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of 158
pro vyhledávání: '"Jault, Jm"'
Members of the ATP-binding cassette (ABC) transporters share the same basic architecture, with a four-core domain made of two transmembrane plus two nucleotide-binding domains. However, a supramolecular organization has been detected in some ABC tran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::b831554251965fcdef489e98c31c24b5
https://hal.archives-ouvertes.fr/hal-00313596
https://hal.archives-ouvertes.fr/hal-00313596
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2002, 315, pp.1075-1085
Journal of Molecular Biology, Elsevier, 2002, 315, pp.1075-1085
International audience; YvcC, a multidrug transporter from Bacillus subtilis, is a member of the ATP-binding cassette superfamily, highly homologous to each half of human multidrug-resistance P-glycoprotein and to several other bacterial half-ABC tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::44b4ffb98c310322b98a910b2eb40886
https://hal.archives-ouvertes.fr/hal-00313616
https://hal.archives-ouvertes.fr/hal-00313616
Autor:
Oudot, C., Cortay, Jc, Blanchet, Christophe, Laporte, Dc, Dipietro, A., Cozzone, Aj, Jault, Jm
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2001, 40, pp.3047-3055
Biochemistry, American Chemical Society, 2001, 40, pp.3047-3055
International audience; The isocitrate dehydrogenase kinase/phosphatase (IDHK/P) of E. coli is a bifunctional enzyme responsible for the reversible phosphorylation of isocitrate dehydrogenase (IDH) on a seryl residue. As such, it belongs to the serin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::4286d94356e39b8aff68c9734206148f
https://hal.archives-ouvertes.fr/hal-00313203
https://hal.archives-ouvertes.fr/hal-00313203
The Pdr5p multidrug ABC ("ATP-binding cassette) transporter was highly overexpressed in plasma membranes from a yeast strain exhibiting both pdr1-3 gain-of-function mutation in the transcription factor-encoding gene PDR1 and disruption of genes encod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::725bb31bccfa510948b9459218019b8e
https://hal.archives-ouvertes.fr/hal-00313622
https://hal.archives-ouvertes.fr/hal-00313622
The rat elongation factor eEF-2 catalyzes the translocation step of protein synthesis. Besides its well-characterized GTP/GDP binding properties, we have previously shown that ATP and ADP bind to eEF-2 [Sontag, B., Reboud, A. M., Divita, G., Di Pietr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::5eea6940d5eefbd789e066f19318035e
https://hal.archives-ouvertes.fr/hal-00314215
https://hal.archives-ouvertes.fr/hal-00314215
Varying length cDNAs encoding the N-terminal nucleotide-binding domain (NBD1) from mouse mdr1 P-glyco- protein were prepared on the basis of structure predictions. Corresponding recombinant proteins were overexpressed in Escherichia coli, and the sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::cac748aba9bdf20a1a0a83051d8e184e
https://hal.archives-ouvertes.fr/hal-00313633
https://hal.archives-ouvertes.fr/hal-00313633
Schizosaccharomyces pombe yeast cells grown on either fermentable or respiratory media were efficiently converted to stable spheroplasts by the alpha-(1-->3)-glucanase Novozym 234 in the presence of 1.2 M sorbitol. Lysis of spheroplasts by gentle hom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::7ca47cdd31c697fdce50dccc26d3e06f
https://hal.archives-ouvertes.fr/hal-00313635
https://hal.archives-ouvertes.fr/hal-00313635
Chemical modification of mitochondrial F1-ATPase from Schizosaccharomyces pombe by the tryptophan-specific reagent N-bromosuccinimide (NBS) at pH 5.0 in the presence of 20% glycerol produced a characteristic lowering in both enzyme absorbance at 280
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::0ef6ffa1e845e2776fded14670f9e805
https://hal.archives-ouvertes.fr/hal-00313641
https://hal.archives-ouvertes.fr/hal-00313641
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