Zobrazeno 1 - 10
of 13
pro vyhledávání: '"MESH: Glycosyltransferases"'
Publikováno v:
Scientific Reports
Scientific Reports, Nature Publishing Group, 2020, 10 (1), pp.15137. ⟨10.1038/s41598-020-71746-9⟩
Scientific Reports, Vol 10, Iss 1, Pp 1-10 (2020)
Scientific Reports, Nature Publishing Group, 2020, 10 (1), pp.15137. ⟨10.1038/s41598-020-71746-9⟩
Scientific Reports, Vol 10, Iss 1, Pp 1-10 (2020)
Glycosylation is a key modification that contributes to determine bioactivity and bioavailability of plant natural products, including that of terpenoids and steviol glycosides (SVglys). It is mediated by uridine-diphosphate glycosyltransferases (UGT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::886e9ca646dc72fd0c8c449f8fb16caa
https://pubmed.ncbi.nlm.nih.gov/32934264
https://pubmed.ncbi.nlm.nih.gov/32934264
Serum resistance and phase variation of a nasopharyngeal non-typeable Haemophilus influenzae isolate
Autor:
Sabine Lichtenegger, Philippe Glaser, Isabelle Bina, Sanel Durakovic, Stefan Schild, Joachim Reidl, Sarah Tutz
Publikováno v:
International Journal of Medical Microbiology
International Journal of Medical Microbiology, Elsevier, 2017, 307 (2), pp.139-146. ⟨10.1016/j.ijmm.2017.01.005⟩
International Journal of Medical Microbiology, 2017, 307 (2), pp.139-146. ⟨10.1016/j.ijmm.2017.01.005⟩
International Journal of Medical Microbiology, Elsevier, 2017, 307 (2), pp.139-146. ⟨10.1016/j.ijmm.2017.01.005⟩
International Journal of Medical Microbiology, 2017, 307 (2), pp.139-146. ⟨10.1016/j.ijmm.2017.01.005⟩
International audience; Haemophilus influenzae harbours a complex array of factors to resist human complement attack. As non-typeable H. influenzae (NTHi) strains do not possess a capsule, their serum resistance mainly depends on other mechanisms inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04abf3869ed7d75d52931af4b4969464
https://doi.org/10.1016/j.ijmm.2017.01.005
https://doi.org/10.1016/j.ijmm.2017.01.005
Autor:
Colette Larré, A. Partier, Dominique Tessier, Caroline Pont, Hélène Rogniaux, J. Marion, Brigitte Bouchet, Mathilde Francin-Allami, Fabienne Guillon, Anne-Laure Chateigner-Boutin, M. Suliman, Jérôme Salse
Publikováno v:
Journal of Proteomics
Journal of Proteomics, Elsevier, 2013, 78, pp.508-521. ⟨10.1016/j.jprot.2012.10.021⟩
Journal of Proteomics, 2013, 78, pp.508-521. ⟨10.1016/j.jprot.2012.10.021⟩
Journal of Proteomics, Elsevier, 2013, 78, pp.508-21. ⟨10.1016/j.jprot.2012.10.021⟩
Journal of Proteomics, Elsevier, 2013, 78, pp.508-521. ⟨10.1016/j.jprot.2012.10.021⟩
Journal of Proteomics, 2013, 78, pp.508-521. ⟨10.1016/j.jprot.2012.10.021⟩
Journal of Proteomics, Elsevier, 2013, 78, pp.508-21. ⟨10.1016/j.jprot.2012.10.021⟩
International audience; Plant cell walls are complex structures critical for plant fitness and valuable for human nutrition as dietary fiber and for industrial uses such as biofuel production. The cell wall polysaccharides in wheat endosperm consist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69e6a63a6b970c83689ef03950ce6988
https://doi.org/10.1016/j.jprot.2012.10.021
https://doi.org/10.1016/j.jprot.2012.10.021
Autor:
Marco Bellinzoni, Alexandre Chenal, David Albesa-Jové, Natalia Comino, David Giganti, Mariano A. Martinez, Marcelo E. Guerin, Saioa Urresti, Ane Rodrigo-Unzueta, Nathalie Barilone, Pedro M. Alzari
