Nombre de documents archivés : 13.
Lemay-St-Denis, Claudèle; Alejaldre, Lorea; Jemouai, Zakaria; Lafontaine, Kiana; St-Aubin, Maxime; Hitache, Katia; Valikhani, Donya; Weerasinghe, Nuwani W; Létourneau, Myriam; Thibodeaux, Christopher J; Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380; Baron, Christian; Copp, Janine N et Pelletier, Joelle N.
(2023).
A conserved SH3-like fold in diverse putative proteins tetramerizes into an oxidoreductase providing an antimicrobial resistance phenotype
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
, vol. 378
, nº 1871:202.
pp. 1-14.
DOI: 10.1098/rstb.2022.0040.
Lemay-St-Denis, Claudèle; Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380 et Pelletier, Joelle N.
(2022).
Integrating dynamics into enzyme engineering
Protein Engineering, Design and Selection
, vol. 35
, nº gzac015.
pp. 1-11.
DOI: 10.1093/protein/gzac015.
Gobeil, Sophie; Ebert, Maximilian; Park, Jaeok; Gagné, Donald; Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380; Berghuis, Albert M.; Pleiss, Jürgen et Pelletier, Joelle N.
(2019).
The Structural Dynamics of Engineered beta-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function
Scientifc Reports
, vol. 9
, nº 6656.
pp. 1-12.
DOI: 10.1038/s41598-019-42866-8.
Gobeil, Sophie; Gagné, Donald; Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380 et Pelletier, Joelle N.
(2016).
15N, 13C and 1H backbone resonance assignments of an artificially engineered TEM-1/PSE-4 class A β-lactamase chimera and its deconvoluted mutant
Biomolecular NMR Assignments
, vol. 10
, nº 1.
pp. 93-99.
DOI: 10.1007/s12104-015-9645-8.
Gobeil, Sophie; Clouthier, Christopher M.; Park, Jaeok; Gagné, Donald; Berghuis, Albert M.; Doucet, Nicolas et Pelletier, Joelle N.
(2014).
Maintenance of Native-like Protein Dynamics May Not Be Required for Engineering Functional Proteins
Chemistry and Biology
, vol. 21
, nº 10.
pp. 1330-1340.
DOI: http://dx.doi.org/ 10.1016/j.chembiol.2014.07.016.
Gobeil, Sophie; Park, Jaeok; Clouthier, Christopher M.; Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380; Berghuis, Albert M. et Pelletier, Joelle N.
(2012).
Structure-based recombination of beta-lactamases: functional, structural and dynamic investigation of artificially-evolved enzymes
In: 26th Annual Symposium of the Protein-Society, August 5–8, 2012, San Diego, California,.
Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380 et Pelletier, Joelle N.
(2009).
Gaining Insight into Enzyme Function through Correlation with Protein Motions
In:
Protein Engineering Handbook.
Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Federal Republic of Germany, pp. 187-211.
De Wals, Pierre-Yves; Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380 et Pelletier, Joelle N.
(2009).
High tolerance to simultaneous active-site mutations in TEM-1 beta-lactamase: Distinct mutational paths provide more generalized beta-lactam recognition
Protein Science
, vol. 18
, nº 1.
pp. 147-160.
DOI: 10.1002/pro.25.
Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380; Savard, Pierre-Yves; Pelletier, Joelle N. et Gagné, Stephane M
(2007).
NMR investigation of Tyr105 mutants in TEM-1 beta-lactamase: dynamics are correlated with function
Journal of Biological Chemistry
, vol. 282
, nº 29.
pp. 21448-21459.
DOI: 10.1074/jbc.M609777200.
Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380 et Pelletier, Joelle N.
(2007).
Simulated annealing exploration of an active-site tyrosine in TEM-1 beta-lactamase suggests the existence of alternate conformations
Proteins
, vol. 69
, nº 2.
pp. 340-348.
DOI: 10.1002/prot.21485.
Chica, Roberto A; Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380 et Pelletier, Joelle N.
(2005).
Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design
Current Opinion in Biotechnology
, vol. 16
, nº 4.
pp. 378-384.
DOI: 10.1016/j.copbio.2005.06.004.
Doucet, Nicolas
ORCID: https://orcid.org/0000-0002-1952-9380; De Wals, Pierre-Yves et Pelletier, Joelle N.
(2004).
Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 beta-lactamase
Journal of Biological Chemistry
, vol. 279
, nº 44.
pp. 46295-46303.
DOI: 10.1074/jbc.M407606200.
Gobeil, Sophie; Park, Jaeok; Ebert, Maximilian; Gagné, Donald; Clouthier, Christopher M.; Pleiss, Jürgen; Doucet, Nicolas; Berghuis, Albert M. et Pelletier, Joelle N.
.
Structure-based recombination of drug resistance enzymes: structural and functional tolerance to new dynamics in artificially-evolved enzymes
In: 2nd Protein Engineering Canada Conference (PEC), 17-19 Juin 2016, Ottawa, Canada.
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