751 related articles for article (PubMed ID: 39543)
1. NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation.
Takeshige K; Minakami S
Biochem J; 1979 Apr; 180(1):129-35. PubMed ID: 39543
[TBL] [Abstract][Full Text] [Related]
2. Pro- and anti-oxidant activities of the mitochondrial respiratory chain: factors influencing NAD(P)H-induced lipid peroxidation.
Glinn MA; Lee CP; Ernster L
Biochim Biophys Acta; 1997 Jan; 1318(1-2):246-54. PubMed ID: 9030267
[TBL] [Abstract][Full Text] [Related]
3. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria.
Turrens JF; Boveris A
Biochem J; 1980 Nov; 191(2):421-7. PubMed ID: 6263247
[TBL] [Abstract][Full Text] [Related]
4. Lipid peroxidation and the reduction of ADP-Fe3+ chelate by NADH-ubiquinone reductase preparation from bovine heart mitochondria.
Takeshige K; Takayanagi R; Minakami S
Biochem J; 1980 Dec; 192(3):861-6. PubMed ID: 6786284
[TBL] [Abstract][Full Text] [Related]
5. NADH- and NADPH-dependent lipid peroxidation in bovine heart submitochondrial particles. Dependence on the rate of electron flow in the respiratory chain and an antioxidant role of ubiquinol.
Takayanagi R; Takeshige K; Minakami S
Biochem J; 1980 Dec; 192(3):853-60. PubMed ID: 7236242
[TBL] [Abstract][Full Text] [Related]
6. Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase.
Kotlyar AB; Vinogradov AD
Biochim Biophys Acta; 1990 Aug; 1019(2):151-8. PubMed ID: 2119805
[TBL] [Abstract][Full Text] [Related]
7. Generation of superoxide by the mitochondrial Complex I.
Grivennikova VG; Vinogradov AD
Biochim Biophys Acta; 2006; 1757(5-6):553-61. PubMed ID: 16678117
[TBL] [Abstract][Full Text] [Related]
8. The pathway of electron transfer in NADH:Q oxidoreductase.
van Belzen R; Albracht SP
Biochim Biophys Acta; 1989 May; 974(3):311-20. PubMed ID: 2499359
[TBL] [Abstract][Full Text] [Related]
9. Kinetics of superoxide formation by respiratory chain NADH- dehydrogenase of bovine heart mitochondria.
Kang D; Narabayashi H; Sata T; Takeshige K
J Biochem; 1983 Oct; 94(4):1301-6. PubMed ID: 6317663
[TBL] [Abstract][Full Text] [Related]
10. Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A, and MPP+.
Ramsay RR; Singer TP
Biochem Biophys Res Commun; 1992 Nov; 189(1):47-52. PubMed ID: 1333196
[TBL] [Abstract][Full Text] [Related]
11. -->H+/2e- stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles.
Galkin AS; Grivennikova VG; Vinogradov AD
FEBS Lett; 1999 May; 451(2):157-61. PubMed ID: 10371157
[TBL] [Abstract][Full Text] [Related]
12. Comparison of the inhibitory action of natural rotenone and its stereoisomers with various NADH-ubiquinone reductases.
Ueno H; Miyoshi H; Ebisui K; Iwamura H
Eur J Biochem; 1994 Oct; 225(1):411-7. PubMed ID: 7925463
[TBL] [Abstract][Full Text] [Related]
13. The mechanism of oxidation of reduced nicotinamide dinucleotide phosphate by submitochondrial particles from beef heart.
Rydström J; Montelius J; Bäckström D; Ernster L
Biochim Biophys Acta; 1978 Mar; 501(3):370-80. PubMed ID: 24468
[TBL] [Abstract][Full Text] [Related]
14. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria.
Cadenas E; Boveris A; Ragan CI; Stoppani AO
Arch Biochem Biophys; 1977 Apr; 180(2):248-57. PubMed ID: 195520
[No Abstract] [Full Text] [Related]
15. Selective inhibition of mitochondrial NADH-ubiquinone reductase (Complex I) by an alkyl polyoxyethylene ether.
Suzuki H; Wakai M; Ozawa T
Biochem Int; 1986 Aug; 13(2):351-7. PubMed ID: 3094534
[TBL] [Abstract][Full Text] [Related]
16. Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone.
De Jong AM; Albracht SP
Eur J Biochem; 1994 Jun; 222(3):975-82. PubMed ID: 8026508
[TBL] [Abstract][Full Text] [Related]
17. 1-Methyl-4-phenylpyridinium (MPP+) induces NADH-dependent superoxide formation and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles.
Hasegawa E; Takeshige K; Oishi T; Murai Y; Minakami S
Biochem Biophys Res Commun; 1990 Aug; 170(3):1049-55. PubMed ID: 2167668
[TBL] [Abstract][Full Text] [Related]
18. Coupling site I and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles.
Kotlyar AB; Sled VD; Burbaev DS; Moroz IA; Vinogradov AD
FEBS Lett; 1990 May; 264(1):17-20. PubMed ID: 2159893
[TBL] [Abstract][Full Text] [Related]
19. The locus of inhibition of NADH oxidation by benzothiadiazoles in beef heart submitochondrial particles.
Ferreira J; Wilkinson C; Gil L
Biochem Int; 1986 Mar; 12(3):447-59. PubMed ID: 3707593
[TBL] [Abstract][Full Text] [Related]
20. Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. I. Pre-steady-state kinetics with NADPH.
Bakker PT; Albracht SP
Biochim Biophys Acta; 1986 Jul; 850(3):413-22. PubMed ID: 3015206
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]