Zobrazeno 1 - 10
of 111
pro vyhledávání: '"Charles, Tellier"'
Autor:
Edward K. Muge, Charles Tellier, Michel Dion, Amélie Saumonneau, Francis Mulaa, Benson Wamalwa, Lydia Awuor Ogonda
Publikováno v:
Biotechnology Letters. 43:691-700
To search for new alkaliphilic cellulases and to improve their efficiency on crystalline cellulose through molecular engineering Two novel cellulases, BpGH9 and BpGH48, from a Bacillus pumilus strain were identified, cloned and biochemically characte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cce7860c2cb7a6378ca5805b34d0cf39
https://doi.org/10.1007/s10529-020-03056-z
https://doi.org/10.1007/s10529-020-03056-z
Autor:
Claude Solleux, Valentina Kalichuk, David Teze, Joan Coines, Corinne André-Miral, Lluís Raich, Carme Rovira, Birte Svensson, Charles Tellier
Publikováno v:
Teze, D, Coines, J, Raich, L, Kalichuk, V, Solleux, C, Tellier, C, André-Miral, C, Svensson, B & Rovira, C 2020, ' A Single Point Mutation Converts GH84 O-GlcNAc Hydrolases into Phosphorylases: Experimental and Theoretical Evidence ', Journal of the American Chemical Society, vol. 142, no. 5, pp. 2120-2124 . https://doi.org/10.1021/jacs.9b09655
Glycoside hydrolases and phosphorylases are two major classes of enzymes responsible for the cleavage of glycosidic bonds. Here we show that two GH84 O-GlcNAcase enzymes can be converted to efficient phosphorylases by a single point mutation. Notewor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::faac0b50615939e885bae04a84487fbf
https://doi.org/10.1021/jacs.9b09655
https://doi.org/10.1021/jacs.9b09655
Autor:
Amélie Saumonneau, Nathan Lagneau, Lydia Awuor Ogonda, Catherine Dupré, Stéphanie Dutertre, Dominique Grizeau, Charles Tellier, Cyrille Grandjean, Franck Daligault
Publikováno v:
Bioresource Technology Reports
Bioresource Technology Reports, 2023, 21, pp.101335. ⟨10.1016/j.biteb.2023.101335⟩
Bioresource Technology Reports, 2023, 21, pp.101335. ⟨10.1016/j.biteb.2023.101335⟩
International audience; Microalgae are a promising alternative resource to fossil-based products. Botryococcus braunii is a colonial green microalga having the ability to convert CO2 by photosynthesis into long chain hydrocarbons. These are excreted
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09f90429efae5ba0991456e8e23aeca8
https://doi.org/10.1016/j.biteb.2023.101335
https://doi.org/10.1016/j.biteb.2023.101335
Autor:
Amélie Saumonneau, Coralie Assailly, Benoît Roubinet, Franck Daligault, Ludovic Landemarre, Francesca François, Cyrille Grandjean, Laurent Fontaine, Sagrario Pascual, paul lottin, Eva-Maria Krammer, frederica vena, Sébastien G. Gouin, David Deniaud, Véronique Montembault, Charles Tellier, Clarisse Bridot, Dimitri Alvarez-Dorta, Julie Bouckaert
Publikováno v:
Chemistry – A European Journal
Chemistry-A European Journal
Chemistry-A European Journal, 2020, ⟨10.1002/chem.202004672⟩
Chemistry-A European Journal, Wiley-VCH Verlag, 2020, ⟨10.1002/chem.202004672⟩
Chemistry-A European Journal
Chemistry-A European Journal, 2020, ⟨10.1002/chem.202004672⟩
Chemistry-A European Journal, Wiley-VCH Verlag, 2020, ⟨10.1002/chem.202004672⟩
Bacterial sialidases (SA) are validated drug targets expressed by common human pathogens such as Streptococcus pneumoniae, Vibrio cholerae, or Clostridium perfringens. Noncovalent inhibitors of bacterial SA capable of reaching the submicromolar level
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14e2ed2352152fdbb4d1ae65f567bc10
Autor:
Lydia A, Ogonda, Amélie, Saumonneau, Michel, Dion, Edward K, Muge, Benson M, Wamalwa, Francis J, Mulaa, Charles, Tellier
Publikováno v:
Biotechnology letters. 43(3)
To search for new alkaliphilic cellulases and to improve their efficiency on crystalline cellulose through molecular engineering RESULTS: Two novel cellulases, BpGH9 and BpGH48, from a Bacillus pumilus strain were identified, cloned and biochemically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a2e73d3269bc08b533c886f017bbb1cc
