Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase

Autor: Joël S. Bloch, Alan John, Runyu Mao, Somnath Mukherjee, Jérémy Boilevin, Rossitza N. Irobalieva, Tamis Darbre, Nichollas E. Scott, Jean-Louis Reymond, Anthony A. Kossiakoff, Ethan D. Goddard-Borger, Kaspar P. Locher

Publikováno v: Bloch, Joël S; John, Alan; Mao, Runyu; Mukherjee, Somnath; Boilevin, Jérémy; Irobalieva, Rossitza N; Darbre, Tamis; Scott, Nichollas E; Reymond, Jean-Louis; Kossiakoff, Anthony A; Goddard-Borger, Ethan D; Locher, Kaspar P (2023). Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase. Nature chemical biology, 19(5), pp. 575-584. Springer Nature 10.1038/s41589-022-01219-9
Nature Chemical Biology, 19 (5)

C-linked glycosylation is essential for the trafficking, folding and function of secretory and transmembrane proteins involved in cellular communication processes. The tryptophan C-mannosyltransferase (CMT) enzymes that install the modification attac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b3befc530922426b9dd0cdfdbc85a20

Characterization of the single-subunit oligosaccharyltransferase STT3A from Trypanosoma brucei using synthetic peptides and lipid-linked oligosaccharide analogs

Autor: Ana S. Ramírez, Bee Ha Gan, Kaspar P. Locher, Jérémy Boilevin, Tamis Darbre, Daniel Janser, Markus Aebi, Jean-Louis Reymond, Rasomoy Biswas

Publikováno v: Glycobiology
Glycobiology, 27 (6)
Ramírez, Ana S; Boilevin, Jérémy; Biswas, Rasomoy; Gan, Bee Ha; Janser, Daniel; Aebi, Markus; Darbre, Tamis; Reymond, Jean-Louis; Locher, Kaspar P (2017). Characterization of the single-subunit oligosaccharyltransferase STT3A from Trypanosoma brucei using synthetic peptides and lipid-linked oligosaccharide analogs. Glycobiology, 27(6), pp. 525-535. Oxford University Press 10.1093/glycob/cwx017

The initial transfer of a complex glycan in protein N-glycosylation is catalyzed by oligosaccharyltransferase (OST), which is generally a multisubunit membrane protein complex in the endoplasmic reticulum but a single-subunit enzyme (ssOST) in some p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9370a13b392269e784c0de07bf27257
http://doc.rero.ch/record/332115/files/GLYCOB_27_6_525.pdf

Structure and mechanism of the ER-based glucosyltransferase ALG6

Autor: Tamis Darbre, Markus Aebi, Jean-Louis Reymond, Kamil Nosol, Giorgio Pesciullesi, Rossitza N. Irobalieva, Kaspar P. Locher, Jérémy Boilevin, Anthony A. Kossiakoff, Joël S. Bloch

Publikováno v: Nature
Nature, 579

In eukaryotic protein N-glycosylation, a series of glycosyltransferases catalyse the biosynthesis of a dolichylpyrophosphate-linked oligosaccharide before its transfer onto acceptor proteins1. The final seven steps occur in the lumen of the endoplasm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fc7e8375c337bda406f32a9ecc4674f

Chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins

Autor: Ana S. Ramírez, Daniel Janser, Kaspar P. Locher, Jérémy Boilevin, Tamis Darbre, Bee Ha Gan, Markus Aebi, Chia-Wei Lin, Jean-Louis Reymond

Publikováno v: Glycobiology
Ramírez, Ana S; Boilevin, Jérémy; Lin, Chia-Wei; Gan, Bee Ha; Janser, Daniel; Aebi, Markus; Darbre, Tamis; Reymond, Jean-Louis; Locher, Kaspar P (2017). Chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins. Glycobiology, 27(8), pp. 726-733. Oxford University Press 10.1093/glycob/cwx045

The biosynthesis of eukaryotic lipid-linked oligosaccharides (LLOs) that act as donor substrates in eukaryotic protein N-glycosylation starts on the cytoplasmic side of the endoplasmic reticulum and includes the sequential addition of five mannose un

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e94fd1d1e199b58d80b6762a96c570d2
https://doi.org/10.1093/glycob/cwx045