Publikováno v:
Nature Chemical Biology
Nature Chemical Biology, Nature Publishing Group, 2014, 11 (1), pp.16-18. ⟨10.1038/nchembio.1694⟩
Nature Chemical Biology, 2014, 11 (1), pp.16-18. ⟨10.1038/nchembio.1694⟩
Nature Chemical Biology, Nature Publishing Group, 2014, 11 (1), pp.16-18. ⟨10.1038/nchembio.1694⟩
Nature Chemical Biology, 2014, 11 (1), pp.16-18. ⟨10.1038/nchembio.1694⟩
International audience; Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a064705d1cfe74b90c2166187c6be04
https://hal-pasteur.archives-ouvertes.fr/pasteur-01408804
https://hal-pasteur.archives-ouvertes.fr/pasteur-01408804
Publikováno v:
Glycobiology
Glycobiology, Oxford University Press (OUP), 2014, 24 (2), pp.108-124. ⟨10.1093/glycob/cwt101⟩
Glycobiology, 2014, 24 (2), pp.108-124. ⟨10.1093/glycob/cwt101⟩
Glycobiology; Vol 24
Glycobiology, Oxford University Press (OUP), 2014, 24 (2), pp.108-124. ⟨10.1093/glycob/cwt101⟩
Glycobiology, 2014, 24 (2), pp.108-124. ⟨10.1093/glycob/cwt101⟩
Glycobiology; Vol 24
International audience; Membrane-associated GT-B glycosyltransferases (GTs) comprise a large family of enzymes that catalyze the transfer of a sugar moiety from nucleotide-sugar donors to a wide range of membrane-associated acceptor substrates, mostl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19131027a9fad4f23562adfd2f1d5313
https://hal-pasteur.archives-ouvertes.fr/pasteur-03096123
https://hal-pasteur.archives-ouvertes.fr/pasteur-03096123
Autor:
Kenneth D. Irvine, Muriel Grammont
Publikováno v:
Europe PubMed Central
Development (Cambridge, England)
Development (Cambridge, England), Company of Biologists, 2001, 128 (12), pp.2243-53
Development (Cambridge, England)
Development (Cambridge, England), Company of Biologists, 2001, 128 (12), pp.2243-53
International audience; fringe encodes a glycosyltransferase that modulates the ability of the Notch receptor to be activated by its ligands. We describe studies of fringe function during early stages of Drosophila oogenesis. Animals mutant for hypom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83b362d0c0e197a4356d8c488ee00a60
https://doi.org/10.1242/dev.128.12.2243
https://doi.org/10.1242/dev.128.12.2243
Autor:
Annick Ozil, Marie-Christine Slomianny, Sylvie Juliant, Martine Cerutti, Marie-Luce Violet, Pierre Cérutti, Anne Harduin-Lepers, Marylène Lévêque, Sylvie Choblet
Publikováno v:
Methods in Molecular Biology
Methods in Molecular Biology, 988, pp.59-77, 2012
Methods in Molecular Biology ISBN: 9781627033268
Methods in Molecular Biology, 988, pp.59-77, 2012
Methods in Molecular Biology ISBN: 9781627033268
International audience; Nowadays, recombinant proteins are used with great success for the treatment of a variety of medical conditions, such as cancer, autoimmune, and infectious diseases. Several expression systems have been developed to produce hu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55004b064babe9d507f35766bd05f140
https://hal.science/hal-01224141
https://hal.science/hal-01224141
Autor:
Christian Slomianny, Jorick Vanbeselaere, Christophe Biot, Yann Guérardel, Anne Harduin-Lepers, Kay-Hooi Khoo, Emeline Fabre, Lan-Yi Chang, Nao Yamakawa
