Lee P.YJIA-WEI HSU et al.2021-07-262021-07-262018916749https://www.scopus.com/inward/record.uri?eid=2-s2.0-85050317097&doi=10.1016%2fj.jaci.2018.05.038&partnerID=40&md5=6d04f47633713d048fca42943d1d57b7https://scholars.lib.ntu.edu.tw/handle/123456789/573362adenosine deaminase; adenosine deaminase 2; complementary DNA; glutamine; RNA; unclassified drug; ADA2 protein, human; adenosine deaminase; signal peptide; 3' untranslated region; adenosine deaminase deficiency; allele; Article; brain hemorrhage; case report; child; clinical article; congenital disorder of glycosylation; enzyme activity; exon; female; gene deletion; genetic analysis; genetic variability; glycosylation; heterozygosity; heterozygote; human; inflammation; livedo reticularis; maternal plasma; missense mutation; multiplex ligation dependent probe amplification; papule; preschool child; priority journal; protein expression; protein folding; protein function; protein processing; protein transport; RNA stability; Sanger sequencing; sequence alignment; site directed mutagenesis; stop codon; agammaglobulinemia; blood; genetics; mutation; severe combined immunodeficiency; Adenosine Deaminase; Agammaglobulinemia; Child, Preschool; Female; Glycosylation; Humans; Intercellular Signaling Peptides and Proteins; Mutation; Severe Combined Immunodeficiency[SDGs]SDG3Disrupted N-linked glycosylation as a disease mechanism in deficiency of ADA2journal article10.1016/j.jaci.2018.05.038299361042-s2.0-85050317097