Year |
Citation |
Score |
2023 |
Lemay-St-Denis C, Pelletier JN. From a binding module to essential catalytic activity: how nature stumbled on a good thing. Chemical Communications (Cambridge, England). 59: 12560-12572. PMID 37791701 DOI: 10.1039/d3cc04209j |
0.318 |
|
2023 |
Lemay-St-Denis C, Alejaldre L, Jemouai Z, Lafontaine K, St-Aubin M, Hitache K, Valikhani D, Weerasinghe NW, Létourneau M, Thibodeaux CJ, Doucet N, Baron C, Copp JN, Pelletier JN. 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. 378: 20220040. PMID 36633286 DOI: 10.1098/rstb.2022.0040 |
0.646 |
|
2022 |
Lemay-St-Denis C, Doucet N, Pelletier JN. Integrating dynamics into enzyme engineering. Protein Engineering, Design & Selection : Peds. PMID 36416215 DOI: 10.1093/protein/gzac015 |
0.629 |
|
2020 |
Deweid L, Hadjabdelhafid-Parisien A, Lafontaine K, Rochet LNC, Kolmar H, Pelletier JN. Glutamine-walking: Creating reactive substrates for transglutaminase-mediated protein labeling. Methods in Enzymology. 644: 121-148. PMID 32943142 DOI: 10.1016/Bs.Mie.2020.04.066 |
0.364 |
|
2019 |
Gobeil SMC, Ebert MCCJC, Park J, Gagné D, Doucet N, Berghuis AM, Pleiss J, Pelletier JN. The Structural Dynamics of Engineered β-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function. Scientific Reports. 9: 6656. PMID 31040324 DOI: 10.1038/S41598-019-42866-8 |
0.759 |
|
2019 |
Quaglia D, Alejaldre L, Ouadhi S, Rousseau O, Pelletier JN. Holistic engineering of Cal-A lipase chain-length selectivity identifies triglyceride binding hot-spot. Plos One. 14: e0210100. PMID 30640952 DOI: 10.1371/Journal.Pone.0210100 |
0.383 |
|
2017 |
Charbonneau DM, Aubé A, Rachel NM, Guerrero V, Delorme K, Breault-Turcot J, Masson JF, Pelletier JN. Development of Asparaginase II for Immunosensing: A Trade-Off between Receptor Density and Sensing Efficiency. Acs Omega. 2: 2114-2125. PMID 30023654 DOI: 10.1021/acsomega.7b00110 |
0.648 |
|
2017 |
Charbonneau DM, Breault-Turcot J, Sinnett D, Krajinovic M, Leclerc JM, Masson JF, Pelletier JN. Tracking silent hypersensitivity reactions to asparaginase during leukemia therapy using single-chip indirect plasmonic and fluorescence immunosensing. Acs Sensors. PMID 29168384 DOI: 10.1021/Acssensors.7B00584 |
0.66 |
|
2017 |
Rachel NM, Toulouse JL, Pelletier JN. Transglutaminase-Catalyzed Bioconjugation Using One-Pot Metal-Free Bioorthogonal Chemistry. Bioconjugate Chemistry. PMID 28898047 DOI: 10.1021/Acs.Bioconjchem.7B00509 |
0.339 |
|
2017 |
Rachel NM, Quaglia D, Lévesque É, Charette AB, Pelletier JN. Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements. Protein Science : a Publication of the Protein Society. PMID 28857311 DOI: 10.1002/Pro.3286 |
0.417 |
|
2017 |
Ebert MC, Pelletier JN. Computational tools for enzyme improvement: why everyone can - and should - use them. Current Opinion in Chemical Biology. 37: 89-96. PMID 28231515 DOI: 10.1016/J.Cbpa.2017.01.021 |
0.34 |
|
2017 |
Quaglia D, Ebert MC, Mugford PF, Pelletier JN. Enzyme engineering: A synthetic biology approach for more effective library generation and automated high-throughput screening. Plos One. 12: e0171741. PMID 28178357 DOI: 10.1371/Journal.Pone.0171741 |
0.357 |
