期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 13, 期 5-6, 页码 582-591出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2009.09.011
关键词
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资金
- Ministry of Education, Culture, Sports, Science, and Technology [17GS0420]
- Human Frontier Science Program [RGP0031/2005-C]
- RIKEN Chemical Genomics Program
- Grants-in-Aid for Scientific Research [17GS0420] Funding Source: KAKEN
High-mannose-type oligosaccharides, which are cotranslationally introduced to nascent polypeptides during N-glycosylation, play critical roles in protein quality control. Involved in this process are a number of intracellular carbohydrate-recognizing proteins or carbohydrate-processing enzymes, including calnexin/calreticulin, malectin, glucosidase I (G-I) and II (G-II), UDP-glucose:glycoprotein glucosyltransferase (UGGT), cargo receptors (VIP36, ERGL, and ERGIC-53), ER 1,2-mannosidase I, ER degradation-enhancing alpha-mannosidase-like proteins (EDEMs) and ubiquitin ligase. Although all these proteins seem to recognize high-mannose glycans, their precise specificities are yet to be clarified. In order to conduct quantitative evaluation of the activity and specificity of these proteins, a comprehensive set of high-mannose-type glycans and their variously functionalized derivatives were synthesized and used to analyze enzymes involved in glycoprotein quality control system.
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