asn666 substitutions.Semantic proximity Read ↗

Goodpasture disease. Characterization of a single conformational epitope as the target of pathogenic autoantibodies.Semantic proximity Read ↗

SERPINA2 is a novel gene with a divergent function from SERPINA1.Semantic proximity Read ↗

Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis.Semantic proximity Read ↗

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