ReviewMolecular and cellular biochemistry2010
Atrial natriuretic factor-receptor guanylate cyclase signal transduction mechanism.
Review in Molecular and cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Effects of cGMP/Akt/GSK-3β signaling pathway on atrial natriuretic peptide secretion in rabbits with rapid atrial pacing.Frontiers in physiology · 2022Article
- Neprilysin: A Potential Therapeutic Target of Arterial Hypertension?Current cardiology reviews · 2020Review
- Synthesis, secretion, function, metabolism and application of natriuretic peptides in heart failure.Journal of biological engineering · 2018Review
- Ca(2+) modulation of ANF-RGC: new signaling paradigm interlocked with blood pressure regulation.Biochemistry · 2012Article
- A novel bioassay for the activity determination of therapeutic human brain natriuretic peptide (BNP).PloS one · 2012Article
- Allosteric modification, the primary ATP activation mechanism of atrial natriuretic factor receptor guanylate cyclase.Biochemistry · 2011Article
- Article
- ATP allosteric activation of atrial natriuretic factor receptor guanylate cyclase.The FEBS journal · 2010Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Atrial natriuretic factor (ANF) receptor guanylate cyclase (ANF-RGC), like the other members of the membrane guanylate cyclase family, is a single transmembrane-spanning protein. The transmembrane domain separates the protein into two regions, extracellular and intracellular. The extracellular region contains the ANF-binding domain and the intracellular region the catalytic domain located at the C-terminus of the protein. Preceding the catalytic domain, the intracellular region is comprised of the following functional domains: juxtaposed 40 amino acids to the transmembrane domain is the ATP-regulated module (ARM) domain [also termed the kinase homology domain (KHD)], and the putative dimerization domain. The ANF-RGC signaling is initiated by hormone, ANF, binding to its extracellular binding site. The binding signal is transduced through the transmembrane domain to the intracellular portion where ATP binding to the ARM domain partially activates the cyclase and prepares it for subsequent steps involving phosphorylation and attaining the fully activated state. This chapter reviews the signaling modules of ANF-RGC.
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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.