118.      E. W. J. Gates, A. Prince-Hallée, Y. Heidari, A. Sedighi, J. W. Keillor : “High Affinity Fluorogenic Substrate for Tissue Transglutaminase Reveals Enzymatic Hysteresis”, Biochemistry 2023, 62, 3085-3095.

117.      E. W. J. Gates, N. D. Calvert, N. J. Cundy, F. Brugnoli, P. Navals, A. Kirby, N. Bianchi, G. Adhikary, A. J. Shuhendler, R. L. Eckert, J. W. Keillor* : “Cell Impermeable Inhibitors Confirm that Intracellular Human Transglutaminase 2 is Responsible for the Transglutaminase-Associated Cancer Phenotype”, Int. J. Mol. Sci. 2023, 24, 12546-12563.

116.      M. Gallo, E. Ferrari, A. Terrazzan, F. Brugnoli, A. Spisni, C. Taccioli, G. Aguiari, A. Trentini, S. Volinia, J. W. Keillor, C. M. Bergamini, N. Bianchi*, T. A. Pertinhez : “Metabolic characterisation of transglutaminase 2 inhibitor effects in breast cancer cell lines”, FEBS J. 2023, 290, 5411–5433.

115.      S. K. I. Watt, J.G. Charlebois, C. N. Rowley, and J. W. Keillor. “A kinetic study of thiol addition to N-phenylchloroacetamide”. Org. Biomol. Chem. 2023, 21 922-932.

114.      X. Chen, G. Adhikary, J. J. Newland, W. Xu, J. W. Keillor, D. J. Weber, R. L. Eckert* : “Transglutaminase 2 binds to the CD44v6 cytoplasmic domain to stimulate CD44v6/ERK1/2 signaling and maintain an aggressive cancer phenotype”, Mol. Cancer Res. 2023, 21, 922-932.

113.      A. Buchler, U. S. Ismailani, N. MacMullin, F. Abdirahman, M. Adi, C. Bi, C. Jany, J. W. Keillor, and B. H. Rotstein. “Quinazoline-2-Carboxamides as Selective PET Radiotracers for Matrix Metalloproteinase-13 Imaging in Atherosclerosis”. J. Med. Chem. 2023, 66, 6682-6696.

112.      X.-Y. Qin*, Y. Furutani, K. Yonezawa, N. Shimizu, M. Kato-Murayama, M. Shirouzu, L. Gailhouste, R. Shrestha, J. W. Keillor, S. Fujii, H. Kagechika, T. Masaki, T. Matsuura : “Targeting transglutaminase 2 mediated membrane heparin sulfate signaling in liver cancer stem cells with acyclic retinoid”, Cell Death Dis. 2023, 14, 358.

111.      S. K. I. Watt, J.G. Charlebois, C. N. Rowley, and J. W. Keillor. “A mechanistic study of thiol addition to N-acryloylpiperidine”. Org. Biomol. Chem. 2023, 21, 2204-2212.

110.      E. W. J. Gates, K. Mansour, S. E. Samani, S. Shad, M. T. Kaartinen, and J. W. Keillor. “Peptidic Inhibitors and a Fluorescent Probe for the Selective Inhibition and Labelling of Factor XIIIa Transglutaminase”. Molecules 2023, 28, 1634.

109.      R. Canella, F. Brugnoli, M. Gallo, J. W. Keillor, A. Terrazzan, E. Ferrari, S. Grassilli, E. W. J. Gates, S. Volinia, V. Bertagnolo, N. Bianchi, and C. M. Bergamini. “A Multidisciplinary Approach Establishes a Link between Transglutaminase 2 and the Kv10.1 Voltage-Dependent K+ Channel in Breast Cancer”. Cancers 2023, 15, 178.

108.      N. J. Cundy, J. Arciszewski, E. W. J. Gates, S. L. Acton, K. D. Passley, E. Awoonor-Williams, E. K. Boyd, N. Xu a, É. Pierson, C. Fernandez-Ansieta, M. R. Albert, N. M. R. McNeil, G. Adhikary, R. L. Eckert, and J. W. Keillor. “Novel irreversible peptidic inhibitors of transglutaminase 2”. RSC Med. Chem., 2023, 14, 378-385.

107.      L. Mader, S. K. I. Watt, H. R. Iyer, L. Nguyen, H. Kaurb, and J. W. Keillor. “The war on hTG2: warhead optimization in small molecule human tissue transglutaminase inhibitors”. RSC Med. Chem., 2023, 14, 277-298.

