dgn-np:NP954935.RA4gvA7emjCgeK6BHNVWlAGmJbstou4e-tg_kHr7WpwyE130_provenance {
  dgn-np:NP954935.RA4gvA7emjCgeK6BHNVWlAGmJbstou4e-tg_kHr7WpwyE130_assertion dcterms:description "[Collectively, these results indicate not only that the intra-subunit disulfide bonds are crucial for TNSALP to properly fold and assemble into the dimeric enzyme, but also that the development of HPP associated with TNSALP (C201Y) or TNSALP (C489S) is attributed to decreased cell surface appearance of the functional enzyme.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine."@en ;
    wi:evidence dgn-void:source_evidence_literature ;
    sio:SIO_000772 miriam-pubmed:22266140 ;
    prov:wasDerivedFrom dgn-void:befree-2016 ;
    prov:wasGeneratedBy eco:ECO_0000203 .
  dgn-void:befree-2016 pav:importedOn "2016-02-19"^^xsd:date .
  dgn-void:source_evidence_literature a eco:ECO_0000212 ;
    rdfs:comment "Gene-disease associations inferred from text-mining the literature."@en ;
    rdfs:label "DisGeNET evidence - LITERATURE"@en .
}