Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Danny C. Lenstra"'
Autor:
Michael Martin, Danny C. Lenstra, Elmar Weinhold, Jasmin Mecinović, Qingxi Meng, Ping Qian, Abbas H. K. Al Temimi, Hong Guo
Publikováno v:
ChemBioChem
Al Temimi, A H K, Martin, M, Meng, Q, Lenstra, D C, Qian, P, Guo, H, Weinhold, E & Mecinovic, J 2020, ' Lysine Ethylation by Histone Lysine Methyltransferases ', ChemBioChem, vol. 21, no. 3, pp. 392-400 . https://doi.org/10.1002/cbic.201900359
ChemBioChem : a European journal of chemical biology 21(3), 392-400 (2020). doi:10.1002/cbic.201900359
Chembiochem
Al Temimi, A H K, Martin, M, Meng, Q, Lenstra, D C, Qian, P, Guo, H, Weinhold, E & Mecinovic, J 2020, ' Lysine Ethylation by Histone Lysine Methyltransferases ', ChemBioChem, vol. 21, no. 3, pp. 392-400 . https://doi.org/10.1002/cbic.201900359
ChemBioChem : a European journal of chemical biology 21(3), 392-400 (2020). doi:10.1002/cbic.201900359
Chembiochem
Biomedicinally important histone lysine methyltransferases (KMTs) catalyze the transfer of a methyl group from S‐adenosylmethionine (AdoMet) cosubstrate to lysine residues in histones and other proteins. Herein, experimental and computational inves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4125d646555f925f56e6b06eab521be3
https://doi.org/10.1002/cbic.201900359
https://doi.org/10.1002/cbic.201900359
Autor:
Christoph Schächtele, Jan E. Ehlert, Ruben Gerardus George Leenders, Daniel Müller, Daniel Feger, Danny C. Lenstra, Jasmin Mecinović, Federica Trivarelli, Remco Zijlmans, Gerhard Müller, Bart van Bree, Anita Wegert, Marc van de Sande, Eddy Damen, Carolin Heidemann-Dinger, Michael H.G. Kubbutat
Publikováno v:
Bioorganic & Medicinal Chemistry Letters, 29, 2516-2524
Bioorganic & Medicinal Chemistry Letters, 29, 17, pp. 2516-2524
Bioorganic & Medicinal Chemistry Letters, 29, 17, pp. 2516-2524
Detailed structure activity relationship of two series of quinazoline EHMT1/EHMT2 inhibitors (UNC0224 and UNC0638) have been elaborated. New and active alternatives are presented for the ubiquitous substitution patterns found in literature for the li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::371bee28b62d7f328781fc0bfa1f7d42
https://doi.org/10.1016/j.bmcl.2019.06.012
https://doi.org/10.1016/j.bmcl.2019.06.012
Publikováno v:
Bioorganic & Medicinal Chemistry Letters, 28, 1234-1238
Bioorganic & Medicinal Chemistry Letters, 28, 7, pp. 1234-1238
Bioorganic & Medicinal Chemistry Letters, 28, 7, pp. 1234-1238
Histone lysine methyltransferases G9a and GLP are validated targets for the development of new epigenetic drugs. Most, if not all, inhibitors of G9a and GLP target the histone substrate binding site or/and the S-adenosylmethionine cosubstrate binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac8982a652b1d572b0839515bda197b7
https://hdl.handle.net/https://repository.ubn.ru.nl/handle/2066/190197
https://hdl.handle.net/https://repository.ubn.ru.nl/handle/2066/190197
Publikováno v:
Green Chemistry, 20, 4418-4422
Green Chemistry, 20, 19, pp. 4418-4422
Green Chemistry, 20, 19, pp. 4418-4422
A highly efficient and sustainable catalytic Staudinger reduction for the conversion of organic azides to amines in excellent yields has been developed. The reaction displays excellent functional group tolerance to functionalities that are otherwise
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6551399bd3e134dceb145c6f09f1d5dc
https://doi.org/10.1039/c8gc02136h
https://doi.org/10.1039/c8gc02136h
Autor:
Richard H. Blaauw, Arthur J. Altunc, Jasmin Mecinović, Anita Wegert, Giordano Proietti, Danny C. Lenstra, Abbas H. K. Al Temimi, Yali Wang, Hong Guo, Ping Qian, Paul B. White, Helene I. V. Amatdjais-Groenen, Ruben S. Teeuwen, Vu Uyen Tran, Wansheng Ren
Publikováno v:
Temimi, A H K A, Tran, V, Teeuwen, R S, Altunc, A J, Amatdjais-Groenen, H I V, White, P B, Lenstra, D C, Proietti, G, Wang, Y, Wegert, A, Blaauw, R H, Qian, P, Ren, W, Guo, H & Mecinović, J 2020, ' Examining sterically demanding lysine analogs for histone lysine methyltransferase catalysis ', Scientific Reports, vol. 10, 3671 . https://doi.org/10.1038/s41598-020-60337-3
Scientific Reports, 10, 1-11
Scientific Reports
Scientific Reports, 10, 1, pp. 1-11
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Scientific Reports, 10, 1-11
Scientific Reports
Scientific Reports, 10, 1, pp. 1-11
Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Methylation of lysine residues in histone proteins is catalyzed by S-adenosylmethionine (SAM)-dependent histone lysine methyltransferases (KMTs), a genuinely important class of epigenetic enzymes of biomedical interest. Here we report synthetic, mass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01f96f16f756f157284a26be88463219
https://findresearcher.sdu.dk:8443/ws/files/169051680/s41598_020_60337_3.pdf