|
2017 |
Ebert MCCJC, Guzman Espinola J, Lamoureux G, Pelletier JN. Substrate-Specific Screening for Mutational Hotspots Using Biased Molecular Dynamics Simulations Acs Catalysis. 7: 6786-6797. DOI: 10.1021/Acscatal.7B02634 |
0.348 |
|
2016 |
Aubé A, Charbonneau DM, Pelletier JN, Masson J. Response Monitoring of Acute Lymphoblastic Leukemia Patients Undergoing l-Asparaginase Therapy: Successes and Challenges Associated with Clinical Sample Analysis in Plasmonic Sensing Acs Sensors. 1: 1358-1365. DOI: 10.1021/Acssensors.6B00531 |
0.654 |
|
2016 |
St-Jacques AD, Rachel NM, Curry DR, Gillet SMFG, Clouthier CM, Keillor JW, Pelletier JN, Chica RA. Specificity of transglutaminase-catalyzed peptide synthesis Journal of Molecular Catalysis B: Enzymatic. 123: 53-61. DOI: 10.1016/J.Molcatb.2015.11.009 |
0.677 |
|
2015 |
Gobeil SM, Gagné D, Doucet N, Pelletier JN. (15)N, (13)C and (1)H backbone resonance assignments of an artificially engineered TEM-1/PSE-4 class A β-lactamase chimera and its deconvoluted mutant. Biomolecular Nmr Assignments. PMID 26386961 DOI: 10.1007/S12104-015-9645-8 |
0.755 |
|
2015 |
Ebert MC, Morley KL, Volpato JP, Schmitzer AR, Pelletier JN. Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active-site substitutions. Protein Science : a Publication of the Protein Society. 24: 495-507. PMID 25401264 DOI: 10.1002/Pro.2602 |
0.374 |
|
2015 |
Gobeil SMC, Gagne D, Doucet N, Pelletier JN. 15N, 13C and 1H backbone resonance assignments of TEM-1(M68L-M69T) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26586 |
0.731 |
|
2014 |
Gobeil SM, Clouthier CM, Park J, Gagné D, Berghuis AM, Doucet N, Pelletier JN. Maintenance of native-like protein dynamics may not be required for engineering functional proteins. Chemistry & Biology. 21: 1330-40. PMID 25200606 DOI: 10.1016/J.Chembiol.2014.07.016 |
0.762 |
|
2014 |
Bukar N, Zhao SS, Charbonneau DM, Pelletier JN, Masson JF. Influence of the Debye length on the interaction of a small molecule-modified Au nanoparticle with a surface-bound bioreceptor. Chemical Communications (Cambridge, England). 50: 4947-50. PMID 24705454 DOI: 10.1039/C4Cc01423E |
0.645 |
|
2014 |
Gundersen MT, Keillor JW, Pelletier JN. Microbial transglutaminase displays broad acyl-acceptor substrate specificity Applied Microbiology and Biotechnology. 98: 219-230. PMID 23615739 DOI: 10.1007/S00253-013-4886-X |
0.354 |
|
2012 |
Clouthier CM, Morin S, Gobeil SM, Doucet N, Blanchet J, Nguyen E, Gagné SM, Pelletier JN. Chimeric β-lactamases: global conservation of parental function and fast time-scale dynamics with increased slow motions. Plos One. 7: e52283. PMID 23284969 DOI: 10.1371/Journal.Pone.0052283 |
0.762 |
|
2012 |
Zhao SS, Bichelberger MA, Colin DY, Robitaille R, Pelletier JN, Masson JF. Monitoring methotrexate in clinical samples from cancer patients during chemotherapy with a LSPR-based competitive sensor. The Analyst. 137: 4742-50. PMID 22943049 DOI: 10.1039/C2An35839E |
0.313 |
|
2012 |
Gnaccarini C, Ben-Tahar W, Mulani A, Roy I, Lubell WD, Pelletier JN, Keillor JW. Site-specific protein propargylation using tissue transglutaminase. Organic & Biomolecular Chemistry. 10: 5258-65. PMID 22653499 DOI: 10.1039/C2Ob25752A |