106.      S. K. I. Watt, J.G. Charlebois, C. N. Rowley, and J. W. Keillor. “A mechanistic study of thiol addition to N-phenylacrylamide”. Org. Biomol. Chem., 2022, 20, 8898-8906.

105.      A. M. M. Rangaswamy, P. Navals, E. W. J. Gates, S. Shad, S. K. I. Watt, and J. W. Keillor. “Structure-activity relationships of hydrophobic alkyl acrylamides as tissue transglutaminase inhibitors”. RSC Med. Chem. 2022, 13, 413-428.

104.      N. M. R. McNeil, E. W. J. Gates, N. Firoozi, N. J. Cundy, J. Leccese, S. Eisinga, J. D. A. Tyndall, G. Adhikary, R. L. Eckert, and J. W. Keillor. “Structure-activity relationships of N-terminal variants of peptidomimetic tissue transglutaminase inhibitors”. Eur. J. Med. Chem. 2022, 232, 114172.

103.      G. Aguiari, F. Crudele, C. Taccioli, L. Minotti, F. Corrà, J. W. Keillor, C. Cervellati, S. Volinia, C. M. Bergamini, and N. Bianchi* “Dysregulation of Transglutaminase type 2 through GATA3 defines aggressiveness and Doxorubicin sensitivity in breast cancer”. Int. J. Biol. Sci. 2022, 18, 1-14.

102.      E. A. Rorke, G. Adhikary, H. Szmacinski, J. R. Lakowicz, D. J. Weber, R. Godoy-Ruiz, P. Puranik, J. W. Keillor, E. W. J. Gates, and R. L. Eckert* : “Sulforaphane covalently interacts with transglutaminase type 2 to alter its structure and suppress its activity”. Mol. Carcinog. 2022, 61, 19-32.

101.      N. Bianchi*, F. Brugnoli*, S. Grassilli, K. Bourgeois, J. W. Keillor, C. M. Bergamini, G. Aguiari, S. Volinia, V. Bertagnolo : “The motility and mesenchymal features of breast cancer cells correlate with the levels and intracellular localization of Transglutaminase type 2”, Cells 2021, 10, 3059-3077.

100.      A. Elahi, J. Emerson, J. Rudlong, J. W. Keillor, G. Salois, A. Visca, P. Girardi, G. V. W. Johnson*, C. Proschel : “Deletion or inhibition of astrocytic transglutaminase 2 promotes functional recovery after spinal cord injury”, Cells 2021, 10, 2942-2956.

99.        J. W. Keillor, G. V. W. Johnson* : “Transglutaminase 2 as a therapeutic target for neurological conditions”, Expert Opin. Ther. Targets 2021, 25, 721-731.

98.        X. Chen, G. Adhikary, S. Shrestha, W. Xu, J. W. Keillor, W. Naselsky, R. L. Eckert* : “Transglutaminase 2 maintains hepatocyte growth factor signaling to enhance the cancer cell phenotype”, Mol. Cancer Res. 2021, 19, 2026-2035.

97.   S.-Y. Kim*, J. W. Keillor : “A Precision Strategy to Cure Renal Cell Carcinoma by Targeting Transglutaminase 2”, Int. J. Mol. Sci. 2020, 21, 2493-2504.

96.   K. Jambrovics, I. P. Uray, J. W. Keillor, L. Fésüs,. Z. Balajthy* “Benefits of combined all-trans retinoic acid and arsenic trioxide treatment of acute promyelocytic leukemia cells and further enhancement by inhibition of atypically expressed transglutaminase 2”, Cancers 2020, 12, 648-660.

95.   K. K. Tsao , A. C. Lee, K. É. Racine, J. W. Keillor : “Site-specific fluorogenic protein labelling agent for bioconjugation”, Biomolecules2020, 10, 369-384.

94.   B. Maffei, M. Laverrière, Y. Wu, S. Triboulet, S. Perrinet, M. Duchateau, M. Matondo, R. L. Hollis, C. Gourley, J. Rupp, J. W. Keillor, A. Subtil* : “Infection-driven activation of transglutaminase 2 boosts glucose uptake and hexosamine biosynthesis in epithelial cells”, EMBO J. 2020, 242, 1838-1856.

93.   K. Jambrovics, I. P. Uray, Z. Keressztesy, J. W. Keillor, L. Fésüs, Z. Balajthy* : “Transglutaminase 2 programs differentiating acute promyelocytic leukemia cells in all-trans retinoic acid treatment to inflammatory stage through NF-κB activation.”, Haematologica 2019, 104, 505-515.

