Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)-Reference-Cited by-同舟云学术

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Published:2016-08-09 Issue:8 Volume:17 Page:1286
ISSN:1422-0067
Container-title:International Journal of Molecular Sciences
language:en
Short-container-title:IJMS

Author:

Teppa Roxana,Petit Daniel,Plechakova Olga,Cogez Virginie,Harduin-Lepers Anne

Funder

Agence Nationale de la Recherche

Centre National de la Recherche Scientifique

Ligue Contre le Cancer

Publisher

MDPI AG

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis

Link

http://www.mdpi.com/1422-0067/17/8/1286/pdf

Reference87 articles.

1. Sialome analysis of the cephalochordate Branchiostoma belcheri, a key organism for vertebrate evolution

2. Sialic acids: fascinating sugars in higher animals and man

3. Chemistry, biochemistry and biology of sialic acids;Schauer,1997

4. Diversity in the sialic acids

5. The evolution of galactose α2,3-sialyltransferase: Cionaintestinalis ST3GAL I/II and Takifugu rubripes ST3GAL II sialylate Galβ1,3GalNAc structures on glycoproteins but not glycolipids

Cited by 28 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Sialylation in the gut: From mucosal protection to disease pathogenesis;Carbohydrate Polymers;2024-11

2. LacdiNAc synthase B4GALNT3 has a unique PA14 domain and suppresses N-glycan capping;Journal of Biological Chemistry;2024-07

3. A brief history of galectin evolution;Frontiers in Immunology;2023-06-29

4. The role of glycoconjugates as receptors for insecticidal proteins;FEMS Microbiology Reviews;2023-06-02

5. The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases;Glycoconjugate Journal;2023-05-29