Glycosyltransferases: structures, functions, and mechanisms.
By L. Lairson, Bernard Henrissat, G. Davies, S. Withers. Annual Review of Biochemistry, 2008
1,880 citations recorded by the source corpus.
Subfields: Molecular Biology, Organic Chemistry, Physiology
View Paper: https://www.semanticscholar.org/paper/42146f729aaced87c88c5c36502418de696ee2a5
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- Ronald J. Copeland
- R. Gerardy-Schahn
- H. Hildebrandt
- Gerald W. Hart
- T. Glumoff
- R. Schnaar
- Deborah Harrus
- Antti Hassinen
In Organic Chemistry
In Physiology
Citations in the corpus
- Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family. (2012, background): “As with other retaining GT-A glycosyltransferases, definitive identification of GalNAc-T residues responsible for catalytic activity has not been made and the mechanism of retaining glycosyltransferases remains unclear (Lairson et al. 2008).”
- Glycogen and its metabolism: some new developments and old themes. (2012, background): “More recently, there has been some speculation that this class of enzyme achieves retention of configuration by means of an SNi-type mechanism where the nucleotide diphosphate serves as the general base to activate the acceptor hydroxy group [85].”
- Sialic acids in the brain: gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration. (2014, background): “Unlike nucleic acids and proteins, which are template-based and linearly constructed, glycans are built by suites of biosynthetic enzymes termed glycosyltransferases (59, 253), each of which adds a saccharide building block to the growing glycan chain.”
- Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers (2018, background): “Although the size of the α and β parts vary, the overall structure is always held together by a continuous central twisted β-sheet called the Rossmann fold, which is flanked by α-helices on both sides [16].”
- Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized (2015, background): “The main impact of all these structures is that they have helped to resolve both donor and acceptor glycan binding modes as well as their catalytic mechanisms (for excellent reviews, see [117] [118] [119] [120] [121] ).”
- Glycomics hits the big time. (2010, positive): “Rather the glycan structures that end up on a polypeptide or lipid result from the concerted actions of highly-specific glycosyltransferases (Lairson et al., 2008), which in-turn are dependent upon the concentrations and localization of high-energy nucleotide sugar donors, such as UDP-N-acetylglucos”