Publikováno v:
Journal of Proteome Research
Journal of Proteome Research, American Chemical Society, 2012, 11 (4), pp.2164-2177. ⟨10.1021/pr200948j⟩
Journal of Proteome Research, American Chemical Society, 2012, 11 (4), pp.2164-77
Journal of Proteome Research, 2012, 11 (4), pp.2164-2177. ⟨10.1021/pr200948j⟩
Journal of Proteome Research, 2012, 11 (4), pp.2164-77
Journal of Proteome Research, American Chemical Society, 2012, 11 (4), pp.2164-2177. ⟨10.1021/pr200948j⟩
Journal of Proteome Research, American Chemical Society, 2012, 11 (4), pp.2164-77
Journal of Proteome Research, 2012, 11 (4), pp.2164-2177. ⟨10.1021/pr200948j⟩
Journal of Proteome Research, 2012, 11 (4), pp.2164-77
International audience; The emergence of zebrafish as a model organism for human diseases was accompanied by the development of cellular model systems that extended the possibilities for in vitro manipulation and in vivo studies after cell implantati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69321f77d3d234fc41041acd14b027d7
https://hal.archives-ouvertes.fr/hal-02350669
https://hal.archives-ouvertes.fr/hal-02350669
Autor:
Delphi Chatterjee, Stéphanie Guadagnini, Jérôme Nigou, Patrick J. Brennan, Henrieta Škovierová, Gerald Larrouy-Maumus, Germain Puzo, Marie-Christine Prévost, Martina Belanova, Devinder Kaur, Nathalie Barilone, Mary Jackson, Brigitte Gicquel, Martine Gilleron, Jana Korduláková, Jian Zhang
Publikováno v:
Glycobiology
Glycobiology, 2009, 19 (11), pp.1235-1247. ⟨10.1093/glycob/cwp116⟩
Glycobiology, Oxford University Press (OUP), 2009, 19 (11), pp.1235-1247. ⟨10.1093/glycob/cwp116⟩
Glycobiology, 2009, 19 (11), pp.1235-1247. ⟨10.1093/glycob/cwp116⟩
Glycobiology, Oxford University Press (OUP), 2009, 19 (11), pp.1235-1247. ⟨10.1093/glycob/cwp116⟩
International audience; Arabinogalactan (AG) and lipoarabinomannan (LAM) are the two major cell wall (lipo)polysaccharides of mycobacteria. They share arabinan chains made of linear segments of alpha-1,5-linked D-Araf residues with some alpha-1,3-bra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf74a7f5b47911feace459bb709a4dcb
https://hal.science/hal-03177973
https://hal.science/hal-03177973
Autor:
Frédéric Boudou, Michel Rivière, Marcelo E. Guerin, Nathalie Barilone, Patricia Charles, Brigitte Gicquel, Mary Jackson, Anne Lemassu, Gustavo Stadthagen, Tounkang Sambou, Mamadou Daffé, Germain Puzo, Pedro M. Alzari, Jana Korduláková
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (37), pp.27270-27276. ⟨10.1074/jbc.M702676200⟩
Journal of Biological Chemistry, 2007, 282 (37), pp.27270-27276. ⟨10.1074/jbc.M702676200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (37), pp.27270-27276. ⟨10.1074/jbc.M702676200⟩
Journal of Biological Chemistry, 2007, 282 (37), pp.27270-27276. ⟨10.1074/jbc.M702676200⟩
International audience; Mycobacteria produce two unusual polymethylated polysaccharides, the 6-O-methylglucosyl-containing lipopolysaccharides (MGLP) and the 3-O-methylmannose polysaccharides, which have been shown to regulate fatty acid biosynthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0f7d626865f79309952ddc06db37a88
https://pubmed.ncbi.nlm.nih.gov/17640872
https://pubmed.ncbi.nlm.nih.gov/17640872