92.   W. Kiattiburut, R. Zhi, S. G. Lee, A. C. Foo, D. Hickling, J. W. Keillor, N. K. Goto, W. Li, W. Conlan, J. B. Angel, G. Wang, N. Tanphaichitr* : “Antimicrobial peptide LL-37 and its truncated peptides, GI-20 and GF-17, exert spermicidal effects and microbicidal impacts on Neisseria gonorrhoeae”, Hum. Reprod. 2018, 33, 2175-2183.

91.   G. Adhikary, D. Grun, H. R. Alexander, J. S. Friedberg, W. Xu, J. W. Keillor, S. Kandasamy, R. L. Eckert* : “Transglutaminase is a mesothelioma cancer stem cell survival protein that is required for tumor formation”, Oncotarget 2018, 9, 34495-34505.

90.   M. A. R. Raycroft, K. E. Racine, C. N. Rowley, J. W. Keillor : “Mechanisms of Alkyl and Aryl Thiolate Addition to N-Methylmaleimide”, J. Org. Chem. 2018, 83, 11674-11685.

89.  M. Strmiskova, K. Tsao, J. W. Keillor : “Rational Design of a Highly Reactive Dicysteine Peptide Tag For Fluorogenic Protein Labelling”, Org. Biomol. Chem. 201816, 6332-6340.

88.  Y. Chen, K. Tsao, S. L. Acton, J. W. Keillor : “A BODIPY-based, super-fluorogenic, protein-specific labelling agent”, Angew. Chem. Int. Ed.2018, 57, 12390-12394.

87. S. K. Oteng-Pabi, C. M. Clouthier, J. W. Keillor : “Design of a Glutamine Substrate Tag Enabling Protein Labelling Mediated by Bacillus subtilisTransglutaminase”, PLoS ONE 2018, 13, e0197956. Open Access DOI: 10.1371/journal.pone.0197956

86.  M. Basso, H. H. Chen, D. Tripathy, M. Conte, K. Y. P. Apperley, A. De Simone, J. W. Keillor, R. Ratan, L. Altucci, A. Milelli* : “Designing Novel Dual Transglutaminase 2 / Histone Deacetylase Inhibitors Effective in Halting Neuronal Death”, ChemMedChem 2018, 13, 227-230.

85.  A. Akbar, N. M. R. McNeil, M. R. Albert, V. Ta, K. Bourgeois, and J. W. Keillor : “Structure-Activity Relationships of potent, targeted covalent inhibitors that abolish both the transamidation and GTP binding activities of human tissue transglutaminase” J. Med. Chem. 2017, 60, 7910-7927.

84.  A. De Simone, A. Braschieri, K. Y. P. Apperley, H. H. Chen, M. Guardigni, S. Montanari, L. Valgimigli, V. Andrisano, J. W. Keillor, M. Basso, M. Bartolini, A. Milelli* : “Hydroxy-substituted Trans-cinnamoyl Derivatives as Multifunctional Tools in the Context of Alzheimer’s Disease” Eur. J. Med. Chem. 2017, 139, 378-389.

83.   J. Feola, A. Barton, A. Akbar, J. W. Keillor, G. V. W. Johnson : “Transglutaminase 2 modulation of NF-κB signaling in astrocytes is independent of its ability to mediate astrocytic viability in ischemic injury”  Brain Res. 2017, 1668, 1–11.

82.   K. Y. P. Apperley, I. Roy, V. Saucier, N. Brunet-Filion, S.-P. Piscopo, C. Pardin, É. De Francesco, C. Hao, J. W. Keillor : “Development of new scaffolds as reversible tissue transglutaminase inhibitors, with improved potency or resistance to glutathione addition”, Med. Chem. Comm. 2017, 8, 338-345.

81.   C. Kerr, H. Szmacinski, M. Fisher, B. Nance, J. R. Lakowicz, A. Akbar, J. W. Keillor, E. A. Toth, D. J. Weber, R. L. Eckert* : “Transamidase site-targeted compounds produce a conformation change that inhibits GTP binding to the transglutaminase cancer stem cell survival protein to reduce cancer stem cell survival” Oncogene 2017, 36, 2981-2990.

80. S. Gundemir, A. Monteagudo, A. Akbar, J. W. Keillor, Gail V.W. Johnson* : “The Complex Role of Transglutaminase 2 in Glioblastoma Proliferation” Neuro-Oncology 2017, 19, 208-218.

