Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Chloé Leprêtre"'
Autor:
David Michael Mayes, Sarah Lopez, Chloé Leprêtre, Yohann Moreau, Christine Cavazza, Stéphane Ménage, Caroline Marchi-Delapierre, Serge Crouzy, Nicolai Burzlaff
Publikováno v:
ACS Catalysis
ACS Catalysis, American Chemical Society, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
ACS Catalysis, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
ACS Catalysis, American Chemical Society, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
ACS Catalysis, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
International audience; Artificial enzymes represent an attractive alternative to design abiotic biocatalysis. EcNikA-Rul, an artificial metalloenzyme developed by embedding a ruthenium-based catalyst into the cavity of the periplasmic nickel-binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1e7f4c47df4ae2f4817a1092dda188a
https://hal.archives-ouvertes.fr/hal-02865406
https://hal.archives-ouvertes.fr/hal-02865406
Autor:
Marc Fontecave, Christian Basset, Philippe Carpentier, Djemel Hamdane, Stéphane Torelli, Mohamed G. Atta, Chloé Leprêtre, Victor Duarte, Thierry Douki
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2020, 48 (17), pp.9918-9930. ⟨10.1093/nar/gkaa667⟩
Nucleic Acids Research, Oxford University Press, 2020, 48 (17), pp.9918-9930. ⟨10.1093/nar/gkaa667⟩
'Nucleic Acids Research ', vol: 48, pages: 9918-9930 (2020)
Nucleic Acids Research, 2020, 48 (17), pp.9918-9930. ⟨10.1093/nar/gkaa667⟩
Nucleic Acids Research, Oxford University Press, 2020, 48 (17), pp.9918-9930. ⟨10.1093/nar/gkaa667⟩
'Nucleic Acids Research ', vol: 48, pages: 9918-9930 (2020)
MiaE (2-methylthio-N6-isopentenyl-adenosine37-tRNA monooxygenase) is a unique non-heme diiron enzyme that catalyzes the O2-dependent post-transcriptional allylic hydroxylation of a hypermodified nucleotide 2-methylthio-N6-isopentenyl-adenosine (ms2i6
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abc30397d644239bc33d4cc013fba3cf
https://hal.science/hal-03065929/file/gkaa667.pdf
https://hal.science/hal-03065929/file/gkaa667.pdf
Publikováno v:
Biochemical Pharmacology. 76:1490-1502
The discovery of caspase activation counts as one of the most important finds in the biochemistry of apoptosis. However, targeted disruption of caspases does not impair every type of apoptosis. Other proteases can replace caspases and several so call
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36e104f2e4096e760601ac82852372db
https://doi.org/10.1016/j.bcp.2008.07.039
https://doi.org/10.1016/j.bcp.2008.07.039
Publikováno v:
Apoptosis : an international journal on programmed cell death. 18(9)
Programmed cell death is an important factor in tissue homeostasis. Lot of work has been performed to characterize the caspase-dependent cell death. Caspase-independent cell death, although important in many physiological situations, is less investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d473f6ace077a69bf37aca1ac2d0139c
https://pubmed.ncbi.nlm.nih.gov/23673989
https://pubmed.ncbi.nlm.nih.gov/23673989
Publikováno v:
Annals of the New York Academy of Sciences. 1171
Poly(ADP-ribose) polymerase-1 (PARP-1) uses NAD(+) as a substrate to form ADP-ribose. During apoptosis, caspases cleave PARP-1 to avoid excessive NAD consumption. Because PARP-1 is a key regulator of the activity of DNases involved in caspase-depende
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a062eb6946c3e8c0d2fb75e2f7ae23df
https://pubmed.ncbi.nlm.nih.gov/19723034
https://pubmed.ncbi.nlm.nih.gov/19723034
Publikováno v:
Molecular and Cellular Biology
Molecular and Cellular Biology, 2007, pp.10.1128. ⟨10.1128/MCB.01959-06⟩
Molecular and Cellular Biology, American Society for Microbiology, 2007, pp.10.1128. ⟨10.1128/MCB.01959-06⟩
Molecular and Cellular Biology, 2007, pp.10.1128. ⟨10.1128/MCB.01959-06⟩
Molecular and Cellular Biology, American Society for Microbiology, 2007, pp.10.1128. ⟨10.1128/MCB.01959-06⟩
The best-characterized biochemical feature of apoptosis is degradation of genomic DNA into oligonucleosomes. The endonuclease responsible for DNA degradation in caspase-dependent apoptosis is caspase-activated DNase. In caspase-independent apoptosis,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aad6188ac7e97362cf4c30b8dab1699c
https://www.hal.inserm.fr/inserm-00140748
https://www.hal.inserm.fr/inserm-00140748
Autor:
Alicia Torriglia, Chloé Leprêtre
Publikováno v:
Frontiers in Bioscience. 14:4836
Caspase activation has been seen, for several years, as the biochemical marker of apoptosis. However, in 2005 the Nomenclature Committee on Cell Death (NCCD) established that the 'official' classification of cell death had to rely on morphological cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2b543e166f4e4b8dfdfa56c80ea6e64
https://doi.org/10.2741/3572
https://doi.org/10.2741/3572
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. (10):1755-1766
LEI (Leukocyte Elastase Inhibitor), the precursor of the pro-apoptotic molecule L-DNase II, belongs to the ovalbumin subgroup of serpins. Several serpins can inhibit apoptosis: the viral serpin Crm A inhibits Fas or TNFα-induced apoptosis, and overe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14fc8e73b2c945146d9f6aad0ab38bac