The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Soluble guanylate cyclase
Abstract
Soluble guanylate cyclase (sGC) is a mammalian nitric oxide (NO) sensor. When NO binds to the sGC heme, its GTP cyclase activity markedly increases, thus generating cyclic GMP, which serves to regulate several cell signaling functions. A good deal is known about the kinetics and equilibrium of binding of NO to sGC, leading to a proposed multistep mechanism of sGC activation that involves at least two NO-binding sites. The crystal structure of a member of a recently discovered family of prokaryotic sGC homologues has provided important insights into structure-function relationships within the sGC family of proteins.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The reaction is observed in the three NOS isoforms (750, 973, 1034).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [750]
In the citing paper
“Initial reports indicated that nNOS had the ability to produce superoxide in a reaction dependent on NADPH and Ca2+/CaM (750).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [750]
Citations
Cites
Arnold, W. P., Mittal, C. K., Katsuki, S., & Murad, F. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.8.3203 · Cited by 1,459
Crystal Structure of the Catalytic Domains of Adenylyl Cyclase in a Complex with G sα ·GTPγS
Tesmer, J. J. G., Sunahara, R. K., Gilman, A. G., & Sprang, S. R. (1997) · Science · doi:10.1126/science.278.5345.1907 · Cited by 792
A molecular basis for nitric oxide sensing by soluble guanylate cyclase
Zhao, Y., Brandish, P. E., Ballou, D. P., & Marletta, M. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14753 · Cited by 323
Myoglobin discriminates between O2, NO, and CO by electrostatic interactions with the bound ligand
Olson, J. S., & Phillips, G. N. (1997) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050169 · Cited by 288
Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases
Pellicena, P., Karow, D. S., Boon, E. M., Marletta, M. A., & Kuriyan, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405188101 · Cited by 271
NO activation of guanylyl cyclase
Russwurm, M., & Koesling, D. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600422 · Cited by 222
A molecular basis for NO selectivity in soluble guanylate cyclase
Boon, E. M., Huang, S. H., & Marletta, M. A. (2005) · Nature Chemical Biology · doi:10.1038/nchembio704 · Cited by 188
Karow, D. S., Pan, D., Tran, R., Pellicena, P., Presley, A. D., Mathies, R. A., & Marletta, M. A. (2004) · Biochemistry · doi:10.1021/bi049374l · Cited by 184
Femtomolar Sensitivity of a NO Sensor from Clostridium botulinum
Nioche, P., Berka, V., Vipond, J., Minton, N., Tsai, A., & Raman, C. (2004) · Science · doi:10.1126/science.1103596 · Cited by 179
Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase
Lawson, D. M., Stevenson, C. E. M., Andrew, C. R., & Eady, R. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5661 · Cited by 168
Cited by
Sorted by citations
Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways
Mishanina, T. V., Libiad, M., & Banerjee, R. V. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1834 · Cited by 612
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Understanding nitrate assimilation and its regulation in microalgae
Sanz‐Luque, E., Chamizo‐Ampudia, A., Llamas, Á., Galván, A., & Fernández, E. M. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00899 · Cited by 453
Kajimura, M., Fukuda, R., Bateman, R. M., Yamamoto, T., & Suematsu, M. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2657 · Cited by 271
Novel lead structures and activation mechanisms for CO ‐releasing molecules ( CORMs )
Schatzschneider, U. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12688 · Cited by 251
Metadata
- Authors
- Poulos, T. L.
- Affiliations
- University of California, Irvine (US)
- Corresponding author
- Poulos, Thomas L
- ORCID
- Poulos, Thomas L
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 16
- Issue
- 6
- Pages
- 736-743
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2074306377
- Cited by
- 129
- References
- 29
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 4 · 2023: 6 · 2022: 9 · 2020: 3 · 2019: 2 · 2018: 6 · 2017: 2 · 2016: 6 · 2015: 4 · 2014: 14 · 2013: 10 · 2012: 12
- FWCI
- 0.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- soluble guanylate cyclase, nitric oxide sensor, cyclic GMP, crystal structure, structure-function relationship, heme
- MeSH terms
- Animals, Enzyme Activation, Guanylate Cyclase, Heme, Kinetics, Ligands, Models, Molecular, Nitric Oxide, Prokaryotic Cells, Recombinant Proteins, Solubility, Signal Transduction, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
