Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Zuzana Valnickova-Hansen"'
Autor:
Zuzana Valnickova-Hansen, Russell P. Bowler, Line R. Thomsen, Carsten Scavenius, Ebbe Toftgaard Poulsen, Jane S. Petersen, Steen V. Petersen, Tim D. Oury, Jan J. Enghild
Publikováno v:
Scavenius, C, Petersen, J S, Thomsen, L R, Poulsen, E T, Valnickova Hansen, Z, Bowler, R D, Oury, T D, Petersen, S V & Enghild, J J 2013, ' Murine Extracellular Superoxide Dismutase Is Converted into the Inactive Fold by the Ser195Cys Mutation. ', Biochemistry, vol. 52, no. 19, pp. 3369-3375 . https://doi.org/10.1021/bi400171b
We have previously shown that human extracellular superoxide dismutase (EC-SOD) exists as two variants with differences in their disulfide bridge patterns: one form is the active enzyme (aEC-SOD), and the other is inactive (iEC-SOD). The availability
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5623ab94c9ef8802fb11875e62656f9
https://doi.org/10.1021/bi400171b
https://doi.org/10.1021/bi400171b
Autor:
Katelyn F. Leahy, Zuzana Valnickova-Hansen, John M. Hartney, Carsten Scavenius, Richard K.P. Benninger, Jan J. Enghild, Fabienne Gally, Rebecca E. Oberley-Deegan, Michael R. Weaver, Beata Kosmider, Richard J. Johnson, Timothy Stidham, Angela K. Zimmermann, Russell P. Bowler, Eva Nozik-Grayck, David A. Goldstrohm
Publikováno v:
Circulation: Cardiovascular Genetics
Circulation: Cardiovascular Genetics, American Heart Association, 2014, 7 (5), pp.659-66. ⟨10.1161/CIRCGENETICS.113.000504⟩
Circulation: Cardiovascular Genetics, 2014, 7 (5), pp.659-66. ⟨10.1161/CIRCGENETICS.113.000504⟩
Circulation: Cardiovascular Genetics, American Heart Association, 2014, 7 (5), pp.659-66. ⟨10.1161/CIRCGENETICS.113.000504⟩
Circulation: Cardiovascular Genetics, 2014, 7 (5), pp.659-66. ⟨10.1161/CIRCGENETICS.113.000504⟩
Background— The enzyme extracellular superoxide dismutase (EC-SOD; SOD3 ) is a major antioxidant defense in lung and vasculature. A nonsynonomous single-nucleotide polymorphism in EC-SOD (rs1799895) leads to an arginine to glycine amino acid substi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1426d13508b6b61d8f59d7654f89cb1
https://hal.archives-ouvertes.fr/hal-01112272
https://hal.archives-ouvertes.fr/hal-01112272
Autor:
Wojciech Paslawski, Tuomas P. J. Knowles, Alexander K. Buell, Maria Andreasen, Brian S. Vad, Søren B. Nielsen, Gunna Christiansen, Nikolai Lorenzen, Jørn Døvling Kaspersen, Zuzana Valnickova-Hansen, Daniel E. Otzen, Paolo Arosio, Jan J. Enghild, Jan Skov Pedersen, Christopher M. Dobson
Publikováno v:
Lorenzen, N, Nielsen, S B, Buell, A K, Kaspersen, J D, Arosio, P, Vad, B S, Paslawski, W, Christiansen, G, Valnickova Hansen, Z, Andreasen, M, Enghild, J J, Pedersen, J S, Dobson, C M, Knowles, T P J & Otzen, D 2014, ' The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation ', Journal of the American Chemical Society, vol. 136, no. 10, pp. 3859-3868 . https://doi.org/10.1021/ja411577t
Studies of proteins' formation of amyloid fibrils have revealed that potentially cytotoxic oligomers frequently accumulate during fibril formation. An important question in the context of mechanistic studies of this process is whether or not oligomer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9edf33b60fabcb5b087bdc90dada8c7
https://pubmed.ncbi.nlm.nih.gov/24527756
https://pubmed.ncbi.nlm.nih.gov/24527756