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The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein : tetrameric structure determined by cryo-electron microscopy. / Wulff, Ragna Peterson; Lundqvist, Joakim ; Rutsdottir, Gudrun; Hansson, Andreas; Stenbæk, Anne; Elmlund, Dominika; Elmlund, Hans; Jensen, Poul Erik; Hansson, Mats.
I:
Biochemistry, Bind 50, 2011, s. 3713-3723.
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
Wulff, RP, Lundqvist, J, Rutsdottir, G, Hansson, A, Stenbæk, A, Elmlund, D, Elmlund, H
, Jensen, PE & Hansson, M 2011, '
The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein: tetrameric structure determined by cryo-electron microscopy',
Biochemistry, bind 50, s. 3713-3723.
https://doi.org/10.1021/bi200058aAPA
Wulff, R. P., Lundqvist, J., Rutsdottir, G., Hansson, A., Stenbæk, A., Elmlund, D., Elmlund, H.
, Jensen, P. E., & Hansson, M. (2011).
The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein: tetrameric structure determined by cryo-electron microscopy.
Biochemistry,
50, 3713-3723.
https://doi.org/10.1021/bi200058aVancouver
Wulff RP, Lundqvist J, Rutsdottir G, Hansson A, Stenbæk A, Elmlund D o.a.
The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein: tetrameric structure determined by cryo-electron microscopy.
Biochemistry. 2011;50:3713-3723.
https://doi.org/10.1021/bi200058aAuthor
Wulff, Ragna Peterson ; Lundqvist, Joakim ; Rutsdottir, Gudrun ; Hansson, Andreas ; Stenbæk, Anne ; Elmlund, Dominika ; Elmlund, Hans ; Jensen, Poul Erik ; Hansson, Mats. / The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein : tetrameric structure determined by cryo-electron microscopy. I: Biochemistry. 2011 ; Bind 50. s. 3713-3723.
Bibtex
@article{abb5a93ac86c45c9970e7f2d1804ba4d,
title = "The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein: tetrameric structure determined by cryo-electron microscopy",
author = "Wulff, {Ragna Peterson} and Joakim Lundqvist and Gudrun Rutsdottir and Andreas Hansson and Anne Stenb{\ae}k and Dominika Elmlund and Hans Elmlund and Jensen, {Poul Erik} and Mats Hansson",
year = "2011",
doi = "10.1021/bi200058a",
language = "English",
volume = "50",
pages = "3713--3723",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
}
RIS
TY - JOUR
T1 - The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein
T2 - tetrameric structure determined by cryo-electron microscopy
AU - Wulff, Ragna Peterson
AU - Lundqvist, Joakim
AU - Rutsdottir, Gudrun
AU - Hansson, Andreas
AU - Stenbæk, Anne
AU - Elmlund, Dominika
AU - Elmlund, Hans
AU - Jensen, Poul Erik
AU - Hansson, Mats
PY - 2011
Y1 - 2011
U2 - 10.1021/bi200058a
DO - 10.1021/bi200058a
M3 - Journal article
C2 - 21456578
VL - 50
SP - 3713
EP - 3723
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
ER -
