Zobrazeno 1 - 10
of 61
pro vyhledávání: '"André P. M. Eker"'
Autor:
Inês Chaves, Romana M Nijman, Magdalena A Biernat, Monika I Bajek, Karl Brand, António Carvalho da Silva, Shoko Saito, Kazuhiro Yagita, André P M Eker, Gijsbertus T J van der Horst
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23447 (2011)
Despite the sequence and structural conservation between cryptochromes and photolyases, members of the cryptochrome/photolyase (flavo)protein family, their functions are divergent. Whereas photolyases are DNA repair enzymes that use visible light to
Externí odkaz:
https://doaj.org/article/50356ca7e06a4af5969a34790e6e64bd
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2011, 108 (23), pp.9402-9407. ⟨10.1073/pnas.1101026108⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108 (23), pp.9402-9407. ⟨10.1073/pnas.1101026108⟩
Proceedings of the National Academy of Sciences of the U.S.A., 108(23), 9402-9407. National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America, 2011, 108 (23), pp.9402-9407. ⟨10.1073/pnas.1101026108⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108 (23), pp.9402-9407. ⟨10.1073/pnas.1101026108⟩
Proceedings of the National Academy of Sciences of the U.S.A., 108(23), 9402-9407. National Academy of Sciences
CPD photolyase uses light to repair cyclobutane pyrimidine dimers (CPDs) formed between adjacent pyrimidines in UV-irradiated DNA. The enzyme harbors an FAD cofactor in fully reduced state (FADH - ). The CPD repair mechanism involves electron transfe
Publikováno v:
Journal of General Virology, 91(4), 907-914
Journal of General Virology, 91, 907-914. Microbiology Society
Journal of General Virology 91 (2010) 4
Journal of General Virology, 91, 907-914. Microbiology Society
Journal of General Virology 91 (2010) 4
Cyclobutane pyrimidine dimer (CPD) photolyases convert UV-induced CPDs in DNA into monomers using visible light as the energy source. Two phr genes encoding class II CPD photolyases PHR1 and PHR2 have been identified in Chrysodeixis chalcites nucleop
Autor:
André P. M. Eker, Klaus Brettel, Viruthachalam Thiagarajan, Martin Byrdin, Sandrine Villette, Agathe Espagne
Publikováno v:
Biochemistry, 49(2), 297-303. American Chemical Society
Biochemistry
Biochemistry, 2010, 49 (2), pp.297-303. ⟨10.1021/bi901562a⟩
Biochemistry, American Chemical Society, 2010, 49 (2), pp.297-303. ⟨10.1021/bi901562a⟩
Biochemistry
Biochemistry, 2010, 49 (2), pp.297-303. ⟨10.1021/bi901562a⟩
Biochemistry, American Chemical Society, 2010, 49 (2), pp.297-303. ⟨10.1021/bi901562a⟩
International audience; CPD photolyase enzymatically repairs the major UV-induced lesion in DNA, the cyclobutane pyrimidine dimer (CPD), by photoreversion of the damage reaction. An enzyme-bound reduced flavin (FADH(-)) cofactor functions its photose
Publikováno v:
DNA Repair 7 (2008) 8
DNA Repair, 7(8), 1309-1318
DNA Repair, 7(8), 1309-1318. Elsevier
DNA Repair, 7(8), 1309-1318
DNA Repair, 7(8), 1309-1318. Elsevier
The genome of Chrysodeixis chalcites nucleopolyhedrovirus (ChchNPV) contains two open reading frames, Cc-phrl and Cc-phr2, which encode putative class 11 CPD-DNA photolyases. CPD-photolyases repair UV-induced pyrimidine cyclobutane dimers using visib
Publikováno v:
Journal of Physical Chemistry B
Journal of Physical Chemistry B, American Chemical Society, 2008, 112, pp.6866-6871. ⟨10.1021/jp711435y⟩
Journal of Physical Chemistry B, 112(22), 6866-6871. American Chemical Society
Journal of Physical Chemistry B, 2008, 112, pp.6866-6871. ⟨10.1021/jp711435y⟩
Journal of Physical Chemistry B, American Chemical Society, 2008, 112, pp.6866-6871. ⟨10.1021/jp711435y⟩
Journal of Physical Chemistry B, 112(22), 6866-6871. American Chemical Society
Journal of Physical Chemistry B, 2008, 112, pp.6866-6871. ⟨10.1021/jp711435y⟩
International audience; Transient absorption spectroscopy is a powerful tool for studying biological electron-transfer chains, provided that their members give rise to distinct changes of their absorption spectra. There are, however, chains that cont
Autor:
Li Lan, Kazuo Yamamoto, André P. M. Eker, Akira Yasui, Satoshi Nakajima, Shin Ichiro Kanno, Masashi Takao
Publikováno v:
Journal of Biological Chemistry, 279, 46674-46677. American Society for Biochemistry and Molecular Biology Inc.
DNA damage can cause cell death unless it is either repaired or tolerated. The precise contributions of repair and tolerance mechanisms to cell survival have not been previously evaluated. Here we have analyzed the cell killing effect of the two majo
Autor:
Lars-Oliver Essen, Ulrich Hennecke, Petra Gnau, Tobias Klar, André P. M. Eker, Alexandra Mees, Thomas Carell
Publikováno v:
Science, 306, 1789-1793. American Association for the Advancement of Science
DNA photolyases use light energy to repair DNA that comprises ultraviolet-induced lesions such as the cis-syn cyclobutane pyrimidine dimers (CPDs). Here we report the crystal structure of a DNA photolyase bound to duplex DNA that is bent by 50° and
Autor:
Yvonne Rijksen, André P. M. Eker, Wouter Schul, Jan H.J. Hoeijmakers, Satoshi Nakajima, Akira Yasui, Jan de Wit, Judith Jans, Gijsbertus T. J. van der Horst, Kyra H.M. Klemann, Osamu Nikaido
Publikováno v:
EMBO Journal, 21(17), 4719-4729. Wiley-Blackwell
During evolution, placental mammals appear to have lost cyclobutane pyrimidine dimer (CPD) photolyase, an enzyme that efficiently removes UV-induced CPDs from DNA in a light-dependent manner. As a consequence, they have to rely solely on the more com
Publikováno v:
Nature, 405, 586-590. Nature Publishing Group
Nature
Nature, Nature Publishing Group, 2000, 405 (1 june), pp.586. ⟨10.1038/35014644⟩
Nature
Nature, Nature Publishing Group, 2000, 405 (1 june), pp.586. ⟨10.1038/35014644⟩
International audience; Amino-acid radicals play key roles in many enzymatic reactions. Catalysis often involves transfer of a radical character within the protein, as in class I ribonucleotide reductase where radical transfer occurs over 35 Å, from