2009
DOI: 10.1016/j.humimm.2009.07.015
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Human leukocyte antigen-G polymorphism in relation to expression, function, and disease

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Cited by 98 publications
(93 citation statements)
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“…The capability of HLA-G1 and HLA-G5 to form multimers has been demonstrated both in vivo and in vitro (24,34 ). HLA-G has a low polymorphism rate, and most of the alleles do not alter the amino acid sequence, do not change the secondary structure of the heavy chains, and do not produce high molecular weight isoforms (35 ). However, those polymorphisms that alter the epitopes recognized by the antibodies could affect quantification based on the binding to these antibodies, but not the size of the band detected in the Western blot.…”
Section: Soluble Hla-g-like Molecules In Exudatesmentioning
confidence: 99%
“…The capability of HLA-G1 and HLA-G5 to form multimers has been demonstrated both in vivo and in vitro (24,34 ). HLA-G has a low polymorphism rate, and most of the alleles do not alter the amino acid sequence, do not change the secondary structure of the heavy chains, and do not produce high molecular weight isoforms (35 ). However, those polymorphisms that alter the epitopes recognized by the antibodies could affect quantification based on the binding to these antibodies, but not the size of the band detected in the Western blot.…”
Section: Soluble Hla-g-like Molecules In Exudatesmentioning
confidence: 99%
“…However, the mRNA stability conferred by the 14-bp insertion may exert a negative effect on HLA-G expression, and the 14-bp insertion is associated with lower soluble HLA-G levels. 15 The 14-bp insertion also is associated with the generation of a more stable mRNA, but these transcripts have minimal effects on overall HLA-G expression. Conversely, decreased protein expression is associated with the insertion allele.…”
Section: Discussionmentioning
confidence: 99%
“…The other null allele -HLA-G*01:13N -contains a point mutation (C to T) at codon 54 in exon 2 (a1 domain) that causes a premature stop codon (TAG) leading to no HLA-G isoform production. The majority of polymorphisms found in the coding regions were seen in codons 31, 35, 57 and 69 of exon 2 and in codons 93, 107 and 110 of exon 3 [63]. Frequencies of the different HLA-G alleles vary between ethnic populations.…”
Section: Functional Impact Of Hla-g Polymorphismmentioning
confidence: 99%