79.   A. Monteagudo, C. Ji; A. Akbar; J. W. Keillor, G. V. W. Johnson* : “Inhibition or Ablation of Transglutaminase 2 Impairs Astrocyte Migration” Biochem. Biophys. Res. Comm. 2016, 482, 942-947.

78.   M. L. Fisher, C. Kerr, G. Adhikary, D. Grun, W. Xu, J. W. Keillor, and R. L. Eckert* : “Transglutaminase interacts with α6/β4-integrin to stimulate YAP1-dependent ΔNp63α stabilization leading to enhanced cancer stem cell survival and tumor formation”, Cancer Research 2016, 76, 7265-7275.

77. G. G. Mironov, C. M. Clouthier, A. Akbar, J. W. Keillor, M. V. Berezovski* : “Simultaneous Analysis of Enzyme Structure and Activity by Kinetic Capillary Electrophoresis and Mass Spectrometry”  Nature Chem. Biol. 2016, 12, 918-922.

76. J. W. Keillor, K. Y. P. Apperley : “Transglutaminase Inhibitors: A Patent Review” Exp. Opin. Therap. Pat. 2016, 26, 49-63.

75. A. D. St-Jacques, N. M. Rachel, D. R. Curry, S. M. F. G. Gillet, C. M. Clouthier, J. W. Keillor, J. N. Pelletier, R. A. Chica : “Specificity of Transglutaminase-Catalyzed Peptide Synthesis” J. Mol. Cat. B 2016, 123, 53-61.

74. Y. Chen, K. Tsao, É. De Francesco, J. W. Keillor : “Ring substituent effects on the thiol addition and hydrolysis reactions of N-arylmaleimides” J. Org. Chem. 2015, 80, 12182-12192.

73. S. Abraham, K. Keillor, C. J. Capicciotti, G. E. Perley-Robertson, J. W. Keillor, R. N. Ben* : “Quantitative Analysis of the Efficacy and Potency of Novel Small Molecule Ice Recrystallization Inhibitors (IRIs)” Cryst. Growth Des. 2015, 10, 5034-5039.

72. M. L. Fisher, G. Adhikary, W. Xu, C. Kerr, J. W. Keillor, R. L. Eckert* : “Type II Transglutaminase Stimulates Epidermal Cancer Stem Cell Epithelial-Mesenchymal Transition” Oncotarget 2015, 6, 20525-20539.

71. M. L. Fisher, J. W.Keillor, W. Xu, R. L. Eckert*, C. Kerr : “Type II Transglutaminase Is Required For Epidermal Squamous Cell Carcinoma Stem Cell Survival” Mol. Cancer Res. 2015, 13, 1083-1094.

70. J. W. Keillor : “Inhibition of transglutaminase”, In Transglutaminases: multiple functional modifiers and targets for new drug discovery, Eds. K. Hitomi and S. Kojima, Springer 2015, pp. 2347-372.

69. J. W. Keillor, K. Y. P. Apperley, A. Akbar : “Inhibitors of Tissue Transglutaminase”, Trends Pharm. Sci. 2015, 36, 32-40.

68. Y. Chen, K. Tsao, J. W. Keillor : “Fluorogenic Protein Labelling: A Review of Photophysical Quench Mechanisms and Principles of Fluorogen Design”, Can. J. Chem. 2015, 93, 389-398.

67. Y. Chen, C. M. Clouthier, K. Tsao, M. Strmiskova, H. Lachance, J. W. Keillor : “Coumarin-Based Fluorogenic Probes for No-wash Protein Labeling”, Angew. Chem. Int. Ed. 2014, 53, 13785-13788.

66. Y. Chen, J. W. Keillor : “Development of Dimaleimide Based Fluorogens: An Application for Protein Labelling”, Imaging & Microscopy 2014, 16, 28-30.

65. J. W. Keillor, C. M. Clouthier, K. Y. P. Apperley, A. Akbar, A. Mulani : “Acyl Transfer Mechanisms of Tissue Transglutaminase”, Bioorg. Chem. 2014, 57, 186-197.

64. S. K. Oteng-Pabi, C. Pardin, M. Stoica, J. W. Keillor : “Site-specific Protein Labelling and Immobilization Mediated by Microbial Transglutaminase”, Chem. Comm. 2014, 50, 6604-6606.

63. S. K. Oteng-Pabi, J. W. Keillor : “Continuous Enzyme-Coupled Assay for Microbial Transglutaminase Activity”, Anal. Biochem. 2013, 441, 169-173.