0.378 |
|
2012 |
Zhao SS, Bolduc OR, Colin DY, Pelletier JN, Masson JF. Development of LSPR and SPR sensor for the detection of an anti-cancer drug for chemotherapy Progress in Biomedical Optics and Imaging - Proceedings of Spie. 8234. DOI: 10.1117/12.909578 |
0.321 |
|
2011 |
Yachnin BJ, Colin DY, Volpato JP, Ebert M, Pelletier JN, Berghuis AM. Novel crystallization conditions for tandem variant R67 DHFR yield a wild-type crystal structure Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 67: 1316-1322. PMID 22102224 DOI: 10.1107/S1744309111030417 |
0.311 |
|
2011 |
Tang MC, Nisole A, Dupont C, Pelletier JN, Waldron KC. Chemical profiling of the deacetylase activity of acetyl xylan esterase A (AxeA) variants on chitooligosaccharides using hydrophilic interaction chromatography-mass spectrometry Journal of Biotechnology. 155: 257-265. PMID 21767585 DOI: 10.1016/J.Jbiotec.2011.06.041 |
0.361 |
|
2011 |
Bolduc OR, Lambert-Lanteigne P, Colin DY, Zhao SS, Proulx C, Boeglin D, Lubell WD, Pelletier JN, Féthière J, Ong H, Masson JF. Modified peptide monolayer binding His-tagged biomolecules for small ligand screening with SPR biosensors. The Analyst. 136: 3142-8. PMID 21698315 DOI: 10.1039/C1An15235A |
0.324 |
|
2011 |
Doucet N, Pelletier JN. Gaining Insight into Enzyme Function through Correlation with Protein Motions Protein Engineering Handbook, Volume 1 & Volume 2. 1: 187-211. DOI: 10.1002/9783527634026.ch7 |
0.613 |
|
2010 |
Morin S, Clouthier CM, Gobeil S, Pelletier JN, Gagné SM. Backbone resonance assignments of an artificially engineered TEM-1/PSE-4 Class A β-lactamase chimera. Biomolecular Nmr Assignments. 4: 127-30. PMID 20383614 DOI: 10.1007/S12104-010-9227-8 |
0.673 |
|
2009 |
Gnaccarini C, Ben-Tahar W, Lubell WD, Pelletier JN, Keillor JW. Fluorometric assay for tissue transglutaminase-mediated transamidation activity Bioorganic and Medicinal Chemistry. 17: 6354-6359. PMID 19660958 DOI: 10.1016/J.Bmc.2009.07.031 |
0.335 |
|
2009 |
Volpato JP, Yachnin BJ, Blanchet J, Guerrero V, Poulin L, Fossati E, Berghuis AM, Pelletier JN. Multiple conformers in active site of human dihydrofolate reductase F31R/Q35E double mutant suggest structural basis for methotrexate resistance Journal of Biological Chemistry. 284: 20079-20089. PMID 19478082 DOI: 10.1074/Jbc.M109.018010 |
0.402 |
|
2009 |
Volpato JP, Pelletier JN. Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: Sequence and structural comparison Drug Resistance Updates. 12: 28-41. PMID 19272832 DOI: 10.1016/J.Drup.2009.02.001 |
0.301 |
|
2009 |
Pardin C, Roy I, Chica RA, Bonneil E, Thibault P, Lubell WD, Pelletier JN, Keillor JW. Photolabeling of tissue transglutaminase reveals the binding mode of potent cinnamoyl inhibitors Biochemistry. 48: 3346-3353. PMID 19271761 DOI: 10.1021/Bi802021C |
0.674 |
|
2009 |
De Wals PY, Doucet N, Pelletier JN. High tolerance to simultaneous active-site mutations in TEM-1 β-lactamase: Distinct mutational paths provide more generalized β-lactam recognition Protein Science. 18: 147-160. PMID 19177359 DOI: 10.1002/Pro.25 |
0.627 |
|
2008 |
