Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Stephanie A, Michaels"'
Autor:
Yuk-Ching Tse-Dinh, Yves Pommier, Arnaud Vanden Broeck, Shar-yin N. Huang, Andres Canela, Valérie Lamour, Brianna B. Mitchell, Nadim Majdalani, Stephanie A. Michaels
Publikováno v:
Science Advances
Science Advances, 2021, 7 (10), pp.eabe0384. ⟨10.1126/sciadv.abe0384⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2021, 7 (10), pp.eabe0384. ⟨10.1126/sciadv.abe0384⟩
Science Advances, 2021, 7 (10), pp.eabe0384. ⟨10.1126/sciadv.abe0384⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2021, 7 (10), pp.eabe0384. ⟨10.1126/sciadv.abe0384⟩
Exonuclease VII excises trapped DNA gyrase and provides a new strategy to overcome resistance to quinolones.
The widely used quinolone antibiotics act by trapping prokaryotic type IIA topoisomerases, resulting in irreversible topoisomerase cleav
The widely used quinolone antibiotics act by trapping prokaryotic type IIA topoisomerases, resulting in irreversible topoisomerase cleav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::259143a80dcf10f603b94d9d31f9c5e5
https://hal.science/hal-03345910/document
https://hal.science/hal-03345910/document
Autor:
Simone A Baechler, Antonella Spinazzola, Stephanie A. Michaels, Salim Khiati, Valentina M. Factor, L. M. Miller Jenkins, A. Ravji, Leonard M. Neckers, I. Dalla Rosa, Shar-yin N. Huang, Carole Sourbier, Yves Pommier, Hongzhi Zhang, Jens U. Marquardt, D. Becker, Martin Lang
Publikováno v:
Nature Communications
Nature Communications, Nature Publishing Group, 2019, 10, pp.83. ⟨10.1038/s41467-018-07922-3⟩
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Nature Communications, Nature Publishing Group, 2019, 10, pp.83. ⟨10.1038/s41467-018-07922-3⟩
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Mitochondrial topoisomerase IB (TOP1MT) is a nuclear-encoded topoisomerase, exclusively localized to mitochondria, which resolves topological stress generated during mtDNA replication and transcription. Here, we report that TOP1MT is overexpressed in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64c73dbf6e5c74905365abc44ca43524
https://hal.archives-ouvertes.fr/hal-02086952
https://hal.archives-ouvertes.fr/hal-02086952
Autor:
Ilaria Dalla Rosa, Stephanie A. Michaels, Keli Agama, Simone A Baechler, Lisa M. Miller Jenkins, Salim Khiati, Valentina M. Factor, Yves Pommier, Shar-yin N. Huang, Sae Rin Jean, David V. Tulumello, Sudhir Varma, Junko Murai, Shana O. Kelley
Publikováno v:
EMBO Reports
EMBO Reports, EMBO Press, 2018, 19 (3), pp.e42139. ⟨10.15252/embr.201642139⟩
EMBO Reports, EMBO Press, 2018, 19 (3), pp.e42139. ⟨10.15252/embr.201642139⟩
Tyrosyl-DNA phosphodiesterase 2 (TDP2) repairs abortive topoisomerase II cleavage complexes. Here, we identify a novel short isoform of TDP2 (TDP2S) expressed from an alternative transcription start site. TDP2S contains a mitochondrial targeting sequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c105ffa143075ed5117c15840bee30f9
https://doi.org/10.15252/embr.201642139
https://doi.org/10.15252/embr.201642139
Autor:
Shar-Yin N, Huang, Ilaria, Dalla Rosa, Stephanie A, Michaels, David V, Tulumello, Keli, Agama, Salim, Khiati, Sae Rin, Jean, Simone A, Baechler, Valentina M, Factor, Sudhir, Varma, Junko, Murai, Lisa M, Miller Jenkins, Shana O, Kelley, Yves, Pommier
Publikováno v:
EMBO reports. 19(3)
Tyrosyl‐DNA phosphodiesterase 2 (TDP2) repairs abortive topoisomerase II cleavage complexes. Here, we identify a novel short isoform of TDP2 (TDP2(S)) expressed from an alternative transcription start site. TDP2(S) contains a mitochondrial targetin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::504372758a7d105b21a54b3fa9a671ae
https://pubmed.ncbi.nlm.nih.gov/29438979
https://pubmed.ncbi.nlm.nih.gov/29438979
Publikováno v:
Clinical infectious diseases : an official publication of the Infectious Diseases Society of America. 29(2)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77b786890ca60422baa232e30c4d0666
https://pubmed.ncbi.nlm.nih.gov/10476778
https://pubmed.ncbi.nlm.nih.gov/10476778