62. M. T. Gundersen, J. W. Keillor, J. N. Pelletier* : “Microbial transglutaminase displays broad acyl-acceptor substrate specificity”, App. Microbiol. Biotech. 2013, 98, 219-230.

61. Y. Song, L. L. Kirkpatrick, A. B. Schilling, D. L. Helseth, N. Chabot, J. W. Keillor, G. V.W. Johnson, S. T. Brady* : “Transglutaminase and Polyamination of Tubulin: Posttranslational Modification for Stabilizing Axonal Microtubules”, Neuron 2013, 78, 109-123.

(Cover art solicited for the April 2013 issue.)

60. I. Roy, O. Smith, C. M. Clouthier, J. W. Keillor : “Expression, Purification and Kinetic Characterization of Human Tissue Transglutaminase”, Prot. Exp. & Purif. 2013, 87, 41-46.

59. C. M. Clouthier, G. G. Mironov, V. Okhonin, M. V. Berezovski, J. W. Keillor* : “Real-time monitoring of protein conformational dynamics in solution using kinetic capillary electrophoresis”, Angew. Chem. Int. Ed. 2012, 51, 12464-12468.

58. N. S. Caron, L. N. Munsie, J. W. Keillor, R. Truant*: “Tranglutaminase Type 2 Enzyme Inhibitors Can Hold TG2 In Either Open Or Closed Conformations”, PLoS ONE, 2012, 7, e44159.

57. C. Gnaccarini, W. Ben-Tahar, A. Mulani, I. Roy, W. D. Lubell, J. N. Pelletier, J. W. Keillor* : “Site-Specific Protein Propargylation Using Tissue Transglutaminase.”, Org. Biomol. Chem. 2012, 10, 5258-5265.

56. J. Szychowski, J. Kondo, O. Zahr, K. Auclair, E. Westhof, S. Hanessian*, J. W. Keillor* : “Inhibition of Aminoglycoside-Deactivating Enzymes APH(3′)-IIIa and AAC(6′)-Ii by Paromomycin O2” Analogues”, ChemMedChem 2011, 6, 1961-1966.

(Selected for the cover of the November 2011 issue.)

55. K. Caron, V. Lachapelle, J. W. Keillor : “Dramatic Increase of Quench Efficiency in “Spacerless” Dimaleimide Fluorogens”, Org. Biomol. Chem. 2011, 9, 185-197.

54. D. J. Stigers, Z. I. Watts, J. E. Hennessy, H.-K. Kim, R. Martini, M. Taylor, J. W. Keillor, N. E. Dixon, C. J. Easton* : “Incorporation of Chlorinated Isosteres of Aliphatic Amino Acids During Cell-Free Protein Expression”, Chem. Comm. 2011, 47, 1839-1841.

53. J. W. Keillor, N. Chabot, I. Roy, A. Mulani, O. Leogane, C. Pardin : “Irreversible Inhibitors of Tissue Transglutaminase”, Adv. Enzymol. 2011, 78, 415-448.

52. H. F. Al-Jallad, V. Myneni, S. Piercy, N. Chabot, A. Mulani, J. W. Keillor, M. T. Kaartinen* : “Plasma Membrane Factor XIIIA Transglutaminase Activity Regulates Osteoblast Matrix Secretion and Deposition by Affecting Microtubule Stabilization”, PLoS ONE2011, 6, e15893.

51. G. Colak, J. W. Keillor, G. V. W. Johnson* : “Cytosolic Guanine Nucledotide Binding Deficient Form of Transglutaminase 2 (R580a) Potentiates Cell Death in Oxygen Glucose Deprivation.”, PLoS ONE2011, 6, e16665.

50. N. Chabot, S. Moreau, A. Mulani, P. Moreau, J. W. Keillor* : “Fluorescent Probes of Tissue Transglutaminase Reveal Its Association with Arterial Stiffening”, Chem. & Biol. 2010, 17, 1143-1150.

(Selected for the cover of the 28 October 2010 issue.)

49. J. Guy, R. Castonguay, N.B. Campos-Reales Piñeda, V. Jacquier, K. Caron, S. W. Michnick, J. W. Keillor* : “De novo helical peptides as target sequences for a specific, fluorogenic protein labelling strategy”, Mol. BioSys. 2010, 6, 976-987.

(Selected for the cover of the June 2010 issue.)

48. C. Gnaccarini, W. Ben-Tahar, W.D. Lubell, J. N. Pelletier, J. W. Keillor*: “Fluorometric Assay for Tissue Transglutaminase-Mediated Transamidation Activity”, Bioorg. Med. Chem. 2009, 17, 6354-6359.

