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Biochemical and Biophysical Research Communications|March 3, 2009
Role of substrate functional groups in binding to nitric oxide synthaseBaochen Fan, Dennis J Stuehr, Denis L RousseauJournal of the American Chemical Society|August 8, 2009
Characterization of the proximal ligand in the P420 form of inducible nitric oxide synthaseJoseph Sabat, Dennis J Stuehr, Syun-Ru Yeh, et al.The Journal of Biological Chemistry|April 7, 2004
Heme distortion modulated by ligand-protein interactions in inducible nitric-oxide synthaseDavid Li, Dennis J Stuehr, Syun-Ru Yeh, et al.Journal of the American Chemical Society|May 10, 2007
Substrate- and isoform-specific dioxygen complexes of nitric oxide synthaseDavid Li, Mariam Kabir, Dennis J Stuehr, et al.The Journal of Biological Chemistry|January 20, 2006
Regulation of the monomer-dimer equilibrium in inducible nitric-oxide synthase by nitric oxideDavid Li, Eric Y Hayden, Koustubh Panda, et al.The Journal of Biological Chemistry|December 28, 2012
Catalytic intermediates of inducible nitric-oxide synthase stabilized by the W188H mutationJoseph Sabat, Tsuyoshi Egawa, Changyuan Lu, et al.The Journal of Nutrition|October 7, 2004
Enzymes of the L-arginine to nitric oxide pathwayDennis J StuehrBritish Journal of Pharmacology|May 11, 2021
Inactivation of soluble guanylyl cyclase in living cells proceeds without loss of haem and involves heterodimer dissociation as a common stepYue Dai, Dennis J StuehrProceedings of the National Academy of Sciences of the United States of America|July 28, 2012
Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzymeArnab Ghosh, Dennis J StuehrMolecular Pharmacology|March 3, 2023
BAY58-2667 Activates Different Soluble Guanylyl Cyclase Species by Distinct Mechanisms that Indicate Its Principal Target in Cells is the Heme-Free Soluble Guanylyl Cyclase-Heat Shock Protein 90 ComplexYue Dai, Dennis J StuehrPageof 22