HUGO ID Detailed Result 2294

PMID	Match String	Actual String	Score	Flanking text	Edited by	Edit
11679167	COX	COX	1.4	of anoxia on the expression of the nuclear aerobic genes COX indicated the existence of a signalling pathway from the mitochondria
12618129	COX	COX	1.2	(succinate_amp_#x2013;cytochrome succinate_amp_#x2013 cytochrome c reductase IV (cytochrome cytochrome c oxidase COX and the mitochondrial matrix enzyme citrate synthase (CS) CS were
12618129	COX	COX	1.2	For example in 143B-derived cybrids COX excess capacity is such that even a stop codon mutation
12618129	COX	COX	1.2	is such that even a stop codon mutation in a COX subunit can be tolerated up to 40% heteroplasmy before an
12618129	COX	COX	1.2	Accordingly 5 _amp_#x3bc M KCN a specific inhibitor of COX was added either at the beginning of the assay (
12618129	COX	COX	1.2	Because KCN competes with oxygen for the catalytic site on COX KCN inhibition increased to approximately 20% at O 2-50%RA
12618129	COX	COX	1.2	of the mitochondrial respiratory chain complexes I III II III COX and of the nuclear encoded mitochondrial matrix enzyme citrate synthase
12618129	COX	COX	1.2	DCFDA and incubated in medium containing increasing concentrations of the COX inhibitor KCN from 0 to 10 _amp_#x3bc M
12618129	COX	COX	1.2	NADH cytochrome c reductase II III succinate cytochrome c reductase COX cytochrome c oxidase
17496232	COX	COX	0.9	as resulting from its high-affinity binding to cytochrome oxidase (COX), COX the final electron acceptor ( 19
17496232	COX	COX	0.9	( 119 mtNOS is bound to mitochondrial PDZ domains of COX ( 57 103 and to complex I ( 57 thus
17496232	COX	COX	0.9	( 116 142 or from the reduction of nitrite by COX ( 39
17496232	COX	COX	0.9	( 25 NO reversibly binds to Cu B center of COX and consequently inhibits electron transfer to O 2 and mitochondrial
17496232	COX	COX	0.9	concentrations 50-100 nM NO inhibits by half the activity of COX ( 108 110
17496232	COX	COX	0.9	represents a simple competition between NO and O 2 for COX the formation of the complex between COX and NO was
17496232	COX	COX	0.9	O 2 for COX the formation of the complex between COX and NO was followed by the authors after addition of
17496232	COX	COX	0.9	The time scale for the inhibition of COX by NO is given by k NOon x NO at
17496232	COX	COX	0.9	Therefore the fast inhibition of COX by NO is completely compatible with a direct competition between
17496232	COX	COX	0.9	with a direct competition between NO and O 2 for COX at the steady state and in the presence of NO
17496232	COX	COX	0.9	Eq 2 which describes a simple linear competitive inhibition of COX by NO with an inhibition constant ( K i given
17496232	COX	COX	0.9	These calculations are useful for isolated COX although they should be modified to include additional NO effects
17496232	COX	COX	0.9	Accordingly NO inhibits COX and increases the reduction levels of the components of the
17496232	COX	COX	0.9	chain including ubiquinol and ubisemiquinone on the substrate side of COX and reacts directly with ubiquinol to produce nitroxyl anion (NO
17496232	COX	COX	0.9	and cyclin D In this sense very low NO inhibits COX and determines low H 2 O 2 yield