47. C. Pardin, R. A. Chica, I. Roy, E. Bonneil, P. Thibault, W. Lubell, J. N. Pelletier, J. W. Keillor*: “Photolabeling of Tissue Transglutaminase Reveals Binding Mode of Potent Cinnamoyl Inhibitors”, Biochemistry 2009, 48, 3346-3353.

46. I. W. McNae, J. Martinez-Oyanedel, J. W. Keillor, P. A. Michels, L. A. Fothergill-Gilmore, M. D. Walkinshaw* : “The Crystal Structure of ATP-bound Phosphofructokinase from Trypanosoma brucei Reveals Conformational Transitions Different from those of Other Phosphofructokinases”  J. Mol. Biol. 2009, 385, 1519-1533.

45. C. Pardin, I. Roy, W. D. Lubell, J. W. Keillor*: “Reversible and competitive triazole-based inhibitors of tissue transglutaminase”, Chem. Biol. Drug Design 2008, 72, 189-196.

44. C. Pardin, J. N. Pelletier, W. D. Lubell, J. W. Keillor*: “Cinnamoyl inhibitors of tissue transglutaminase”, J. Org. Chem. 2008, 73, 5766-5775.

43. J. W. Keillor*, R. A. Chica, N. Chabot, V. Vinci, C. Pardin, E. Fortin, S. M. F. G. Gillet, Y. Nakano, M. T. Kaartinen, J. N. Pelletier, W. D. Lubell : “The Bioorganic Chemistry of Transglutaminase: From Mechanism to Inhibition and Engineering”, Can. J. Chem. 2008, 86, 271-276.

(Selected for the cover of the April 2008 issue.)

42. R. Castonguay, D. Halim, M. Morin, C. Lherbet, E. Bonneil, A. Furtos, P. Thibault, J. W. Keillor* : “Kinetic Characterization and Identification of the Acylation and Glycosylation Sites of Recombinant Human gamma-Glutamyltranspeptidase”, Biochemistry 2007, 46, 12253-12262.

41. J. Guy, K. Caron, S. Dufresne, S. W. Michnick, W. G. Skene*, J. W. Keillor* : “Convergent Preparation and Photophysical Characterization of Dimaleimide Dansyl Fluorogens: Elucidation of the Maleimide Fluorescence Quenching Mechanism”, J. Am. Chem. Soc. 2007, 129, 11969-11977.

40. C. Gravel, D. Lapierre, J. Labelle, J. W. Keillor : “Acyl Transfer from Carboxylate, Carbonate and Thiocarbonate Esters to Enzymatic and Non-Enzymatic Thiolates”, Can. J. Chem., 2007, 85, 164-174.

39. S. Hanessian,* J. Szychowski, P. Kandasamy, N. B. Campos-Reales Pineda, A. Furtos, J. W. Keillor* : “Ring-to-Ring Macrocyclic Aminoglycosides as Probes for APH(3′)IIIa Kinase”, Bioorg. Med. Chem. Lett. 2007, 17, 3221-3225.

38. J. Martinez-Oyanedel, I. W. McNae, M. W. Nowicki, J. W. Keillor, P. A. M. Michels, L. A. Fothergill-Gilmore and M. D. Walkinshaw* : “The First Crystal Structure of Phosphofructokinase from a Eukaryote: Trypanosoma brucei”, J. Mol. Biol. 2007, 366, 1185-1198.

37. D. Halim, K. Caron, J. W. Keillor : “Synthesis and Evaluation of Peptidic Maleimides as Transglutaminase Inhibitors”, Bioorg. Med. Chem. Lett. 2007, 17, 305-308.

36. C. Pardin, S. M. F. G. Gillet, J. W. Keillor : “Synthesis and Evaluation of Peptidic Irreversible Inhibitors of Tissue Transglutaminase”, Bioorg. Med. Chem. 2006, 14, 8379-8385.

35. M. Morin, C. Rivard, J. W. Keillor : “Gamma-Glutamyl Transpeptidase Acylation with Peptidic Substrates: Free Energy Relationships Measured by an HPLC Kinetic Assay”, Org. Biomol. Chem. 2006, 4, 3790-3801.

(Selected by the RSC for the Chemical Biology Virtual Journal 2006, 19.)

34. S. M. F. G. Gillet, J. N. Pelletier, J. W. Keillor : “A Direct Continuous Fluorometric Assay for Tissue Transglutaminase”, Anal. Biochem. 2005, 347, 221-226.