Pardin C, Pelletier JN, Lubell WD, Keillor JW. Cinnamoyl inhibitors of tissue transglutaminase Journal of Organic Chemistry. 73: 5766-5775. PMID 18582115 DOI: 10.1021/Jo8004843 |
0.322 |
|
2008 |
Fossati E, Volpato JP, Poulin L, Guerrero V, Dugas DA, Pelletier JN. 2-Tier bacterial and in vitro selection of active and methotrexate- resistant variants of human dihydrofolate reductase Journal of Biomolecular Screening. 13: 504-514. PMID 18566481 DOI: 10.1177/1087057108318783 |
0.374 |
|
2008 |
Keillor JW, Chica RA, Chabot N, Vinci V, Pardin C, Fortin E, Gillet SMFG, Nakano Y, Kaartinen MT, Pelletier JN, Lubell WD. The bioorganic chemistry of transglutaminase - from mechanism to inhibition and engineering Canadian Journal of Chemistry. 86: 271-276. DOI: 10.1139/V08-024 |
0.682 |
|
2007 |
Volpato JP, Fossati E, Pelletier JN. Increasing Methotrexate Resistance by Combination of Active-site Mutations in Human Dihydrofolate Reductase Journal of Molecular Biology. 373: 599-611. PMID 17868689 DOI: 10.1016/J.Jmb.2007.07.076 |
0.312 |
|
2007 |
Doucet N, Pelletier JN. Simulated annealing exploration of an active-site tyrosine in TEM-1β-lactamase suggests the existence of alternate conformations Proteins: Structure, Function and Genetics. 69: 340-348. PMID 17600829 DOI: 10.1002/Prot.21485 |
0.655 |
|
2007 |
Doucet N, Savard PY, Pelletier JN, Gagné SM. NMR investigation of Tyr105 mutants in TEM-1 beta-lactamase: dynamics are correlated with function. The Journal of Biological Chemistry. 282: 21448-59. PMID 17426035 DOI: 10.1074/Jbc.M609777200 |
0.657 |
|
2007 |
Denault M, Pelletier JN. Protein library design and screening: working out the probabilities. Methods in Molecular Biology (Clifton, N.J.). 352: 127-154. PMID 17041263 DOI: 10.1385/1-59745-187-8:127 |
0.346 |
|
2005 |
Gillet SMFG, Pelletier JN, Keillor JW. A direct fluorometric assay for tissue transglutaminase Analytical Biochemistry. 347: 221-226. PMID 16289009 DOI: 10.1016/J.Ab.2005.09.035 |
0.309 |
|
2005 |
Chica RA, Doucet N, Pelletier JN. Semi-rational approaches to engineering enzyme activity: Combining the benefits of directed evolution and rational design Current Opinion in Biotechnology. 16: 378-384. PMID 15994074 DOI: 10.1016/J.Copbio.2005.06.004 |
0.767 |
|
2004 |
Schmitzer AR, Lépine F, Pelletier JN. Combinatorial exploration of the catalytic site of a drug-resistant dihydrofolate reductase: Creating alternative functional configurations Protein Engineering, Design and Selection. 17: 809-819. PMID 15576381 DOI: 10.1093/Protein/Gzh090 |
0.344 |
|
2004 |
Doucet N, De Wals PY, Pelletier JN. Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 β-lactamase Journal of Biological Chemistry. 279: 46295-46303. PMID 15326193 DOI: 10.1074/Jbc.M407606200 |
0.652 |
|
2004 |
Tousignant A, Pelletier JN. Protein motions promote catalysis Chemistry and Biology. 11: 1037-1042. PMID 15324804 DOI: 10.1016/J.Chembiol.2004.06.007 |
0.392 |
|
2004 |
Chica RA, Gagnon P, Keillor JW, Pelletier JN. Tissue transglutaminase acylation: Proposed role of conserved active site Tyr and Trp residues revealed by molecular modeling of peptide substrate binding Protein Science. 13: 979-991. PMID 15010546 DOI: 10.1110/Ps.03433304 |
0.683 |
|
2004 |
