Matches in Nanopublications for { ?s ?p "where CO takes over the roles of NO under conditions of oxidative stress (Maines, 1997). Therefore, HO activity is important in controlling the activity of heme proteins, such as cytochromes P450, COX, guanylyl cyclase, and NOS, not only at the level of the intracellular heme pool available for the apo-heme proteins (Kappas and Drummond, 1986) but possibly also at the level of HO's downstream effector molecule CO by interactions with the heme group (Haider et al., 2002). " ?g. }
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- _6 value "where CO takes over the roles of NO under conditions of oxidative stress (Maines, 1997). Therefore, HO activity is important in controlling the activity of heme proteins, such as cytochromes P450, COX, guanylyl cyclase, and NOS, not only at the level of the intracellular heme pool available for the apo-heme proteins (Kappas and Drummond, 1986) but possibly also at the level of HO's downstream effector molecule CO by interactions with the heme group (Haider et al., 2002). " provenance.
- _6 value "where CO takes over the roles of NO under conditions of oxidative stress (Maines, 1997). Therefore, HO activity is important in controlling the activity of heme proteins, such as cytochromes P450, COX, guanylyl cyclase, and NOS, not only at the level of the intracellular heme pool available for the apo-heme proteins (Kappas and Drummond, 1986) but possibly also at the level of HO's downstream effector molecule CO by interactions with the heme group (Haider et al., 2002). " provenance.
- _6 value "where CO takes over the roles of NO under conditions of oxidative stress (Maines, 1997). Therefore, HO activity is important in controlling the activity of heme proteins, such as cytochromes P450, COX, guanylyl cyclase, and NOS, not only at the level of the intracellular heme pool available for the apo-heme proteins (Kappas and Drummond, 1986) but possibly also at the level of HO's downstream effector molecule CO by interactions with the heme group (Haider et al., 2002). " provenance.
- _6 value "where CO takes over the roles of NO under conditions of oxidative stress (Maines, 1997). Therefore, HO activity is important in controlling the activity of heme proteins, such as cytochromes P450, COX, guanylyl cyclase, and NOS, not only at the level of the intracellular heme pool available for the apo-heme proteins (Kappas and Drummond, 1986) but possibly also at the level of HO's downstream effector molecule CO by interactions with the heme group (Haider et al., 2002). " provenance.