Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Nina, Voevodskaya"'
Autor:
Michael Haumann, Nina Voevodskaya, Astrid Gräslund, Kajsa G. V. Havelius, Ana Popović-Bijelić, Petko Chernev, Nils Leidel
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(3):430-444
Ribonucleotide reductases (RNRs) are essential for DNA synthesis in most organisms. In class-Ic RNR from Chlamydia trachomatis (Ct), a MnFe cofactor in subunit R2 forms the site required for enzyme activity, instead of an FeFe cofactor plus a redox-a
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804:2198-2206
In mammals, the pyrimidines uracil and thymine are metabolised by a three-step reductive degradation pathway. Dihydropyrimidine dehydrogenase (DPD) catalyses its first and rate-limiting step, reducing uracil and thymine to the corresponding 5,6-dihyd
Autor:
Ute Jungwirth, Thomas Szekeres, Walter Berger, Daniele Biglino, Michael A. Jakupec, Michael Micksche, Petra Heffeter, L. Elbling, P. Saiko, R. Dornetshuber, Ana Popović-Bijelić, Astrid Gräslund, Bernhard K. Keppler, Nina Voevodskaya
Publikováno v:
Current Cancer Drug Targets. 9:595-607
KP772 is a new lanthanum complex containing three 1,10-phenathroline molecules. Recently, we have demonstrated that the promising in vitro and in vivo anticancer properties of KP772 are based on p53-independent G(0)G(1) arrest and apoptosis induction
Autor:
Astrid Gräslund, Nina Voevodskaya, Oliver Sanganas, Alexander Grundmeier, Michael Haumann, Friedhelm Lendzian
Publikováno v:
Journal of Biological Chemistry. 284:4555-4566
The R2 protein of class I ribonucleotide reductase (RNR) from Chlamydia trachomatis (Ct) can contain a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which i
Publikováno v:
Journal of Biological Chemistry. 277:43608-43614
The alternative oxidase (AOX) is a ubiquinol oxidase found in the mitochondrial respiratory chain of plants as well as some fungi and protists. It has been predicted to contain a coupled diiron center on the basis of a conserved sequence motif consis
Autor:
Astrid Gräslund, Pelle Håkansson, Nina Voevodskaya, Lars Thelander, Hirofumi Arakawa, Olivier Guittet, Susan Fridd, Yusuke Nakamura
Publikováno v:
Journal of Biological Chemistry. 276:40647-40651
Recently, a homologue of the small subunit of mammalian ribonucleotide reductase (RNR) was discovered, called p53R2. Unlike the well characterized S phase-specific RNR R2 protein, the new form was induced in response to DNA damage by the p53 protein.
Publikováno v:
Biochemistry. 48(27)
Class Ic ribonucleotide reductase (RNR) from Chlamydia trachomatis (C. tm.) lacks the tyrosyl radical and uses a Mn(IV)-Fe(III) cluster for cysteinyl radical initiation in the large subunit. Here we investigated and compared the metal content and spe
Autor:
Nina, Voevodskaya, Friedhelm, Lendzian, Oliver, Sanganas, Alexander, Grundmeier, Astrid, Gräslund, Michael, Haumann
Publikováno v:
The Journal of biological chemistry. 284(7)
The R2 protein of class I ribonucleotide reductase (RNR) from Chlamydia trachomatis (Ct) can contain a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which i
Autor:
Susanne Gräslund, Astrid Gräslund, Martin Hammarström, Ann-Gerd Thorsell, Robert D. Busam, B. Martin Hallberg, Nina Voevodskaya, Camilla Persson
Publikováno v:
The Journal of biological chemistry. 283(22)
Altered inositol metabolism is implicated in a number of diabetic complications. The first committed step in mammalian inositol catabolism is performed by myo-inositol oxygenase (MIOX), which catalyzes a unique four-electron dioxygen-dependent ring c
Publikováno v:
FEBS letters. 581(18)
Ribonucleotide reductase (class I) contains two components: protein R1 binds the substrate, and protein R2 normally has a diferric site and a tyrosyl free radical needed for catalysis. In Chlamydia trachomatis RNR, protein R2 functions without radica