Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Vladimir S, Borodkin"'
Autor:
Karim Rafie, Olawale Raimi, Andrew T. Ferenbach, Vladimir S. Borodkin, Vaibhav Kapuria, Daan M. F. van Aalten
Publikováno v:
Open Biology, Vol 7, Iss 6 (2017)
O-linked N-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-Glc
Externí odkaz:
https://doaj.org/article/21a9f124fabb4a7cbe3a2df051cdbdb9
Author Correction: The active site of O-GlcNAc transferase imposes constraints on substrate sequence
Autor:
Shalini Pathak, Jana Alonso, Marianne Schimpl, Karim Rafie, David E. Blair, Vladimir S. Borodkin, Alexander W. Schüttelkopf, Osama Albarbarawi, Daan M. F. van Aalten
Publikováno v:
Nature Structural & Molecular Biology. 30:564-564
Autor:
Daan M. F. van Aalten, Ramon Hurtado-Guerrero, Michael A. J. Ferguson, Michael D. Urbaniak, Andrew T. Ferenbach, Vladimir S. Borodkin, Olawale G. Raimi
Publikováno v:
RSC Chemical Biology
'RSC Chemical Biology ', vol: 1, pages: 13-25 (2020)
'RSC Chemical Biology ', vol: 1, pages: 13-25 (2020)
UDP-N-acetylglucosamine pyrophosphorylase (UAP1) catalyses the last step in eukaryotic biosynthesis of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), converting UTP and GlcNAc-1P to the sugar nucleotide. Gene disruption studies have shown that
Autor:
Veronica M. Pravata, Villo Muha, Mehmet Gundogdu, Andrew T. Ferenbach, Poonam S. Kakade, Vasudha Vandadi, Ariane C. Wilmes, Vladimir S. Borodkin, Shelagh Joss, Marios P. Stavridis, Daan M. F. van Aalten
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Protein O-GlcNAcylation is a posttranslational modification essential for development. Recently, mutations in the O-GlcNAc transferase (OGT) substrate binding domain have been described that lead to intellectual disability, but the mecha
Autor:
Daan M. F. van Aalten, Nithya Selvan, Tonia Aristotelous, Vladimir S. Borodkin, Iva Navratilova, Andrew T. Ferenbach, Karim Rafie
Publikováno v:
ACS Chem Biol
The attachment of the sugar N-acetyl-D-glucosamine (GlcNAc) to specific serine and threonine residues on proteins is referred to as protein O-GlcNAcylation. O-GlcNAc transferase (OGT) is the enzyme responsible for carrying out the modification, while
Autor:
Andrii Gorelik, Sergio Galan Bartual, Vladimir S. Borodkin, Joby Varghese, Andrew T. Ferenbach, Daan M. F. van Aalten
Publikováno v:
Nature structural & molecular biology
Modification of specific Ser and Thr residues of nucleocytoplasmic proteins with O-GlcNAc, catalyzed by O-GlcNAc transferase (OGT), is an abundant post-translational event essential for proper animal development and dysregulated in various diseases.
Autor:
Lluís Raich, Jorge Castro-López, Vladimir S. Borodkin, Wenxia Fang, Ramon Hurtado-Guerrero, Daan M. F. van Aalten, Carme Rovira
Publikováno v:
Journal of the American Chemical Society. 138:3325-3332
The conversion of glycoside hydrolases (GHs) into transglycosylases (TGs), i.e., from enzymes that hydrolyze carbohydrates to enzymes that synthesize them, represents a promising solution for the large-scale synthesis of complex carbohydrates for bio
Autor:
Daan M. F. van Aalten, Vladimir S. Borodkin, Vincent Zoete, Ute F. Röhrig, Fabienne Lammers, Patrice Waridel, Winship Herr, Vaibhav Kapuria
Publikováno v:
The Journal of biological chemistry, vol. 293, no. 46, pp. 17754-17768
O-Linked GlcNAc transferase (OGT) possesses dual glycosyltransferase-protease activities. OGT thereby stably glycosylates serines and threonines of numerous proteins and, via a transient glutamate glycosylation, cleaves a single known substrate-the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68ed876b3531baab7bad629e97b6180b
https://serval.unil.ch/resource/serval:BIB_2C5B11AB86FD.P001/REF.pdf
https://serval.unil.ch/resource/serval:BIB_2C5B11AB86FD.P001/REF.pdf
Autor:
Vaibhav, Kapuria, Ute F, Röhrig, Patrice, Waridel, Fabienne, Lammers, Vladimir S, Borodkin, Daan M F, van Aalten, Vincent, Zoete, Winship, Herr
Publikováno v:
The Journal of Biological Chemistry
O-Linked GlcNAc transferase (OGT) possesses dual glycosyltransferase–protease activities. OGT thereby stably glycosylates serines and threonines of numerous proteins and, via a transient glutamate glycosylation, cleaves a single known substrate—t
Autor:
Daniel Mariappa, Jana Alonso, Nithya Selvan, Claire A. Shepherd, Iva Navratilova, Andrew T. Ferenbach, Daan M. F. van Aalten, Vladimir S. Borodkin
Publikováno v:
Biochemical Journal. 470:255-262
O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynam