Concerted complex assembly and GTPase activation in the chloroplast signal recognition particle. Read more about Concerted complex assembly and GTPase activation in the chloroplast signal recognition particle.
Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft. Read more about Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft.
A novel intermediate in the reaction of seleno CYP119 with m-chloroperbenzoic acid. Read more about A novel intermediate in the reaction of seleno CYP119 with m-chloroperbenzoic acid.
Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosis. Read more about Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosis.
Heparan sulfate-dependent signaling of fibroblast growth factor 18 by chondrocyte-derived perlecan. Read more about Heparan sulfate-dependent signaling of fibroblast growth factor 18 by chondrocyte-derived perlecan.
Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase. Read more about Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.
Reengineering the signaling properties of a Src family kinase. Read more about Reengineering the signaling properties of a Src family kinase.
Isocyanides inhibit human heme oxygenases at the verdoheme stage. Read more about Isocyanides inhibit human heme oxygenases at the verdoheme stage.
DevS oxy complex stability identifies this heme protein as a gas sensor in Mycobacterium tuberculosis dormancy. Read more about DevS oxy complex stability identifies this heme protein as a gas sensor in Mycobacterium tuberculosis dormancy.
The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism. Read more about The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.