https://findresearcher.sdu.dk:8443/ws/files/169051680/s41598_020_60337_3.pdf
Publikováno v:
Journal of Organic Chemistry, 84, 10, pp. 6536-6545
Lenstra, D C, Wolf, J J & Mecinović, J 2019, ' Catalytic Staudinger Reduction at Room Temperature ', The Journal of Organic Chemistry, vol. 84, no. 10, pp. 6536-6545 . https://doi.org/10.1021/acs.joc.9b00831
Journal of Organic Chemistry, 84, 6536-6545
Lenstra, D C, Wolf, J J & Mecinović, J 2019, ' Catalytic Staudinger Reduction at Room Temperature ', The Journal of Organic Chemistry, vol. 84, no. 10, pp. 6536-6545 . https://doi.org/10.1021/acs.joc.9b00831
Journal of Organic Chemistry, 84, 6536-6545
We report an efficient catalytic Staudinger reduction at room temperature that enables the preparation of a structurally diverse set of amines from azides in excellent yields. The reaction is based on the use of catalytic amounts of triphenylphosphin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80435b5cca36f83b1a5f4c076a626cbf
https://hdl.handle.net/2066/203982
https://hdl.handle.net/2066/203982
Autor:
Danny C. Lenstra, Jasmin Mecinović, Arthur J. Altunc, Wansheng Ren, Ruben S. Teeuwen, Abbas H. K. Al Temimi, Ping Qian, Vu Uyen Tran, Hong Guo
Publikováno v:
Organic & Biomolecular Chemistry, 17, 5693-5697
Temimi, A H K A, Teeuwen, R S, Tran, V, Altunc, A J, Lenstra, D C, Ren, W, Qian, P, Guo, H & Mecinović, J 2019, ' Importance of the main chain of lysine for histone lysine methyltransferase catalysis ', Organic & Biomolecular Chemistry, vol. 17, no. 23, pp. 5693-5697 . https://doi.org/10.1039/C9OB01038F
Organic & Biomolecular Chemistry, 17, 23, pp. 5693-5697
Temimi, A H K A, Teeuwen, R S, Tran, V, Altunc, A J, Lenstra, D C, Ren, W, Qian, P, Guo, H & Mecinović, J 2019, ' Importance of the main chain of lysine for histone lysine methyltransferase catalysis ', Organic & Biomolecular Chemistry, vol. 17, no. 23, pp. 5693-5697 . https://doi.org/10.1039/C9OB01038F
Organic & Biomolecular Chemistry, 17, 23, pp. 5693-5697
Histone lysine methyltransferases (KMTs) are biomedicinally important class of epigenetic enzymes that catalyse methylation of lysine residues in histones and other proteins. Enzymatic and computational studies on the simplest lysine analogues that p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63ce3f7ba477b9b97251c67bc2117093
http://hdl.handle.net/2066/206079
http://hdl.handle.net/2066/206079
Autor:
Hanka Venselaar, Jasmin Mecinović, Frank H. T. Nelissen, Yali Wang, Abbas H. K. Al Temimi, Y. Vijayendar Reddy, Danny C. Lenstra
Publikováno v:
Biochemical Journal, 476, 1109-1119
Wang, Y, Reddy, Y V, Al Temimi, A H K, Venselaar, H, Nelissen, F H T, Lenstra, D C & Mecinović, J 2019, ' Investigating the active site of human trimethyllysine hydroxylase ', The Biochemical journal, vol. 476, no. 7, pp. 1109-1119 . https://doi.org/10.1042/BCJ20180857
Biochemical Journal, 476, pp. 1109-1119
Wang, Y, Reddy, Y V, Al Temimi, A H K, Venselaar, H, Nelissen, F H T, Lenstra, D C & Mecinović, J 2019, ' Investigating the active site of human trimethyllysine hydroxylase ', The Biochemical journal, vol. 476, no. 7, pp. 1109-1119 . https://doi.org/10.1042/BCJ20180857
Biochemical Journal, 476, pp. 1109-1119
The biologically important carnitine biosynthesis pathway in humans proceeds via four enzymatic steps. The first step in carnitine biosynthesis is catalyzed by trimethyllysine hydroxylase (TMLH), a non-heme Fe(II) and 2-oxoglutarate (2OG)-dependent o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5cd812430655ad52a07c7cf40e14b8f
https://pubmed.ncbi.nlm.nih.gov/30898847
https://pubmed.ncbi.nlm.nih.gov/30898847
Publikováno v:
Tetrahedron, 71, 5547-5553
Tetrahedron, 71, 34, pp. 5547-5553
Tetrahedron, 71, 34, pp. 5547-5553
Development of catalytic amide bond formation reactions from readily available starting materials remains a challenging task for modern organic chemistry. Herein, we report that unactivated carboxylic esters and amines react in the presence of 10 mol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c140f725ae522af824c17ec0d67a9d2d
https://doi.org/10.1016/j.tet.2015.06.066
https://doi.org/10.1016/j.tet.2015.06.066
Autor:
Danny C. Lenstra, Ruben Gerardus George Leenders, Jasmin Mecinović, Richard H. Blaauw, Anita Wegert, Eddy Damen, Floris P. J. T. Rutjes
Publikováno v:
Chemmedchem, 13, 14, pp. 1405-1413
Chemmedchem, 13, 1405-1413
Chemmedchem, 13, 1405-1413
SETD7 is a histone H3K4 lysine methyltransferase involved in human gene regulation. Aberrant expression of SETD7 has been associated with various diseases, including cancer. Therefore, SETD7 is considered a good target for the development of new epig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ad6207eb960f60220fdb327ae3daa2c
https://doi.org/10.1002/cmdc.201800242
https://doi.org/10.1002/cmdc.201800242