Zobrazeno 1 - 10
of 232
pro vyhledávání: '"van Aalten, D.M.F."'
Autor:
Muha, V., Williamson, Ritchie, Hills, R., McNeilly, A.D., McWilliams, T.G., Alonso, J., Schimpl, M., Leney, A.C., Heck, A.J.R., Sutherland, C., Read, K.D., McCrimmon, R.J., Brooks, S.P., van Aalten, D.M.F.
Yes
O-GlcNAcylation is an abundant post-translational modification in the nervous system, linked to both neurodevelopmental and neurodegenerative disease. However, the mechanistic links between these phenotypes and site-specific O-GlcNAcylation
O-GlcNAcylation is an abundant post-translational modification in the nervous system, linked to both neurodevelopmental and neurodegenerative disease. However, the mechanistic links between these phenotypes and site-specific O-GlcNAcylation
Externí odkaz:
http://hdl.handle.net/10454/17525
Autor:
Selvan, N., Williamson, Ritchie, Mariappa, D., Campbell, D.G., Gourlay, R., Ferenbach, A.T., Aristotelous, T., Hopkins-Navratilova, I., Trost, M., van Aalten, D.M.F.
Yes
Protein O-GlcNAcylation is a reversible post-translational modification of serines/threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA). Genetic approach
Protein O-GlcNAcylation is a reversible post-translational modification of serines/threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA). Genetic approach
Externí odkaz:
http://hdl.handle.net/10454/12133
Akademický článek
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Autor:
Fang, W., Sanz, A.B., Bartual, Sergio G., Wang, B., Ferenbach, A.T., Farkaš, V., Hurtado-Guerrero, R., Arroyo, J., van Aalten, D.M.F.
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
E-Prints Complutense. Archivo Institucional de la UCM
instname
'Nature Communications ', vol: 10, pages: 1669-1-1669-10 (2019)
Zaguán. Repositorio Digital de la Universidad de Zaragoza
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
E-Prints Complutense. Archivo Institucional de la UCM
instname
'Nature Communications ', vol: 10, pages: 1669-1-1669-10 (2019)
Zaguán. Repositorio Digital de la Universidad de Zaragoza
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
Nature Communications
Digital.CSIC. Repositorio Institucional del CSIC
10 pags., 3 figs., 2 tabs. -- Open Access funded by Creative Commons Atribution Licence 4.0
Fungal cell wall synthesis is achieved by a balance of glycosyltransferase, hydrolase and transglycosylase activities. Transglycosylases strengthen the c
Fungal cell wall synthesis is achieved by a balance of glycosyltransferase, hydrolase and transglycosylase activities. Transglycosylases strengthen the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::f1afb491c8c6fec2282b8642f6685ab5
http://link.springer.com/article/10.1038/s41467-019-09674-0
http://link.springer.com/article/10.1038/s41467-019-09674-0
Publikováno v:
Biochemical Journal
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
'Biochemical Journal ', vol: 475, pages: 2547-2557 (2018)
Digital.CSIC. Repositorio Institucional del CSIC
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
'Biochemical Journal ', vol: 475, pages: 2547-2557 (2018)
Digital.CSIC. Repositorio Institucional del CSIC
11 pags, 4 figs, 2 tabs . -- Supplementary data is available at the Publisher's web page
N-acetylphosphoglucosamine mutase (AGM1) is a key component of the hexosamine biosynthetic pathway that produces UDP-GlcNAc, an essential precursor for a wi
N-acetylphosphoglucosamine mutase (AGM1) is a key component of the hexosamine biosynthetic pathway that produces UDP-GlcNAc, an essential precursor for a wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::4e0c5b1e8ae7c72536ad1a3f283b5c17
http://europepmc.org/articles/PMC6096347
http://europepmc.org/articles/PMC6096347
Publikováno v:
'Bioconjugate Chemistry ', vol: 29, pages: 1834-1840 (2018)
O-GlcNAc transferase (OGT) is an essential glycosyltransferase that installs the O-GlcNAc post-translational modification on the nucleocytoplasmic proteome. We report the development of Blinked UDP-peptide conjugates as potent bisubstrate OGT inhibit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=illesrfpubli::4db57f8b823a3f9b07ecee176069b006
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:51847
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:51847
Akademický článek
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Akademický článek
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Publikováno v:
Genes and Development
In complex with the cosubstrate UDP N acetylglucosamine (UDP GlcNAc) O linked GlcNAc transferase (OGT) catalyzes Ser/Thr O GlcNAcylation of many cellular proteins and proteolysis of the transcriptional coregulator HCF 1. Such a dual glycosyltransfera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=snsf_p3_pubs::27da8f2807bfe812d4151c72d6f1fcae
http://genesdev.cshlp.org/content/30/8/960.long
http://genesdev.cshlp.org/content/30/8/960.long
Autor:
Tabudravu, J.N, Eijsink, V.G.H, Gooday, G.W, Jaspars, M, Komander, D, Legg, M, Synstad, B, van Aalten, D.M.F
Publikováno v:
In Bioorganic & Medicinal Chemistry April 2002 10(4):1123-1128