33. J. W. Keillor, R. Castonguay, C. Lherbet : “Gamma-Glutamyl Transpeptidase Substrate Specificity and Catalytic Mechanism”, Methods Enzymol. 2005, 401, 449-467.

32. J. W. Keillor : “Tissue Transglutaminase Inhibitors”, Chem. & Biol. 2005, 12, 410-412.

31. C. Lherbet, R. Castonguay, J. W. Keillor : “Transesterification of Trialkyl Phosphates from Alkyl Bromides”, Tetrahedron Lett. 2005, 46, 3565-3567.

30. S. Girouard, M.-H. Houle, A. Grandbois, J. W. Keillor*, S. W. Michnick : “Synthesis and Characterization of Dimaleimide Fluorogens Designed for Labeling of Specific Proteins”, J. Am. Chem. Soc. 2005, 127, 559-566.

29. C. Lherbet, C. Gravel, J. W. Keillor : “Synthesis of S-Alkyl L-Homocysteine Analogues of Glutathione and their Kinetic Studies with gamma-Glutamyl Transpeptidase”, Bioorg. Med. Chem. Lett. 2004, 14, 3451-3455.

28. J. W. Keillor, A. Ménard, R. Castonguay, C. Lherbet, C. Rivard : “Pre-Steady State Kinetic Studies of Rat Kidney gamma-Glutamyl Transpeptidase Confirm its Ping-Pong Mechanism”, J. Phys. Org. Chem. 2004, 17, 529-536.

27. R. A. Chica, P. Gagnon, J. W. Keillor, J. N. Pelletier : “Tissue transglutaminase acylation: proposed role of conserved active site Tyr and Trp residues revealed by molecular modelling of peptide substrate binding”, Prot. Sci. 2004, 13, 979-991.

26. C. Lherbet, J. W. Keillor : “Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulphur derivatives of L-glutamic acid”, Org. Biomol. Chem. 2004, 2, 238-245.

25. S. M. F. G. Gillet, R. A. Chica, J. W. Keillor, J. N. Pelletier : “Expression in Escherichia coli and Purification of Hexahistidine-Tagged Guinea Pig Liver Transglutaminase”, Prot. Exp. & Purif. 2004, 33, 256-264.

24. R. Castonguay, C. Lherbet, J. W. Keillor : “Kinetic Studies of Rat Kidney gamma-Glutamyl Transpeptidase Deacylation Reveal a General-Base-Catalysed Mechanism”, Biochemistry 2003, 42, 11504-11513.

23. C. Lherbet, M. Morin, R. Castonguay, J. W. Keillor : “Synthesis of Aza and Oxaglutamyl-p-nitroanilide Derivatives and their Kinetic Studies with gamma-Glutamyltranspeptidase”, Bioorg. Med. Chem. Lett. 2003, 13, 997-1000.

22. J. W. Keillor, C. Lherbet, R. Castonguay, D. Lapierre, J. Martinez-Oyanedel, L. A. Fothergill-Gilmore, M. D. Walkinshaw : “Expression, purification, crystallisation and preliminary crystallographic analysis of Trypanosoma brucei phosphofructokinase”, Acta Cryst. D 2003, 59, 532-534.

21. P. Gagnon, X. Huang, É. Therrien, J. W. Keillor : “Peptide Coupling of Unprotected Amino Acids Through In Situ p‑Nitrophenyl Ester Formation”, Tetrahedron Lett. 2002, 43, 7717-7719.

20. R. Castonguay, C. Lherbet, J. W. Keillor : “Mapping of the Active Site of -Glutamyl Transpeptidase Using Activated Esters and their Amide Derivatives”, Bioorg. Med. Chem. 2002, 10, 4185-4191.

19. P. de Macédo, C. Marrano, J. W. Keillor : “Synthesis of Dipeptide-Bound Epoxides and ,-Unsaturated Amides as Potential Irreversible Transglutaminase Inhibitors”, Bioorg. & Med. Chem.2002, 10, 355-360.

18. A. Ménard, R. Castonguay, C. Lherbet, C. Rivard, Y. Roupioz, J. W. Keillor : “Nonlinear Free Energy Relationship in the General-Acid-Catalyzed Acylation of Rat Kidney gamma-Glutamyl Transpeptidase by a Series of gamma-Glutamyl Anilide Substrate Analogues”, Biochemistry 2001, 40, 12678-12685.

17. C. Marrano, P. de Macédo, P. Gagnon, D. Lapierre, J. W. Keillor : “Synthesis and Evaluation of Dipeptide-Bound 1,2,4-Thiadiazoles as Irreversible Transglutaminase Inhibitors”, Bioorg. & Med. Chem. 2001, 9, 3231-3241.

