Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Matthieu J. Caron"'
Autor:
Donna M. Gordon, Paula D. Green, Matthieu J. Caron, Aurelio Reyes, Janine H. Santos, Nilesh Kumar Sharma, Marcelo G. Bonini, Ian J. Holt
Publikováno v:
Nucleic Acids Research
Human telomerase reverse transcriptase (hTERT) is localized to mitochondria, as well as the nucleus, but details about its biology and function in the organelle remain largely unknown. Here we show, using multiple approaches, that mammalian TERT is m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bedceecaddd2e5369217ba265e9e548
https://doi.org/10.1093/nar/gkr758
https://doi.org/10.1093/nar/gkr758
Autor:
John T. Lis, Amanda Mei, Katie L. Zobeck, Thomas Kusch, M. Behfar Ardehali, Matthieu J. Caron
Publikováno v:
The EMBO Journal. 30:2817-2828
Histone H3 lysine 4 trimethylation (H3K4me3) is a major hallmark of promoter-proximal histones at transcribed genes. Here, we report that a previously uncharacterized Drosophila H3K4 methyltransferase, dSet1, and not the other putative histone H3K4 m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d328278e71e5691cac98905c20460224
https://doi.org/10.1038/emboj.2011.194
https://doi.org/10.1038/emboj.2011.194
Autor:
Utz Herbig, Janine H. Santos, Marcelo G. Bonini, Perihan Ulema, Matthieu J. Caron, Olga A. Kovalenko, Masayuki Kimura, Carolina Medrano, Andrew P. Thomas
Publikováno v:
Aging Cell. 9:203-219
Telomerase is a reverse transcriptase specialized in telomere synthesis. The enzyme is primarily nuclear where it elongates telomeres, but many reports show that the catalytic component of telomerase (in humans called hTERT) also localizes outside of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c6bbf2337d12c557eb35607eea720a2
https://doi.org/10.1111/j.1474-9726.2010.00551.x
https://doi.org/10.1111/j.1474-9726.2010.00551.x
Autor:
Matthieu J. Caron, Marie-France Giraud, Jean-Paul di Rago, Jean Velours, Stéphane Duvezin-Caubet
Publikováno v:
Proceedings of the National Academy of Sciences. 100:13235-13240
The mitochondrial ATP synthase is made of a membrane-integrated F 0 component that forms a proton-permeable pore through the inner membrane and a globular peripheral F 1 domain where ATP is synthesized. The catalytic mechanism is thought to involve t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f12acfd437ae3c418e719653685b8a5a
https://doi.org/10.1073/pnas.2135169100
https://doi.org/10.1073/pnas.2135169100