ArticleThe Journal of biological chemistry2011
Dynamic ligand exchange in soluble guanylyl cyclase (sGC): implications for sGC regulation and desensitization.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed.
- A BODIPY-picolinium-cation conjugate as a blue-light-responsive caged group.RSC advances · 2023Article
- A heme pocket aromatic quadrupole modulates gas binding to cytochrome c'-β: Implications for NO sensors.The Journal of biological chemistry · 2023Article
- Cellular Factors That Shape the Activity or Function of Nitric Oxide-Stimulated Soluble Guanylyl Cyclase.Cells · 2023Review
- Inactivation of soluble guanylyl cyclase in living cells proceeds without loss of haem and involves heterodimer dissociation as a common step.British journal of pharmacology · 2022Article
- Soluble guanylyl cyclase: Molecular basis for ligand selectivity and actionFrontiers in molecular biosciences · 2022Review
- Activation mechanism of human soluble guanylate cyclase by stimulators and activators.Nature communications · 2021Article
- Higher susceptibility to heme oxidation and lower protein stability of the rare αBiochemical pharmacology · 2021Article
- A new paradigm for gaseous ligand selectivity of hemoproteins highlighted by soluble guanylate cyclase.Journal of inorganic biochemistry · 2021Review
- Structure and reactivity of chlorite dismutase nitrosyls.Journal of inorganic biochemistry · 2020Article
- Article
- Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their RegulationPhysiological reviews · 2019Review
- Regulation of nitric oxide signaling by formation of a distal receptor-ligand complex.Nature chemical biology · 2017Article
- Thrombospondins: A Role in Cardiovascular Disease.International journal of molecular sciences · 2017Review
- Engineering proximalChemical science · 2017Article
- Regulation of sGC via hsp90, Cellular Heme, sGC Agonists, and NO: New Pathways and Clinical Perspectives.Antioxidants & redox signaling · 2017Article
- The Role of Reactive Oxygen and Nitrogen Species in the Expression and Splicing of Nitric Oxide Receptor.Antioxidants & redox signaling · 2017Review
- Structure and Activation of Soluble Guanylyl Cyclase, the Nitric Oxide Sensor.Antioxidants & redox signaling · 2017Review
- Endothelium-dependent vasodilation effects ofExperimental and therapeutic medicine · 2016Article
- Can erythrocytes release biologically active NO?Cell communication and signaling : CCS · 2016Article
- S-nitrosothiols dilate the mesenteric artery more potently than the femoral artery by a cGMP and L-type calcium channel-dependent mechanism.Nitric oxide : biology and chemistry · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Accumulating evidence indicates that the functional properties of soluble guanylyl cyclase (sGC) are affected not only by the binding of NO but also by the NO:sGC ratio and a number of cellular factors, including GTP. In this study, we monitored the time-resolved transformations of sGC and sGC-NO complexes generated with stoichiometric or excess NO in the presence and absence of GTP. We demonstrate that the initial five-coordinate sGC-NO complex is highly activated by stoichiometric NO but is unstable and transforms into a five-coordinate sGC-2 state. This sGC-2 rebinds NO to form a low activity sGC-NO complex. The stability of the initial complex is greatly enhanced by GTP binding, binding of an additional NO molecule, or substitution of βHis-107. We propose that the transient nature of the sGC-NO complex, the formation of a desensitized sGC-2 state, and its transformation into a low activity sGC-NO adduct require βHis-107. We conclude that conformational changes leading to sGC desensitization may be prevented by GTP binding to the catalytic site or by binding of an additional NO molecule to the proximal side of the heme. The implications of these observations for cellular NO/cGMP signaling and the process of rapid desensitization of sGC are discussed in the context of the proposed model of sGC/NO interactions and dynamic transformations.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.