Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP-Reference-Cited by-同舟云学术

Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP

Published:2018-02-13 Issue:4 Volume:14 Page:368-374
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Sengoku Toru^ORCID,Suzuki Takehiro,Dohmae Naoshi,Watanabe Chiduru^ORCID,Honma Teruki^ORCID,Hikida Yasushi^ORCID,Yamaguchi Yoshiki^ORCID,Takahashi Hideyuki,Yokoyama Shigeyuki^ORCID,Yanagisawa Tatsuo^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/s41589-018-0002-y.pdf

Reference45 articles.

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2. Coutinho, P. M., Deleury, E., Davies, G. J. & Henrissat, B. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328, 307–317 (2003).

3. Liu, J. & Mushegian, A. Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci. 12, 1418–1431 (2003).

4. Cantarel, B. L. et al. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 37, D233–D238 (2009).

5. Hurtado-Guerrero, R. & Davies, G. J. Recent structural and mechanistic insights into post-translational enzymatic glycosylation. Curr. Opin. Chem. Biol. 16, 479–487 (2012).

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