16. C. Marrano, P. de Macédo, J. W. Keillor : “Evaluation of Novel Dipeptide-Bound alpha, beta-Unsaturated Amides and Epoxides as Irreversible Inhibitors of Guinea Pig Liver Transglutaminase”, Bioorg. & Med. Chem. 2001, 9, 1923-1928.

15. A. Leblanc, C. Gravel, J. Labelle, J. W. Keillor : “Kinetic Studies of Guinea Pig Liver Transglutaminase Reveal a General Base Catalyzed Deacylation Mechanism”, Biochemistry 2001, 40, 8335-8342.

14. X. Huang, J. W. Keillor : “Methyl Carbamate Formation via Modified Hofmann Rearrangement Reactions: Methyl p-Methoxyphenylcarbamate”, Organic Syntheses 2001, 78, 234-238.

13. P. de Macédo, C. Marrano, J. W. Keillor : “A Direct and Continuous Spectrophotometric Assay for Transglutaminase Mediated Transpeptidation Activity”, Anal. Biochem. 2000, 285, 16-20.

12. N. Day, J. W. Keillor : “A Continuous Spectrophotometric Linked-Enzyme Assay for Transglutaminase Mediated Transpeptidation Activity”, Anal. Biochem. 1999, 274, 141-144.

11. A. Leblanc, N. Day, A. Ménard, J. W. Keillor : “Guinea Pig Liver Transglutaminase: A Modified Purification Procedure Affording Enzyme with Superior Activity in Greater Yield”, Prot. Exp. & Purif. 1999, 17, 89-95.

10. X. Huang, N. Day, X. Luo, Y. Roupioz, M. Seid, J. W. Keillor : “Synthesis and Characterization of a Series of Novel Glutamic gamma-15N-Anilide Dipeptides”, J. Pept. Res. 1999, 53, 126-133.

9. X. Huang, X. Luo, Y. Roupioz, J. W. Keillor : “Controlled Regioselective Anilide Formation from Aspartic and Glutamic Anhydrides”, J. Org. Chem. 1997, 62, 8821-8825.

8. X. Huang, M. Seid, J. W. Keillor : “A Mild and Efficient Modified Hofmann Rearrangement”, J. Org. Chem. 1997, 62, 7495-7496.

7. X. Huang, J. W. Keillor : “Preparation of Methyl Carbamates via a Modified Hofmann Rearrangement”, Tetrahedron Lett. 1997, 38, 313-316.

6. J. W. Keillor, W. P. Jencks : “Phosphorylation of the Sodium-Potassium Adenosinetriphosphatase Proceeds Through a Rate-Limiting Conformational Change Followed by Rapid Phosphoryl Transfer”, Biochemistry 1996, 35, 2750-2753.

5. J. W. Keillor, A. A. Neverov, R. S. Brown : “Catalysis of Amide Hydrolysis and Formation under Neutral Conditions by a Zwitterionic Imidazolium Thiolate”, J. Am. Chem. Soc. 1994, 116, 4669-4673.

4. J. W. Keillor, R. S. Brown : “Attack of Zwitterionic Thiolates on a Distorted Anilide as a Model for the Acylation of Papain by Amides. A Simple Demonstration of a Bell-Shaped pH-Rate Profile”, J. Am. Chem. Soc. 1992, 114, 7983-7989.

3. J. W. Keillor, R. S. Brown : “Reaction of a Distorted Amide with Nucleophilic Thiolate-Containing Zwitterions Produced from Thiolamines. A Model for the Acylation Step in Cysteine Proteases and Transglutaminases”, J. Am. Chem Soc. 1991, 113, 5114-5116.

2. H. Slebocka-Tilk, A. J. Bennet, J. W. Keillor, R. S. Brown, J. Peter Guthrie, A. Jodhan : “18O Exchange Accompanying the Basic Hydrolysis of Primary, Secondary, and Tertiary Toluamides. 2. The Importance of Amine Leaving Abilities from the Anionic Tetrahedral Intermediates”, J. Am. Chem. Soc. 1990, 112, 8507-8514.

1. V. Somayaji, J. Keillor, R. S. Brown : “Model for the Aspartate Proteinases : Hydrolysis of a Distorted Amide Catalyzed by Dicarboxylic Acids Capable of Forming Cyclic Anhydrides”, J. Am. Chem. Soc. 1988, 110, 2625-2629.