ArticleNature chemical biology2017
Regulation of nitric oxide signaling by formation of a distal receptor-ligand complex.
Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Nitric Oxide Binding Geometry in Heme-Proteins: Relevance for Signal Transduction.Antioxidants (Basel, Switzerland) · 2024Review
- Metalloprotein enabled redox signal transduction in microbes.Current opinion in chemical biology · 2023Review
- The Mechanism of Biochemical NO-Sensing: Insights from Computational Chemistry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Structural Perspectives on the Mechanism of Soluble Guanylate Cyclase Activation.International journal of molecular sciences · 2021Review
- A new paradigm for gaseous ligand selectivity of hemoproteins highlighted by soluble guanylate cyclase.Journal of inorganic biochemistry · 2021Review
- Article
- Structure/function of the soluble guanylyl cyclase catalytic domain.Nitric oxide : biology and chemistry · 2018Review
- Physiological activation and deactivation of soluble guanylate cyclase.Nitric oxide : biology and chemistry · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The binding of nitric oxide (NO) to the heme cofactor of heme-nitric oxide/oxygen binding (H-NOX) proteins can lead to the dissociation of the heme-ligating histidine residue and yield a five-coordinate nitrosyl complex, an important step for NO-dependent signaling. In the five-coordinate nitrosyl complex, NO can reside on either the distal or proximal side of the heme, which could have a profound influence over the lifetime of the in vivo signal. To investigate this central molecular question, we characterized the Shewanella oneidensis H-NOX (So H-NOX)-NO complex biophysically under limiting and excess NO conditions. The results show that So H-NOX preferably forms a distal NO species with both limiting and excess NO. Therefore, signal strength and complex lifetime in vivo will be dictated by the dissociation rate of NO from the distal complex and the rebinding of the histidine ligand to the heme.
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What OpenQuestion holds
Registered trials
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.