Zobrazeno 1 - 2
of 2
pro vyhledávání: '"MESH: Apolipoprotein E3"'
Autor:
Alexander D. Dergunov, Michel Desmadril, Vanessa Clément-Collin, Lawrence P. Aggerbeck, Gérard Siest, Anne Barbier, Masa Takahashi, Athanase Visvikis
Publikováno v:
Biophysical Chemistry
Biophysical Chemistry, Elsevier, 2006, 119 (2), pp.170-85. ⟨10.1016/j.bpc.2005.07.009⟩
Biophysical Chemistry, Elsevier, 2006, 119 (2), pp.170-85. ⟨10.1016/j.bpc.2005.07.009⟩
The stabilities toward thermal and chemical denaturation of three recombinant isoforms of human apolipoprotein E (r-apoE2, r-apoE3 and r-apoE4), human plasma apoE3, the recombinant amino-terminal (NT) and the carboxyl-terminal (CT) domains of plasma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e91810836e47c8412b3067f550d81cbd
https://hal.archives-ouvertes.fr/hal-00132154
https://hal.archives-ouvertes.fr/hal-00132154
The structure of human apolipoprotein E2, E3 and E4 in solution 1. Tertiary and quaternary structure
Autor:
Barbier, Anne, Clément-Collin, Vanessa, Dergunov, Alexander D, Visvikis, Athanase, Siest, Gérard, Aggerbeck, Lawrence P
Publikováno v:
Biophysical Chemistry
Biophysical Chemistry, Elsevier, 2006, 119 (2), pp.158-69. ⟨10.1016/j.bpc.2005.07.010⟩
Biophysical Chemistry, Elsevier, 2006, 119 (2), pp.158-69. ⟨10.1016/j.bpc.2005.07.010⟩
Three recombinant apoE isoforms fused with an amino-terminal extension of 43 amino acids were produced in a heterologous expression system in E. coli. Their state of association in aqueous phase was analyzed by size-exclusion liquid chromatography, s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::6442775930ddbfc81a0c6aeb333c0628
https://hal.archives-ouvertes.fr/hal-00131021
https://hal.archives-ouvertes.fr/hal-00131021