https://pubmed.ncbi.nlm.nih.gov/33386499
https://pubmed.ncbi.nlm.nih.gov/33386499
Autor:
coralie assailly, clarisse bridot, amélie saumonneau, paul lottin, Benoit Roubinet, Eva-Maria Krammer, francesca François, frederica vena, ludovic landemarre, Dimitri Alvarez-Dorta, david deniaud, cyrille grandjean, charles tellier, Sagrario Pascual, Véronique montembault, Laurent Fontaine, Franck Daligault, Julie Bouckaert, sebastien gouin
Conjugation of the transitionstate-cation analogue DANA to polymeric scaffolds led to highly potent inhibitors of bacterial sialidases. Each clustered DANA on the polymers saw its inhibitory potency for S. pneumoniae or B. thetaiotaomicron sialidases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5aa700c6467ff3cd88a902a760f6c303
https://doi.org/10.26434/chemrxiv.13013291.v1
https://doi.org/10.26434/chemrxiv.13013291.v1
Background The demand for a carbohydrate driven economy coupled with the abundant cellulosic biomass has driven the search for cellulases that can be applied for the utilization of the cellulosic biomass.Context of the study Of special focus for our
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc872ead1a244ff61ecc61c0ef9519bb
https://doi.org/10.21203/rs.3.rs-41635/v1
https://doi.org/10.21203/rs.3.rs-41635/v1
Autor:
David, Teze, Joan, Coines, Lluís, Raich, Valentina, Kalichuk, Claude, Solleux, Charles, Tellier, Corinne, André-Miral, Birte, Svensson, Carme, Rovira
Publikováno v:
Journal of the American Chemical Society. 142(5)
Glycoside hydrolases and phosphorylases are two major classes of enzymes responsible for the cleavage of glycosidic bonds. Here we show that two GH84
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a36c7fac8b5888fed994f1dfd8fb476e
https://pubmed.ncbi.nlm.nih.gov/31917561
https://pubmed.ncbi.nlm.nih.gov/31917561
Publikováno v:
Protein Engineering, Design and Selection
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2019, 32 (7), pp.309-316. ⟨10.1093/protein/gzz032⟩
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2019, 32 (7), pp.309-316. ⟨10.1093/protein/gzz032⟩
Using the information available in the sequences of well-characterized transglycosidases found in plants, mutations were introduced in the glycoside hydrolase of the bacterium Thermus thermophilus, with the aim of turning it into an efficient transgl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d4bbc8f3f3e6428c68a9255078edc3d
https://hal.archives-ouvertes.fr/hal-02322263
https://hal.archives-ouvertes.fr/hal-02322263
Autor:
Charles Tellier, Hélène Rogniaux, Mirjam Czjzek, David Ropartz, Mathieu Fanuel, Robert Larocque, Gurvan Michel, Anaïs Naretto
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (17), pp.6923-6939. ⟨10.1074/jbc.RA118.006609⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294, pp.6923-6939. ⟨10.1074/jbc.ra118.006609⟩
Journal of Biological Chemistry 17 (294), 6923-6939. (2019)
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (17), pp.6923-6939. ⟨10.1074/jbc.RA118.006609⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294, pp.6923-6939. ⟨10.1074/jbc.ra118.006609⟩
Journal of Biological Chemistry 17 (294), 6923-6939. (2019)
International audience; Agars are sulfated galactans from red macroalgae and are composed of a D-galactose (G unit) and L-galactose (L unit) alternatively linked by α-1,3 and β-1,4 glycosidic bonds. These polysaccharides display high complexity, wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b281e24142ba0f035b5ad97f5109a01
https://hal.archives-ouvertes.fr/hal-02137861/file/190222_AgaC_revised_final_figures.pdf
https://hal.archives-ouvertes.fr/hal-02137861/file/190222_AgaC_revised_final_figures.pdf