Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Eva Maria Dürr"'
Autor:
Eva-Maria Dürr, Joanna F. McGouran
Publikováno v:
Molecules, Vol 26, Iss 2, p 320 (2021)
SNM1A is a nuclease that is implicated in DNA interstrand crosslink repair and, as such, its inhibition is of interest for overcoming resistance to chemotherapeutic crosslinking agents. However, the number and identity of the metal ion(s) in the acti
Externí odkaz:
https://doaj.org/article/5241643fdb134e38bc85fe821f66f33d
Autor:
Joanna F. McGouran, Eva-Maria Dürr
Publikováno v:
Molecules, Vol 26, Iss 320, p 320 (2021)
Molecules
Volume 26
Issue 2
Molecules
Volume 26
Issue 2
SNM1A is a nuclease that is implicated in DNA interstrand crosslink repair and, as such, its inhibition is of interest for overcoming resistance to chemotherapeutic crosslinking agents. However, the number and identity of the metal ion(s) in the acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1727c4ebeda68b3f7811cf02b49faee
https://www.mdpi.com/1420-3049/26/2/320
https://www.mdpi.com/1420-3049/26/2/320
Autor:
Eva-Maria Dürr, Joanna F. McGouran, William Doherty, Mark Berney, Manav T Manoj, Werner Theodor Jauslin
Publikováno v:
Bioorganic & Medicinal Chemistry
Graphical abstract
SNM1A is a zinc-dependent nuclease involved in the removal of interstrand crosslink lesions from DNA. Inhibition of interstrand crosslink repair enzymes such as SNM1A is a promising strategy for improving the efficacy of cross
SNM1A is a zinc-dependent nuclease involved in the removal of interstrand crosslink lesions from DNA. Inhibition of interstrand crosslink repair enzymes such as SNM1A is a promising strategy for improving the efficacy of cross
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f3ae6c9cf80859c7c4e1e9fb75d1503
https://doi.org/10.1016/j.bmc.2021.116369
https://doi.org/10.1016/j.bmc.2021.116369
Autor:
Joanna F. McGouran, Tom Brown, Sook Y. Lee, Eva-Maria Dürr, Arun Shivalingam, Peter J. McHugh, Afaf H. El-Sagheer, William Doherty
Publikováno v:
Chemistryselect
Phosphate groups are often crucial to biological activity and interactions of oligonucleotides, but confer poor membrane permeability. In addition, the group's lability to enzymatic hydrolysis is an obstacle to its use in therapeutics and in biologic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebe5aa5f3f45b01e186fc716f7e17335
http://ora.ox.ac.uk/objects/uuid:
http://ora.ox.ac.uk/objects/uuid:
Autor:
Gang Hu, Burkhard Göke, Georg J. Arnold, Frank T. Kolligs, Dagmar C. Kress, Sören T. Eichhorst, Sebastian Baehs, Eric R. Fearon, Claudia Jäger, Guido T. Bommer, Thomas Fröhlich, Thomas Brabletz, Eva Maria Dürr
Publikováno v:
Journal of Biological Chemistry. 280:7962-7975
Neoplastic progression in human tissues appears to be paralleled by a series of genetic and epigenetic alterations. In human colorectal cancers, defect Wnt/beta-catenin/T-cell factor and RAS/RAF signaling pathways have a major contributing role in tu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbabe0c8ba0a8bfa8a5ef5e1424a5624
https://doi.org/10.1074/jbc.m412593200
https://doi.org/10.1074/jbc.m412593200
Autor:
Barbara Rauch, Ralf-T. Hoffmann, Frank T. Kolligs, Maximilian F. Reiser, Eva-Maria Dürr, Thomas Helmberger, Christoph Trumm, Tobias F. Jakobs, Fabian Bamberg, Philipp M. Paprottka, Agnes Schön, Alexander Haug
Publikováno v:
Cardiovascular and interventional radiology. 35(1)
In unresectable intrahepatic cholangiocarcinoma (ICC), systemic chemotherapy often is viewed as the only option, although efficacy is limited. Radioembolization (RE) using yttrium-90 ((90)Y) microspheres is an accepted therapy for patients with hepat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcbe2fac477d5f287777d23e73983e5c
https://pubmed.ncbi.nlm.nih.gov/21431970
https://pubmed.ncbi.nlm.nih.gov/21431970
Autor:
Maja Köhn, Eva-Maria Dürr
Publikováno v:
ACS Central Science
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bdce592ad5202edd143521e7025f434