Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases.
Pius S Padayatti, Priyaranjan Pattanaik, Xiaolei Ma, Focco van den Akker. Pharmacol Ther 2004
Times Cited: 41
Times Cited: 41
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Structure, regulation, and function of mammalian membrane guanylyl cyclase receptors, with a focus on guanylyl cyclase-A.
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19
Expression and characterization of the catalytic domains of soluble guanylate cyclase: interaction with the heme domain.
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The protein kinase domain of the ANP receptor is required for signaling.
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Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins.
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A receptor guanylyl cyclase expressed specifically in olfactory sensory neurons.
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Chronic inhibition of cyclic GMP phosphodiesterase 5A prevents and reverses cardiac hypertrophy.
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The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme.
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Structure of the adenylyl cyclase catalytic core.
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Femtomolar sensitivity of a NO sensor from Clostridium botulinum.
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Phosphorylation of the kinase homology domain is essential for activation of the A-type natriuretic peptide receptor.
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NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism.
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Structural and functional characterization of the dimerization region of soluble guanylyl cyclase.
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Crystal structure of the guanylyl cyclase Cya2.
Annika Rauch, Martina Leipelt, Michael Russwurm, Clemens Steegborn. Proc Natl Acad Sci U S A 2008
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Mechanisms of ligand discrimination by heme proteins.
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Agonistic induction of a covalent dimer in a mutant of natriuretic peptide receptor-A documents a juxtamembrane interaction that accompanies receptor activation.
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Ligand binding-dependent limited proteolysis of the atrial natriuretic peptide receptor: juxtamembrane hinge structure essential for transmembrane signal transduction.
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Nitric oxide regulates cardiac Ca2+ current. Involvement of cGMP-inhibited and cGMP-stimulated phosphodiesterases through guanylyl cyclase activation.
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Functional characterization of nitric oxide and YC-1 activation of soluble guanylyl cyclase: structural implication for the YC-1 binding site?
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.