Regulation of Glycosylation by Golgi Units

• Goto Satoshi

  Mitsubishi-Kagaku Institute of Life Sciences 11 Minamiooya

Bibliographic Information

Other Title

• ゴルジ体ユニットによる糖修飾の制御
• ゴルジタイ ユニット ニ ヨル トウ シュウショク ノ セイギョ ガン エイブン

Abstract

Most secretory and transmembrane proteins are posttranslationally modified with various glycans. The structures of glycans attached to the proteins depend on proteins, cells, tissues, ages, species and individuals. However, the mechanism of regulation to generate such diverse glycans in a cell has not been revealed. In this review, we would like to discuss our finding, “Golgi units” that would regulate the variety of glycosylation.

Journal

• Trends in Glycoscience and Glycotechnology

  Trends in Glycoscience and Glycotechnology 18 (104), 347-351, 2006

  FCCA(Forum: Carbohydrates Coming of Age)

Keywords

• nucleotide-sugar transporter
• Drosophila melanogaster
• fringe connection
• Notch
• proteoglycan

Details

• CRID: 1390282679345660800
• NII Article ID: 10018515970
• NII Book ID: AA10995236
• DOI: 10.4052/tigg.18.347
• ISSN: 18832113
• ISSN: 09157352
• NDL BIB ID: 8682753
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8682753
• Web Site: https://search.jamas.or.jp/link/ui/2007176336
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed