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2021<\/span><\/h3>\n
86. Rufo, N.; Korovesis, D.; Van Eygen, S.; Derua, R.; Garg, A.D.; Finotello, F.; Vara-Perez, M.; Dewaele, M., De Witte, P.A.; Alexopoulos, L.; Janssens, S.; Sinkkonen, L.; Sauter, T.; Verhelst, S. H. L., Agostinis, P. (2021) The IRE1 inhibitor KIRA6 curtails the inflammatory trait of immunogenic anticancer treatments by targeting HSP60 independent of IRE1. Cell Death Diff.<\/em>, accepted.<\/p>\n
85. Kahler, J.P.; Verhelst, S. H. L. (2021) Phosphinate esters as novel warheads for activity-based probes targeting serine proteases. RSC Chem. Biol.<\/em>, 2: 1285-1290.<\/p>\n
84. Korovesis, D.; Beard, H. A.; M\u00e9rillat, C.; Verhelst, S. H. L. (2021) Probes for photoaffinity labeling of kinases. ChemBioChem<\/em>, 2206-2218. Selected as \u2018very important paper\u2019.<\/p>\n
83. Beard, H. A.; Korovesis, D.; Chen, S.; Verhelst, S. H. L. (2021) Cleavable linkers and their application in MS-based target identification. Mol. Omics<\/em>, 17: 197-209.<\/p>\n
82. Yang, J.; Mendowicz, R. J.; Verhelst, S. H. L. (2021) Tagged benzoxazin-4-ones as novel activity-based probes for serine proteases. ChemBioChem<\/em>, 22: 1578-1581. Selected as \u2018very important paper\u2019.<\/p>\n
81. Van Kersavond, T.; Konopatzki, R.; Van de Plassche, M. A. T.; Yang, J.; Verhelst, S. H. L. (2021) Rapid synthesis of internal peptidyl a-ketoamides by on resin oxidation for the construction of rhomboid protease inhibitors. RSC Adv.<\/em>, 11: 4196-4199.<\/p>\n
80. Barniol-Xicota, M.; Verhelst, S. H. L. (2021) Comparative analysis of maleic acid copolymer-based lipid nanodiscs reveals preferential lipid and protein solubilization. Communications Biol.<\/em>, 4: 218.<\/p>\n
79. Hamouda, N.N.; Van Den Haute, C.; Vanhoutte, R.; Sannerud, R.; Azfar, M.; Mayer, R.; Cortes-Calabuig, A.; Swinnen, J. V.; Agostinis, P.; Baekelandt, V.; Annaert, W.; Impens, F.; Verhelst, S. H. L.; Eggermont, J.; Martin, S.; Vangheluwe, P. (2021) ATP13A3 is a new member of the mammalian polyamine transport system. J. Biol. Chem.<\/em>, 296:100182.<\/p>\n
2020<\/span><\/h3>\n
78. Verhelst, S. H. L.; Bonger, K. M.; Willems, L. I. (2020) Bioorthogonal reactions in activity-based protein profiling. Molecules<\/em>, 25: 5994.<\/p>\n
77. Korovesis, D.; Rufo, N.; Derua, R.; Agostinis, P.; Verhelst, S. H. L. (2020) Photoaffinity labeling for off-target profiling of kinase inhibitors: low selectivity profile of the IRE1 targeting imidazopyrazine-based KIRA6 inhibitor. ACS Chem. Biol.<\/em>, 15: 3106\u20133111.<\/p>\n
76. Vanhoutte, R.; Van de Plassche, M. A. T.; Verhelst, S. H. L. (2020) Rapid solid phase construction of serine hydrolase probes results in selective activity-based probes for acyl protein thioesterases-1\/2. J. Med. Chem.<\/i>, 63: 11845-11853.<\/p>\n
75. Chakrabarty, S.; Verhelst, S. H. L. (2020) Controlled inhibition of apoptosis by photoactivatable caspase inhibitors. Cell Chem. Biol.<\/i>, 27: 1434-1440. Highlighted in The Scientist<\/em> magazine, January 2021.<\/p>\n
74. Kahler, J.P.; Lenders, S.; Van de Plassche, M. A. T.; Verhelst, S. H. L. (2020) Facile synthesis of aminomethyl phosphinate esters as serine protease inhibitors with primed site interaction. ACS Med. Chem. Lett.<\/i>, 11: 1739-1744.<\/p>\n
73. Van de Plassche, M. A. T.; Barniol-Xicota, M.; Verhelst, S. H. L. (2020) Peptidyl Acyloxymethyl Ketones as Activity-Based Probes for the Main Protease of SARS-CoV-2. ChemBioChem<\/i>, 21: 3383-3388. Indicated as Very Important Paper; Featured on the front cover; Highlighted in The Voice, International Student Publication<\/em>, based in Leuven, January 2021.<\/p>\n\n\n
72. Van de Plassche, M.; O\u2019Neill, T. J.; Seeholzer, T.; Turk, B.; Krappmann, D.; Verhelst, S. H. L. (2020) Use of non-natural amino acids for the design and synthesis of a selective, cell-permeable MALT1 activity-based probe, J. Med. Chem.<\/em>, 6:3996-4004. <\/p>\n\n\n\n
71. Kahler, J. P.; Vanhoutte, R.; Verhelst, S. H. L. (2020) Activity-based protein profiling of serine protease in immune cells. Arch. Immunol. Ther. Exp.<\/em>, accepted. <\/p>\n\n\n\n
70. Barniol-Xicota, M.; Verhelst, S. H. L. Isolation of intramembrane proteases in membrane-like environments. Biochem. Biophys. Acta – Biomembranes <\/em>, 1862(4):183-193 .<\/p>\n\n\n\n
69. Van Veen, S.; Martin, S.; Van den Haute, C. Benoy, V.; Schuermans, M.; Lyons, J.; Vanhoutte, R.; Kahler, J. P.; Decuypere, J.-P.; Swinnen, J.; Annaert, W. Agostinis, P.; Ghesqui\u00e8re, B.; Verhelst, S.; Baekelandt, V.; Eggermont, J.; Vangheluwe, P. ATP13A2 deficiency disrupts lysosomal polyamine export. Nature<\/em>, 578:419-424.<\/p>\n\n\n\n
2019<\/h3>\n\n\n\n
68. Beard, H.; Barniol-Xicota, M.; Yang, J.; Verhelst, S. H. L. (2019) Discovery of cellular roles of intramembrane proteases, ACS Chem. Biol.<\/em>, 14: 2372-2388.<\/em><\/p>\n\n\n\n
67. Mnatsakanyan, R.; Markoutsa, S.; Wallbrunn, K.; Roos, A.; Verhelst, S. H. L.; Zahedi^{, <\/sup>R. P. (2019) Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique. Nature Comm.<\/em>, 10: 2195.<\/em><\/p>\n\n\n\n}
66. Chakrabarty, S.; Kahler, J. P.; Van de Plassche, M. A. T.; Vanhoutte, R.; Verhelst, S. H. L. (2019) Recent advances in activity-based protein profiling of proteases, Curr. Top. Microbiol. Immunol.<\/em>, 420: 253-281.<\/p>\n\n\n\n
65. Van Kersavond, T.; Konopatzki, R.; Chakrabarty, S.; Blank-Landeshammer, B.; Sickmann, A.; Verhelst, S. H. L. (2019) Short peptides with uncleavable peptide bond mimetics as photoactivatable protease inhibitors. Molecules<\/em>, 24: 206.<\/p>\n\n\n\n
2018<\/h3>\n\n\n\n
64. Barniol-Xicota, M.; Verhelst, S. H. L. (2018) Stable and Functional Rhomboid Proteases in Lipid Nanodiscs by Using Diisobutylene\/Maleic Acid Copolymers. J. Am. Chem. Soc.<\/em>, 140: 14557-14561.<\/p>\n\n\n\n
63. Arutyunova, E.; Jiang, Z.; Yang, J.; Kulepa, A. N.; Young, H. S.; Verhelst, S.; O\u2019Donoghue, A. J.; Lemieux, M. J. (2018) Internally quenched peptide as new model substrate for rhomboid intramembrane proteases, Biol. Chem.<\/em>, 399: 1389-1397.<\/p>\n\n\n\n
62. Goncalves, P.; Verhelst, S. H. L. (2018) Chemical probes targeting proteases for imaging and diagnostics in cancer, in: Extracellular Targeting of Cell Signaling in Cancer: Strategies Directed at MET and RON Receptor Tyrosine Kinase Pathways (Eds. Janetka, J. W.; Benson, R. M.), Wiley-VCH, chapter 12, 351-376.<\/p>\n\n\n\n
61. Nguyen, M. T. N.; Shema, G.; Zahedi, R. P.; Verhelst, S. H. L. (2018) Protease specificity profiling in a pipette tip using \u201ccharged-synchronized\u201d proteome-derived peptide libraries, J. Proteome Res.<\/em>, 17: 1923-1933.<\/p>\n\n\n\n
60. Vanhoutte, R.; Kahler, J. P.; Martin, S.; Van Veen, S.; Verhelst, S. H. L. (2018) Clickable polyamine derivatives as chemical probes for the polyamine transport system, ChemBioChem<\/em>, 19: 907-911. Featured as inside back cover<\/a>.<\/p>\n\n\n\n
59. Shema, G.; Nguyen, M. T. N.; Solari, F. A.; Loroch, S.; Venne, A. S.; Kollipara, L.; Sickmann, A.; Vehelst, S. H. L.; Zahedi, R. P. (2018) Simple, scalable and ultra-sensitive tip-based identification of protease substrates, Mol. Cell. Proteomics<\/em>, 17: 826-834.<\/p>\n\n\n\n
58. Yang, J.; Barniol-Xicota, M.; Nguyen, M. T. N.; Tich\u00e1, A.; Strisovsky, K.; Verhelst, S. H. L. (2018) Benzoxazin-4-ones as novel, easily accessible inhibitors for rhomboid proteases, Bioorg. Med. Chem. Lett.<\/em>, 28: 1423-1427.<\/p>\n\n\n\n
2017<\/h3>\n\n\n\n
57. Goel, P.; Jumpertz, T.; Mikles, D. C.; Tich\u00e1, A.; Nguyen, M. T. N.; Verhelst, S.; Hubalek, M.; Johnson, D. C.; Bachovchin, D. A.; Ogorek, I.; Pietrzik, C. U.; Strisovsky, K.; Schmidt, B.; Weggen, S. (2017) Discovery and biological evaluation of potent and selective N-methylene saccharin-derived inhibitors for rhomboid intramembrane proteases, Biochemistry<\/em>, 56: 6713-6725.<\/p>\n\n\n\n
56. Tich\u00e1, A.; Stanchev, S.; Vinothkumar, K. R.; Mikles, D. C.; Pachl, P.; \u0160vehlov\u00e1, K.; Nguyen, M. T. N.; Verhelst, S. H. L.; Johnson, D. C.; Bachovchin, D. A.; Lep\u0161\u00edk, M.; Majer, P.; Strisovsky, K. (2017) A modular and generalizable route to potent, selective and pharmacologically compliant inhibitors of rhomboid proteases, Cell Chem. Biol.<\/em>, 24: 1523-1536. Highlighted in: Cell Chem. Biol., 24: 1431-1433.<\/p>\n\n\n\n
55. Van Kersavond, T.; Nguyen, M. ; Verhelst, S. H. L. (2017) Synthesis and application of activity-based probes for proteases, Methods Mol. Biol.<\/em> 1574: 255-266.<\/p>\n\n\n\n
54. Wolf, E. V.; Verhelst, S. H. L. (2017) Activity-based protein profiling, in: Chemoselective and Bioorthogonal Ligation Reactions: Concepts and Applications (Eds Algar, R.; Dawson, P.; Medintz, I.), Wiley-VCH.<\/p>\n\n\n\n
53. Yang, Y.; Fonovic, M.; Verhelst, S. H. L. (2017) Cleavable linkers in chemical proteomics applications. Methods Mol. Biol.<\/em>, 1491: 185-203.<\/p>\n\n\n\n
52. Verhelst, S. H. L. (2017) Intramembrane proteases as drug targets. FEBS J.<\/em>, 284: 1489-1502.<\/p>\n\n\n\n
2016<\/h3>\n\n\n\n
51. Verdoes, M.; Verhelst, S. H. L.(2016) Detection of protease activity in cells and animals. Biochemical Biophysical Acta<\/em>, 1864: 130-142.<\/p>\n\n\n\n
50. Wolf, E. V.; Verhelst, S. H. L. (2016) Inhibitors of rhomboid proteases. Biochimie<\/em>, 122:38-47. Recommended by Faculty of 1000.<\/p>\n\n\n\n
2015<\/h3>\n\n\n\n
49. Nguyen, M.; Van Kersavond, T.; Verhelst, S. H. L. (2015) Chemical tools for the study of intramembrane proteases. ACS Chem. Biol.<\/em>, 10: 2423-2434.<\/p>\n\n\n\n
48. Wolf, E. V.; Zeissler, A.; Verhelst, S. H. L. (2015) Inhibitor fingerprinting of rhomboid proteases by activity-based protein profiling reveals inhibitor selectivity and rhomboid autoprocessing. ACS Chem. Biol.<\/em>, 10: 2325-2333.<\/p>\n\n\n\n
47. Wolf, E. V.; Seybolt, M.; Hadravova, R.; Strisovsky, K.; Verhelst, S. H. L. (2015) Activity-based protein profiling of rhomboid proteases in liposomes. ChemBioChem<\/em>, 16: 1616-1621.<\/p>\n\n\n\n
46. Serim, S.; Baer, P.; Verhelst, S. H. L. (2015) Mixed Alkyl Aryl Phosphonate Esters as Quenched Fluorescent Activity-Based Probes for Serine Proteases. Org. Biomol. Chem.<\/em>, 13: 2293-2299.<\/p>\n\n\n\n
45. Eitelhuber, A. C.; Vosyka, O.; Nagel, D.; Bognar, M.; Lenze, D.; Lammens, K.; Schlauderer, F.; Hlahla, D.; Hopfner, K.-P.; Lenz, G.; Hummel, M.; Verhelst, S. H. L.; Krappmann, D. (2015) Activity-based probes for detection of active MALT1 paracaspase in immune cells and lymphomas. Chem. Biol.<\/em>, 22: 129-138.<\/p>\n\n\n\n
2014<\/h3>\n\n\n\n
44. Choo, J. A. L.; Thong, S. Y.; Yap, J.; Van Esch, W. J. E.; Raida, M.; Meijers, R.; Lescar, J.; Verhelst, S. H. L.; Grotenbreg, G. M. (2014) Bioorthonogal Cleavage and Exchange of Major Histocompatibility Complex Ligands employing Azobenzene-containing (Abc) peptides. Angew. Chem. Int. Ed.<\/em>, 53:13390-13394.<\/p>\n\n\n\n
43. Haedke, U. R.; Frommel, S. C.; Hansen, F.; Hahne, H.; Kuster, B.; Bogyo, M.; Verhelst, S. H. L. (2014) Phosphoramidates as novel activity-based probes for serine proteases. ChemBioChem<\/em>, 15: 1106-1110. Recommended by Faculty of 1000.<\/p>\n\n\n\n
2013<\/h3>\n\n\n\n
42. Yang, Y.; Yang, X.; Verhelst, S. H. L. (2013) Comparative analysis of click chemistry mediated activity-based protein profiling in cell lysates. Molecules<\/em>, 18: 12599-12608. Special issue Advances in Click Chemistry<\/em>.<\/p>\n\n\n\n
41. Serim, S.; Mayer, S. V.; Verhelst, S. H. L. (2013) Tuning Activity-Based Probe Selectivity for Serine Proteases by On-Resin \u2018Click\u2019 Construction of Peptide Diphenyl Phosphonates. Org. Biomol. Chem.<\/em>, 11: 5714-5721.<\/p>\n\n\n\n
40. Wolf, E. V.; Zeissler, A.; Vosyka, O.; Zeiler, E.; Sieber, S. A.; Verhelst, S. H. L. (2013) A new class of rhomboid protease inhibitors discovered by activity-based fluorescence polarization. PLoS ONE<\/em>, 8: e72307.<\/p>\n\n\n\n
39. Schlauderer, F.; Lammens, K.; Nagel, D.; Vincendeau, M.; Eitelhuber, A. C.; Verhelst, S. H. L.; Kling, D.; Chrusciel, A.; Ruland, J.; Krappmann, D.; Hopfner, K. P. (2013) Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase. Angew. Chem. Int. Ed.<\/em>, 52: 10384-10387.<\/p>\n\n\n\n
38. Yang, Y.; Verhelst. S. H. L. (2013) Cleavable trifunctional biotin reagents for protein labeling, capture and release. Chem. Commun.<\/em> 49: 5366. Selected as \u2018hot article\u2019.<\/p>\n\n\n\n
37. Verhelst, S. H. L. (2013) Probing functional tyrosines. Chem. Biol., 20: 457-458. Commentary on: Chem. Biol.<\/em> 2013, 20: 541-548.<\/p>\n\n\n\n
36. Vosyka, O.; Vinothkumar, K. R.; K\u00fcttler, E. V.; Brouwer, A. J.; Liskamp, R. J. M.; Verhelst, S. H. L. (2013) Activity-based probes for rhomboid proteases discovered in a mass spectrometry-based assay. Proc. Natl. Acad. Sci. USA<\/em>, 110: 2472-2477.<\/p>\n\n\n\n
35. Lu, H.; Wang, Z.; Shabab, M.; Oeljeklaus, J.; Verhelst, S. H.; Kaschani, F.; Kaiser, M.; Bogyo, M.; Van der Hoorn, R. A. (2013) A substrate-insipred probe monitors translocation, activation and subcellular localization of bacterial type III effector protease AvrPphB. Chem. Biol.<\/em>, 20: 168-176. Highlighted in: Chem. Biol.<\/em> 2013, 20: 137-138.<\/p>\n\n\n\n
34. Battenberg, O. A.; Yang, Y.; Verhelst, S. H. L.; Sieber, S. A. (2013) Target profiling of 4-hydroxyderricin in S. aureus reveals seryl-tRNA synthetase binding and inhibition by covalent modification. Mol. Biosyst.<\/em>, 9: 343-351.<\/p>\n\n\n\n
33. Haedke, U.; K\u00fcttler, E. V.; Vosyka, O.; Yang, Y.; Verhelst, S. H. L. (2013) Tuning probe selectivity for chemical proteomics applications. Curr. Opin. Chem. Biol.<\/em>, 17: 102-109.<\/p>\n\n\n\n
32. Yang, Y.; Hahne, H.; K\u00fcster, B.; Verhelst, S. H. L. (2013) A Simple and Effective Cleavable Linker for Chemical Proteomics Applications. Mol. Cell. Proteomics<\/em>, 12: 237-244.<\/p>\n\n\n\n
2012<\/h3>\n\n\n\n
31. Serim, S.; Haedke, U.; Verhelst, S. H. L. (2012) Activity-based probes for the study of proteases: recent advances and developments. ChemMedChem<\/em>, 7: 1146-1159.<\/p>\n\n\n\n
30. Haedke, U.; G\u00f6tz, M.; Baer, P.; Verhelst, S. H. L. (2012) Alkyne derivatives of isocoumarins as clickable activity-based probes for serine proteases. Bioorg. Med. Chem.<\/em>, 20: 633-640.<\/p>\n\n\n\n
2010<\/h3>\n\n\n\n
29. Vinothkumar, K. R.; Strisovsky, K.; Andreeva, A.; Christova, Y.; Verhelst, S. H. L.; Freeman, M. (2010) The structural basis for catalysis and substrate specificity of a rhomboid protease. EMBO J.<\/em>, 29: 3797-3809.<\/p>\n\n\n\n
2009<\/h3>\n\n\n\n
(work from post-doc, PhD and undergraduate)<\/p>\n\n\n\n
28. Ravindran, S.; Lodoen, M. B.; Verhelst, S. H. L.; Bogyo, M.; Boothroyd, J. C. (2009) 4-Bromophenacyl bromide specifically inhibits rhoptry secretion during Toxoplasma invasion. PlosOne<\/em>, 4: e8143.<\/p>\n\n\n\n
27. Beckham, S. A.; Piedrafita, D.; Phillips, C. I.; Samarawickrema, N.; Law, R. H. P.;Smooker, P. M.; Quinsey, N. S.; Irving, J. A.; Greenwood, S.; Verhelst, S. H. L.; Bogyo, M.; Turk, B.; Coetzer, T. H.; Wijeyewickrema, L. C.; Spithill, T. W.; Pike R. N. (2009) A major Cathepsin B protease from the liver fluke Fasciola hepatica exhibits novel biochemical properties and plays a vital role in the survival of newly excysted juvenile forms in vitro. Int. J. Biochem. Cell Biol.<\/em>, 41: 1601-1612.<\/p>\n\n\n\n
26. Kaschani, F.; Verhelst, S. H. L.; Van Swieten, P. F.; Wang, Z.; Kaiser, M.; Overkleeft, H. S.; Bogyo, M.; Van der Hoorn, R. A. L. (2009) Minitags for small molecules: detecting targets of reactive small molecules in living plant tissues using click-chemistry. The Plant Journal<\/em>, 57:373-385.<\/p>\n\n\n\n
25. Yang, Z.; Fonovic, M.; Verhelst, S. H. L.; Blum, G.; Bogyo, M. (2009) Evaluation of a,b-unsaturated ketone-based probes for papain-family cysteine proteases. Bioorg. Med. Chem.<\/em>, 17: 1071-1078.<\/p>\n\n\n\n
2007<\/h3>\n\n\n\n
24. Burster, T.; Marin-Esteban, V.; Boehm, B. O.; Dunn, S.; Rotzschke, O.; Falk, K.; Weber, E.; Verhelst, S. H. L.; Kalbacher, H.; Driessen, C. (2007) Design of protease-resistant myelin basic protein-derived peptides by cleavage site directed amino acid substitutions. Biochem. Pharm.<\/em>, 74: 1514-1523.<\/p>\n\n\n\n
23. Fonovic, M.; Verhelst, S. H. L.; Sorum, M. T.; Bogyo, M. (2007) Proteomic evaluation of chemically cleavable activity based probes. Mol. Cell. Proteomics<\/em>, 6: 1761-1770.<\/p>\n\n\n\n
22. Sadaghiani, A. M.; Verhelst, S. H. L.; Gocheva, V.; Hill, K.; Majerova, E.; Stinson, S.; Joyce, J. A.; Bogyo, M. (2007) Design, synthesis and evaluation of in vivo potency and selectivity of epoxysuccinyl-based inhibitors of papain family cysteine proteases. Chem. Biol.<\/em>, 14: 499-511.<\/p>\n\n\n\n
21. Verhelst, S. H. L.; Fonovic, M.; Bogyo, M. (2007) A mild chemically cleavable linker system for functional proteomic applications. Angew. Chem. Int. Ed.<\/em>, 46: 1284-1286.<\/p>\n\n\n\n
20. Cuerrier, D.; Moldoveanu, T.; Campbell, R. L.; Kelly, J.; Yoruk, B.; Verhelst, S. H. L. ; Greenbaum, D.; Bogyo, M.; Davies, P. L. (2007) Development of calpain-specific inactivators by screening of positional-scanning epoxide libraries. J. Biol. Chem.<\/em>, 282: 9600-9611.<\/p>\n\n\n\n
19. Sexton, K. B.; Kato, D.; Berger, A.; Fonovic, M.; Verhelst, S. H. L.; Bogyo, M. (2007) Specificity of aza-peptide electrophile activity-based probes of caspases. Cell Death Differ.<\/em>, 14: 727-732.<\/p>\n\n\n\n
18. Sadaghiani, A. M.; Verhelst, S. H. L.; Bogyo, M. (2007) Tagging and detection strategies for activity-based proteomics. Curr. Opin. Chem. Biol.<\/em>, 11: 20-28.<\/p>\n\n\n\n
2006<\/h3>\n\n\n\n
17. Sadaghiani, A. M.; Verhelst, S. H. L.; Bogyo, M. (2006) Solid phase methods for the preparation of epoxysuccinate-based inhibitors of cysteine proteases. J. Comb. Chem.<\/em>, 8: 802-804.<\/p>\n\n\n\n
16. Yuan, F.; Verhelst, S. H. L.; Blum, G.; Coussens, L. M.; Bogyo, M. (2006) A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I\/cathepsin C. J. Am. Chem. Soc.<\/em>, 128: 5616-5617.<\/p>\n\n\n\n
15. Verhelst, S. H. L.; Witte, M. D.; Arastu-Kapur, S.; Fonovic, M.; Bogyo, M. (2006) Novel aza peptide inhibitors and active site probes of papain family cysteine proteases. ChemBioChem<\/em>, 7: 943-950.<\/p>\n\n\n\n
2005<\/h3>\n\n\n\n
14. Kato, D.;* Verhelst, S. H. L.;* Sexton, K. B.; Bogyo, M. (2005) A general solid phase method for the preparation of diverse azapeptide probes directed against cysteine proteases. Org. Lett.<\/em>, 7: 5649-5652. equal authorship.<\/p>\n\n\n\n*
13. Verhelst, S. H. L.; Bogyo, M. (2005) Solid phase synthesis of double headed epoxysuccinyl activity based probes for selective targeting of papain family cysteine proteases. ChemBioChem<\/em>, 6: 824-827.<\/p>\n\n\n\n
12. Verhelst, S. H. L.; Bogyo, M. (2005) Dissecting protein function using chemical proteomic methods. QSAR Comb. Sci.<\/em>, 24: 261-269.<\/p>\n\n\n\n
11. Verhelst, S. H. L.; Bogyo, M. (2005) Chemical proteomics applied to target identification and drug discovery. Biotechniques<\/em>, 38: 175-177.<\/p>\n\n\n\n
10. Chehade, K. A. H.; Baruch, A.; Verhelst, S. H. L., Bogyo, M. (2005) An improved preparation of the activity-based probe JPM-OEt and in situ applications. Synthesis<\/em>, 240-244.<\/p>\n\n\n\n
9. Timmer, M. S. M.; Verhelst, S. H. L.; Grotenbreg, G. M.; Overhand, M.; Overkleeft, H. S. (2005) Carbohydrates as versatile platforms in the construction of small compound libraries. Pure & Applied Chem.<\/em>, 77: 1173-1182.<\/p>\n\n\n\n
2004<\/h3>\n\n\n\n
8. Verhelst, S. H. L.; Magn\u00e9e, L.; Wennekes, T.; Wiedenhof, W.; Van der Marel, G. A.; Overkleeft, H. S.; Van Boeckel, C. A. A.; Van Boom, J. H. (2004) Glycosylation of cyclitols: novel analogs of aminoglycoside antibiotics. Eur. J. Org. Chem.<\/em> 11: 2404-2410.<\/p>\n\n\n\n
7. Verhelst, S. H. L.; Michiels, P. J. A.; Van der Marel, G. A.; Van Boeckel, C. A. A.; Van Boom, J. H. (2004) Surface plasmon resonance evaluation of various aminoglycoside \u2013 RNA hairpin interactions reveals low degree of selectivity. ChemBioChem<\/em>, 5: 937-942.<\/p>\n\n\n\n
6. Verhelst, S. H. L.; Wennekes, T.; Van der Marel, G. A.; Overkleeft, H. S.; Van Boeckel, C. A. A.; Van Boom, J. H. (2004) Synthesis of orthogonally protected 2-deoxystreptamine stereoisomers. Tetrahedron<\/em> 60: 2813-2822.<\/p>\n\n\n\n
2003<\/h3>\n\n\n\n
5. Verhelst, S. H. L.; Paez Martinez, B.; Timmer, M. S. M.; Lodder, G.; Van der Marel, G. A.; Overkleeft, H. S.; Van Boom, J. H. (2003) A short chiral route towards polyhydroxylated indolizidines and quinolizidines. J. Org. Chem.<\/em> 68: 9598-9603.<\/p>\n\n\n\n
2002<\/h3>\n\n\n\n
4. Verhelst, S. H. L.; Wiedenhof, W.; Ovaa, H.; Van der Marel, G. A.; Overkleeft, H. S.; Van Boeckel, C. A. A.; Van Boom, J. H. (2002) A stereoselective route towards highly functionalized 4,6-diaminocyclohexene derivatives. Tetrahedron Lett.<\/em> 43: 6451-6455.<\/p>\n\n\n\n
2000<\/h3>\n\n\n\n
3. Shi, G. P.; Bryant, R. A. R.; Riese, R.; Verhelst, S.; Driessen, C.; Li, Z. Q.; Br\u00f6mme, D.; Ploegh, H. L.; Chapman, H. A. (2000) Role for cathepsin F in invariant chain processing and major histocompatability complex class II peptide loading by macrophages. J. Exp. Med.<\/em> 191: 1177-1185.<\/p>\n\n\n\n
2. Bogyo, M.; Verhelst, S.; Bellingard-Dubouchaud, V.; Toba, S.; Greenbaum, D. (2000) Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs. Chem. Biol.<\/em> 7: 27-38.<\/p>\n\n\n\n
1999<\/h3>\n\n\n\n
1. Overkleeft, H. S.; Verhelst, S. H. L.; Pieterman, E.; Meeuwenoord, N. J.; Overhand, M.; Cohen, L. H.; Van der Marel, G. A.; Van Boom, J. H. (1999) Design and synthesis of a protein: farnesyltransferase inhibitor based on sugar amino acids. Tetrahedron Lett.<\/em> 40: 4103-4106.<\/p>\n","protected":false},"excerpt":{"rendered":"
2021 86. Rufo, N.; Korovesis, D.; Van Eygen, S.; Derua, R.; Garg, A.D.; Finotello, F.; Vara-Perez, M.; Dewaele, M., De Witte, P.A.; Alexopoulos, L.; Janssens, S.; Sinkkonen, L.; Sauter, T.; Verhelst, S. H. L., Agostinis, P. (2021) The IRE1 inhibitor …<\/span> Continue reading →<\/span><\/a><\/p>\n","protected":false},"author":1,"featured_media":36,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"_links":{"self":[{"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/pages\/9"}],"collection":[{"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/comments?post=9"}],"version-history":[{"count":51,"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/pages\/9\/revisions"}],"predecessor-version":[{"id":538,"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/pages\/9\/revisions\/538"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/media\/36"}],"wp:attachment":[{"href":"https:\/\/www.verhelstlab.net\/wp-json\/wp\/v2\/media?parent=9"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}