Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Paul J. A. Michiels"'
SALMON: solvent accessibility, ligand binding, and mapping of ligand orientation by NMR spectroscopy
Autor:
Paul J. A. Michiels, Kathryn L. Kavanagh, Christian Ludwig, Udo Oppermann, Ulrich L. Günther, Anna Jansson, Ewa S. Pilka, Xiaoqiu Wu
Quinone oxidoreductase 2 (NQO2) binds the prodrug tretazicar (also known as CB1954, 5-(aziridin-1-yl)-2,4-dinitrobenzamide), which exhibits a profound antitumor effect in human cancers when administered together with caricotamide. X-ray structure det
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d1e539118980438f1f9e1d430e07d96
https://doi.org/10.1021/jm701020f
https://doi.org/10.1021/jm701020f
Autor:
Oliver Kayser, Herman J. Woerdenbag, Annie van Dam, Herald G. Aantjes, Oktavia Hendrawati, Paul J. A. Michiels
Publikováno v:
Phytochemistry, 72(17), 2172-2179. PERGAMON-ELSEVIER SCIENCE LTD
The aryltetralin lignan deoxypodophyllotoxin is much more widespread in the plant kingdom than podophyllotoxin. The latter serves as a starting compound for the production of cytostatic drugs like etoposide. A better insight into the occurrence of de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13261392d84ba38a8bde8153f62a8272
https://doi.org/10.1016/j.phytochem.2011.08.009
https://doi.org/10.1016/j.phytochem.2011.08.009
Autor:
Maria J.P. van Dongen, Christian Ludwig, Paul J. A. Michiels, Ulrich L. Günther, Sara B.-M. Whittaker, Karen Atkins
Publikováno v:
Biomolecular NMR Assignments. 4:101-105
The orphan nuclear receptor Nurr1 has been implicated in a number of conditions including Parkinson's disease and Schizophrenia. As such, it is of interest to study its interactions with other proteins, possibly mediated by small molecules, consideri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58f170eae22c59052951ca1b34f501d5
https://doi.org/10.1007/s12104-010-9210-4
https://doi.org/10.1007/s12104-010-9210-4
Autor:
Josef Messinger, Ulrich L. Günther, Christian Ludwig, Jerzy Adamski, Maria J.P. van Dongen, Hubert Thole, Gabriele Möller, Michel Stephan, Christina Fischer, Paul J. A. Michiels
Publikováno v:
The Journal of Steroid Biochemistry and Molecular Biology. 117:93-98
The enzyme 17beta-hydroxysteroid dehydrogenase type 1 (17beta-HSD1) has become an important drug target for breast cancer because it catalyzes the interconversion of estrone to the biologically more potent estradiol which also plays a crucial role in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0553528e6084b6351d8f4e7c61e707b5
https://doi.org/10.1016/j.jsbmb.2009.07.004
https://doi.org/10.1016/j.jsbmb.2009.07.004
Autor:
Christian Ludwig, Brian Schaffhausen, Tao Jiang, Sara B.-M. Whittaker, Konstantin Knoblich, Paul J. A. Michiels, Ulrich L. Günther
Publikováno v:
Biomolecular NMR Assignments. 3:119-123
Polyoma Large T antigen (PyLT) is a viral oncoprotein that targets cell proteins important for growth regulation. PyLT has two functional domains. Here we report (1)H, (15)N, (13)C backbone and (13)C beta assignments of 76% of the residues of the pol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eff8598f7bd743b41cc80f0502d28934
https://doi.org/10.1007/s12104-009-9155-7
https://doi.org/10.1007/s12104-009-9155-7
Publikováno v:
Drug Discovery Today: Technologies, 8(7), 297-306. Elsevier
Historically, pharmaceutical industries have focussed on the discovery of compounds that target the protein products of genes. The intermediary product between gene and protein, consisting of RNA, has remained largely unexplored. Several drugs target
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0262bc8424fd00c313378064eae58e31
https://doi.org/10.1016/S1359-6446(03)02624-2
https://doi.org/10.1016/S1359-6446(03)02624-2
Autor:
Hans A. Heus, Cornelis W. A. Pleij, Cornelis W. Hilbers, Paul W.G. Verlaan, Alexandra A M Versleijen, Paul J. A. Michiels
Publikováno v:
Journal of Molecular Biology. 310:1109-1123
RNA pseudoknots play important roles in many biological processes. In the simian retrovirus type-1 (SRV-1) a pseudoknot together with a heptanucleotide slippery sequence are responsible for programmed ribosomal frameshifting, a translational recoding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30da07545f8558196fe1098106c79752
https://doi.org/10.1006/jmbi.2001.4823
https://doi.org/10.1006/jmbi.2001.4823
Publikováno v:
RNA. 6:1821-1832
The cleavage site of the Neurospora VS RNA ribozyme is located in a separate hairpin domain containing a hexanucleotide internal loop with an A-C mismatch and two adjacent G-A mismatches. The solution structure of the internal loop and helix la of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d48ec3b43f01882fd8459f13ea8eb800
https://doi.org/10.1017/s1355838200001394
https://doi.org/10.1017/s1355838200001394
Publikováno v:
Biopolymers. 48:137-153
Recently, several high-resolution structures of-RNA pseudoknots have become available. Here we review the progress in this area. The majority of the structures obtained belong to the classical or H-type pseudoknot family. The most complicated pseudok
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e5bcbe6493cc76d001c3446eee20f61
https://doi.org/10.1002/(sici)1097-0282(1998)48:2<137::aid-bip4>3.0.co
https://doi.org/10.1002/(sici)1097-0282(1998)48:2<137::aid-bip4>3.0.co
Autor:
Paul J. A. Michiels, Jacques H. van Boom, Constant A. A. van Boeckel, Gijsbert A. van der Marel, Steven H. L. Verhelst
Publikováno v:
Chembiochem : a European journal of chemical biology. 5(7)
Aminoglycoside antibiotics, which are able to selectively bind to RNA, are considered to be an important lead in RNA-targeting drug discovery. In this study, surface plasmon resonance (SPR) was employed to explore the interaction of aminoglycosides w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::caf79eb066652259b81b3145d06ff7af
https://pubmed.ncbi.nlm.nih.gov/15239050
https://pubmed.ncbi.nlm.nih.gov/15239050