253 related articles for article (PubMed ID: 6786284)
1. 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]
2. 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]
3. 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]
4. 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]
5. 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]
6. 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]
7. Lipid peroxidation and changes in the ubiquinone content and the respiratory chain enzymes of submitochondrial particles.
Forsmark-Andrée P; Lee CP; Dallner G; Ernster L
Free Radic Biol Med; 1997; 22(3):391-400. PubMed ID: 8981030
[TBL] [Abstract][Full Text] [Related]
8. Alteration of inner-membrane components and damage to electron-transfer activities of bovine heart submitochondrial particles induced by NADPH-dependent lipid peroxidation.
Narabayashi H; Takeshige K; Minakami S
Biochem J; 1982 Jan; 202(1):97-105. PubMed ID: 7082319
[TBL] [Abstract][Full Text] [Related]
9. Inhibition of NADH-ubiquinone reductase activity by N,N'-dicyclohexylcarbodiimide and correlation of this inhibition with the occurrence of energy-coupling site 1 in various organisms.
Yagi T
Biochemistry; 1987 May; 26(10):2822-8. PubMed ID: 3111526
[TBL] [Abstract][Full Text] [Related]
10. Further observations on the inhibition of NADH oxidase by short chain ubiquinone homologs.
Pasquali P; Landi L; Cabrini L; Sechi AM; Lenaz G
Boll Soc Ital Biol Sper; 1982 May; 58(10):585-90. PubMed ID: 6810905
[No Abstract] [Full Text] [Related]
11. On the mechanism of rotenone-insensitive reduction of quinones by mitochondrial NADH:ubiquinone reductase. The high affinity binding of NAD+ and NADH to the reduced enzyme form.
Cénas NK; Bironaité DA; Kulys JJ
FEBS Lett; 1991 Jun; 284(2):192-4. PubMed ID: 1905649
[TBL] [Abstract][Full Text] [Related]
12. The role of phospholipids in the reduction of ubiquinone analogues by the mitochondrial reduced nicotinamide-adenine dinucleotide-ubiquinone oxidoreductase complex.
Ragan CI
Biochem J; 1978 Jun; 172(3):539-47. PubMed ID: 210762
[TBL] [Abstract][Full Text] [Related]
13. Comparison of cumene hydroperoxide- and NADPH/Fe3+/ADP-induced lipid peroxidation in heart and liver submitochondrial particles. Mechanisms of protection by succinate.
Cavallini L; Valente M; Bindoli A
Biochim Biophys Acta; 1984 Oct; 795(3):466-72. PubMed ID: 6089907
[TBL] [Abstract][Full Text] [Related]
14. Succinate-dependent lipid peroxidation and its prevention by reduced ubiquinone in beef heart submitochondrial particles.
Eto Y; Kang D; Hasegawa E; Takeshige K; Minakami S
Arch Biochem Biophys; 1992 May; 295(1):101-6. PubMed ID: 1575504
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. 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]
17. Kinetic indication for multiple sites of ubiquinol-1 interaction in ubiquinol-cytochrome c reductase in bovine heart mitochondria.
Esposti MD; Lenaz G
Arch Biochem Biophys; 1982 Jul; 216(2):727-35. PubMed ID: 6287942
[No Abstract] [Full Text] [Related]
18. 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]
19. The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Evidence for stoicheiometric association.
Ragan CI; Heron C
Biochem J; 1978 Sep; 174(3):783-90. PubMed ID: 215122
[TBL] [Abstract][Full Text] [Related]
20. Kinetics of ubiquinol-1-cytochrome c reductase in bovine heart mitochondria and submitochondrial particles.
Degli Esposti M; Lenaz G
Biochim Biophys Acta; 1982 Nov; 682(2):189-200. PubMed ID: 6293557
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
