P Decottignies
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Explore the profile of P Decottignies including associated specialties, affiliations and a list of published articles.
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Articles
37
Citations
347
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Recent Articles
1.
Goyer A, Decottignies P, Miginiac-Maslow M
FEBS Lett
. 2001 Sep;
505(3):405-8.
PMID: 11576537
The activation pathway of the chloroplastic NADP-dependent malate dehydrogenase (MDH) by reduced thioredoxin has been examined using a method based on the mechanism of thiol/disulfide interchanges, i.e. the transient formation...
2.
Schepens I, Ruelland E, Miginiac-Maslow M, Le Marechal P, Decottignies P
J Biol Chem
. 2000 Aug;
275(46):35792-8.
PMID: 10958800
The activation of sorghum NADP-malate dehydrogenase is initiated by thiol/disulfide interchanges with reduced thioredoxin followed by the release of the C-terminal autoinhibitory extension and a structural modification shaping the active...
3.
Schepens I, Johansson K, Decottignies P, Gillibert M, Hirasawa M, Knaff D, et al.
J Biol Chem
. 2000 May;
275(28):20996-1001.
PMID: 10801830
The chloroplastic NADP-malate dehydrogenase is activated by reduction of its N- and C-terminal disulfides by reduced thioredoxin. The activation is inhibited by NADP(+), the oxidized form of the cofactor. Previous...
4.
Guittet O, Decottignies P, Serani L, Henry Y, Le Marechal P, Laprevote O, et al.
Biochemistry
. 2000 Apr;
39(16):4640-8.
PMID: 10769119
Ribonucleotide reductase activity is rate-limiting for DNA synthesis, and inhibition of this enzyme supports cytostatic antitumor effects of inducible NO synthase. The small R2 subunit of class I ribonucleotide reductases...
5.
Schepens I, Decottignies P, Ruelland E, Johansson K, Miginiac-Maslow M
FEBS Lett
. 2000 Apr;
471(2-3):240-4.
PMID: 10767431
During thioredoxin-mediated activation of chloroplastic NADP-malate dehydrogenase, a homodimeric enzyme, the interaction between subunits is known to be loosened but maintained. A modeling of the 3D structure of the protein...
6.
Goyer A, Decottignies P, Lemaire S, Ruelland E, Jacquot J, Miginiac-Maslow M
FEBS Lett
. 1999 Mar;
444(2-3):165-9.
PMID: 10050751
The role of the internal Cys-207 of sorghum NADP-malate dehydrogenase (NADP-MDH) in the activation of the enzyme has been investigated through the examination of the ability of this residue to...
7.
Ruelland E, Johansson K, Decottignies P, DJUKIC N, Miginiac-Maslow M
J Biol Chem
. 1998 Dec;
273(50):33482-8.
PMID: 9837927
The chloroplastic NADP malate dehydrogenase is completely inactive in its oxidized form and is activated by thiol/disulfide interchange with reduced thioredoxin. To elucidate the molecular mechanism underlying the absence of...
8.
de Lamotte-Guery F, Pruvost C, Minard P, Delsuc M, Miginiac-Maslow M, Schmitter J, et al.
Protein Eng
. 1998 May;
10(12):1425-32.
PMID: 9543004
Proline 40 in Escherichia coli thioredoxin is located close to the redox active site (Cys32-Cys35) within the alpha2 helix. The conservation of this residue among most of the thioredoxins suggests...
9.
Mikulasova D, Kollarova M, Miginiac-Maslow M, Decottignies P, Jacquot J, Kutejova E, et al.
FEMS Microbiol Lett
. 1998 Mar;
159(2):299-305.
PMID: 9503625
The malate dehydrogenase (MDH) from Streptomyces aureofaciens was purified to homogeneity and its physical and biochemical properties were studied. Its amino-terminal sequence perfectly matched the amino-terminal sequence of the MDH...
10.
Issakidis E, Lemaire M, Decottignies P, Jacquot J, Miginiac-Maslow M
FEBS Lett
. 1996 Aug;
392(2):121-4.
PMID: 8772188
Plant NADP-dependent malate dehydrogenase is activated through thiol/disulfide interchange with reduced thioredoxin. Previous studies showed that this process involves the reduction of two different disulfides per subunit: one N-terminal, the...