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  1. C. 医薬保健学域; 医学類・薬学類・医薬科学類・保健学類
  2. c 10. 学術雑誌掲載論文(医・保健)
  3. 2.査読済論文(薬)

Evaluation of the reactivity and receptor competition of HLA-G isoforms toward available antibodies: Implications of structural characteristics of HLA-G isoforms

https://doi.org/10.24517/00067079
https://doi.org/10.24517/00067079
82ec6a68-e0b1-4b2f-9373-d1bf0e1e6255
名前 / ファイル ライセンス アクション
PH-PR-FURUKAWA-A-20-05947.pdf PH-PR-FURUKAWA-A-20-05947.pdf (1.8 MB)
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Item type 学術雑誌論文 / Journal Article(1)
公開日 2022-09-12
タイトル
タイトル Evaluation of the reactivity and receptor competition of HLA-G isoforms toward available antibodies: Implications of structural characteristics of HLA-G isoforms
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
ID登録
ID登録 10.24517/00067079
ID登録タイプ JaLC
著者 Furukawa, Atsushi

× Furukawa, Atsushi

WEKO 106955
e-Rad 30727699

Furukawa, Atsushi

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Meguro, Manami

× Meguro, Manami

WEKO 106970

Meguro, Manami

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Yamazaki, Rika

× Yamazaki, Rika

WEKO 106971

Yamazaki, Rika

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Watanabe, Hiroshi

× Watanabe, Hiroshi

WEKO 17798

Watanabe, Hiroshi

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Takahashi, Ami

× Takahashi, Ami

WEKO 106973

Takahashi, Ami

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Kuroki, Kimiko

× Kuroki, Kimiko

WEKO 106948

Kuroki, Kimiko

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Maenaka, Katsumi

× Maenaka, Katsumi

WEKO 106954

Maenaka, Katsumi

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著者別表示 古川, 敦

× 古川, 敦

古川, 敦

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提供者所属
内容記述タイプ Other
内容記述 金沢大学医薬保健研究域薬学系
書誌情報 International Journal of Molecular Sciences

巻 20, 号 23, p. 5947, 発行日 2019-12-01
ISSN
収録物識別子タイプ ISSN
収録物識別子 1661-6596
ISSN
収録物識別子タイプ ISSN
収録物識別子 1422-0067
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 10.3390/ijms20235947
出版者
出版者 MDPI AG
抄録
内容記述タイプ Abstract
内容記述 The human leucocyte antigen (HLA)-G, which consists of seven splice variants, is a tolerogenic immune checkpoint molecule. It plays an important role in the protection of the fetus from the maternal immune response by binding to inhibitory receptors, including leukocyte Ig-like receptors (LILRs). Recent studies have also revealed that HLA-G is involved in the progression of cancer cells and the protection from autoimmune diseases. In contrast to its well characterized isoform, HLA-G1, the binding activities of other major HLA-G isoforms, such as HLA-G2, toward available anti-HLA-G antibodies are only partially understood. Here, we investigate the binding specificities of anti-HLA-G antibodies by using surface plasmon resonance. MEM-G9 and G233 showed strong affinities to HLA-G1, with a nM range for their dissociation constants, but did not show affinities to HLA-G2. The disulfide-linker HLA-G1 dimer further exhibited significant avidity effects. On the other hand, 4H84 and MEM-G1, which can be used for the Western blotting of HLA-G isoforms, can bind to native HLA-G2, while MEM-G9 and G233 cannot. These results reveal that HLA-G2 has a partially intrinsically disordered structure. Furthermore, MEM-G1, but not 4H84, competes with the LILRB2 binding of HLA-G2. These results provide novel insight into the functional characterization of HLA-G isoforms and their detection systems. © 2019 by the authors. Licensee MDPI, Basel, Switzerland.
権利
権利情報 Copyright © This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連URI
識別子タイプ URI
関連識別子 https://www.mdpi.com/1422-0067/20/23/5947
関連名称 https://www.mdpi.com/1422-0067/20/23/5947
関連URI
識別子タイプ URI
関連識別子 https://www.mdpi.com/journal/ijms
関連名称 https://www.mdpi.com/journal/ijms
関連URI
識別子タイプ URI
関連識別子 http://www.mdpi.com/
関連名称 http://www.mdpi.com/
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