Gillet SMFG, Chica RA, Keillor JW, Pelletier JN. Expression and rapid purification of highly active hexahistidine-tagged guinea pig liver transglutaminase Protein Expression and Purification. 33: 256-264. PMID 14711514 DOI: 10.1016/J.Pep.2003.10.003 |
0.675 |
|
2002 |
Arndt KM, Pelletier JN, Müller KM, Plückthun A, Alber T. Comparison of in vivo selection and rational design of heterodimeric coiled coils. Structure (London, England : 1993). 10: 1235-48. PMID 12220495 DOI: 10.1016/S0969-2126(02)00838-9 |
0.466 |
|
2002 |
Amstutz P, Pelletier JN, Guggisberg A, Jermutus L, Cesaro-Tadic S, Zahnd C, Plückthun A. In vitro selection for catalytic activity with ribosome display. Journal of the American Chemical Society. 124: 9396-403. PMID 12167034 DOI: 10.1021/Ja025870Q |
0.504 |
|
2001 |
Pelletier J, Sidhu S. Mapping protein-protein interactions with combinatorial biology methods Current Opinion in Biotechnology. 12: 340-347. PMID 11551461 DOI: 10.1016/S0958-1669(00)00225-1 |
0.324 |
|
2000 |
Michnick SW, Remy I, Campbell-Valois FX, Vallée-Bélisle A, Pelletier JN. Detection of protein-protein interactions by protein fragment complementation strategies. Methods in Enzymology. 328: 208-30. PMID 11075347 DOI: 10.1016/S0076-6879(00)28399-7 |
0.77 |
|
2000 |
Arndt KM, Pelletier JN, Müller KM, Alber T, Michnick SW, Plückthun A. A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble. Journal of Molecular Biology. 295: 627-39. PMID 10623552 DOI: 10.1006/Jmbi.1999.3352 |
0.659 |
|
1999 |
Pelletier JN, Arndt KM, Plückthun A, Michnick SW. An in vivo library-versus-library selection of optimized protein-protein interactions. Nature Biotechnology. 17: 683-90. PMID 10404162 DOI: 10.1038/10897 |
0.643 |
|
1998 |
Pelletier JN, Campbell-Valois FX, Michnick SW. Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments. Proceedings of the National Academy of Sciences of the United States of America. 95: 12141-6. PMID 9770453 DOI: 10.1073/Pnas.95.21.12141 |
0.65 |
|
1997 |
Pelletier JN, Michnick SW. A protein complementation assay for detection of protein-protein interactions in vivo Protein Engineering. 10: 89. |
0.55 |
|
1996 |
Allaire M, Li Y, Mejia NR, Pelletier JN, MacKenzie RE, Cygler M. Crystallization of the bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase domain of the human trifunctional enzyme Proteins: Structure, Function and Genetics. 26: 479-480. PMID 8990501 DOI: 10.1002/(Sici)1097-0134(199612)26:4<479::Aid-Prot9>3.0.Co;2-6 |
0.587 |
|
1996 |
Pelletier JN, Mackenzie RE. Methenyltetrahydrofolate cyclohydrolase catalyzes the synthesis of (6S)-5-formyltetrahydrofolate Bioorganic Chemistry. 24: 220-228. DOI: 10.1006/Bioo.1996.0020 |
0.581 |
|
1995 |
Pelletier JN, MacKenzie RE. Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase Biochemistry. 34: 12673-12680. PMID 7548019 DOI: 10.1021/Bi00039A025 |
0.61 |
|
1994 |
Pelletier JN, MacKenzie RE. Binding to the 2′,5′-ADP subsite stimulates cyclohydrolase activity of human NADP+-dependent methylenetetrahydrofolate dehydrogenase/cyclohydrolase Biochemistry. 33: 1900-1906. PMID 8110794 DOI: 10.1021/Bi00173A037 |
0.621 |
|
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