Chemical Approaches to Elucidate Enzymatic Profiles of UDP-Glucose: Glycoprotein Glucosyltransferase
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- Hachisu Masakazu
- ERATO Ito Glycotrilogy Project, Japan Science and Technology Agency (JST)
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- Ito Yukishige
- ERATO Ito Glycotrilogy Project, Japan Science and Technology Agency (JST) RIKEN, Synthetic Cellular Chemistry Laboratory
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In the endoplasmic reticulum (ER), uridine 5′-diphosphate-glucose: glycoprotein glucosyltransferase 1 (UGGT1) recognizes misfolded glycoproteins and transfers a glucose residue to the specific non-reducing end of high-mannose-type glycans. However, precise molecular mechanism by which UGGT1 senses the folding has not been understood clearly. To address this issue, various model substrates for UGGT1 have been prepared using biological approaches. Recently, we introduced chemical approaches using synthetic glycan probes that were designed for studying N-glycan processing in the ER and Golgi apparatus. Our approach can outfit the homogeneous and functionalized glycan probes. In this review, recent results on functional analysis of UGGT1 are summarized.
収録刊行物
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- CHEMICAL & PHARMACEUTICAL BULLETIN
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CHEMICAL & PHARMACEUTICAL BULLETIN 64 (7), 687-690, 2016
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390001204178782208
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- NII論文ID
- 130005160027
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- NII書誌ID
- AA00602100
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- ISSN
- 13475223
- 00092363
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- NDL書誌ID
- 027451372
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- PubMed
- 27373624
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可