Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Andrea J. Petschner"'
Autor:
Ljubomir Isakovic, Oscar M. Saavedra, David B. Llewellyn, Stephen Claridge, Lijie Zhan, Naomy Bernstein, Arkadii Vaisburg, Nadine Elowe, Andrea J. Petschner, Jubrail Rahil, Norman Beaulieu, France Gauthier, A. Robert MacLeod, Daniel Delorme, Jeffrey M. Besterman, Amal Wahhab
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:2742-2746
Potent SAH analogues with constrained homocysteine units have been designed and synthesized as inhibitors of human DNMT enzymes. The five membered (2S,4S)-4-mercaptopyrrolidine-2-carboxylic acid, in 1a, was a good replacement for homocysteine, while
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12b27b210b122378d7edc0e3a1d17925
https://doi.org/10.1016/j.bmcl.2009.03.132
https://doi.org/10.1016/j.bmcl.2009.03.132
SAR around (l)-S-adenosyl-l-homocysteine, an inhibitor of human DNA methyltransferase (DNMT) enzymes
Autor:
Stephen William Claridge, Daniel Delorme, Ljubomir Isakovic, David B. Llewellyn, Franck Raeppel, A. Robert MacLeod, Jeffrey M. Besterman, Amal Wahhab, Norman Beaulieu, Arkadii Vaisburg, Lijie Zhan, Jubrail Rahil, Oscar Mario Saavedra, Nadine Elowe, Naomy Bernstein, Andrea J. Petschner
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:2747-2751
The inhibitory activity of base-modified SAH analogues and the specificity of inhibiting human DNMT1 and DNMT3b2 enzymes was explored. The 6-amino group was essential while the 7-N of the adenine ring of SAH could be replaced by CH- without loss of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c33ea1411905c14a49c5e81eae5869a9
https://doi.org/10.1016/j.bmcl.2009.03.113
https://doi.org/10.1016/j.bmcl.2009.03.113
Autor:
Jeffrey M. Besterman, Amal Wahhab, Alain Ajamian, Martin Allan, Sylvain Lefebvre, Alina Nicolescu, Robert Deziel, Eric Therrien, Jacques Rodrigue, Sukhdev Manku, Jubrail Rahil, Andrea J. Petschner, Zuomei Li, Marielle Fournel, James Wang, Tim Guo, Natalie Nguyen
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:1866-1870
We have recently reported on a novel class of histone deacetylase (HDAC) inhibitors bearing a sulfamide group as the zinc-binding unit. Herein, we report on the synthesis of sulfamide based inhibitors designed around a lysine scaffold and their struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6abf3fd06e2b54e9501d6b7a35258c02
https://doi.org/10.1016/j.bmcl.2009.02.075
https://doi.org/10.1016/j.bmcl.2009.02.075
Autor:
A. Robert MacLeod, Robert Deziel, Eric Therrien, Anne-Christine Goulet, Sylvia Styhler, Sukhdev Manku, Gabi Rahil, Hannah Nguyen, Andrea J. Petschner, Martin Allan, Natalie Nguyen, Jeffrey M. Besterman, Amal Wahhab, Marie-France Robert
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(4)
A series of N-benzyl-1-heteroaryl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamides targeting co-activator associated arginine methyltransferase 1 (CARM1) have been designed and synthesized. The potency of these inhibitors was influenced by the nature o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9aca66baaf7a8d920ff206061fcb2062
https://pubmed.ncbi.nlm.nih.gov/19131248
https://pubmed.ncbi.nlm.nih.gov/19131248
Autor:
Zuomei Li, Alain Ajamian, Sukhdev Manku, Silvana Leit, Marielle Fournel, Martin Allan, Jeffrey M. Besterman, Yves Andre Chantigny, Amal Wahhab, Eric Therrien, Theresa P. Yan, Sylvain Lefebvre, Jubrail Rahil, Andrea J. Petschner, Alina Nicolescu, David Smil, Robert Deziel, Aihua Lu, Samuel Montcalm, Natalie Nguyen
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(2)
The sulfamide moiety has been utilized to design novel HDAC inhibitors. The potency and selectivity of these inhibitors were influenced both by the nature of the scaffold, and the capping group. Linear long-chain-based analogs were primarily HDAC6-se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fbc0dcec8fb6f78a60098b9b9bc504b
https://pubmed.ncbi.nlm.nih.gov/19084395
https://pubmed.ncbi.nlm.nih.gov/19084395