The DOI matches its Crossref record; 32 of the 33 references it cites were found in a registry or an index.
Structural and catalytic chemistry of magnesium-dependent enzymes
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
“Collectively, ribosomes and other negatively charged macromolecules and metabolites buffer free Mg2+ near 1 mM, with a range of ∼0.3 to 3 mM.5,8,71,72”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [71]
In the citing paper
“Although many Mg2+-dependent enzymes bind to ATP:Mg2+ (or other substrate:Mg2+ complexes), a subset form relatively stable associations with Mg2+ (Kd of 10–100 μM),71 and it is possible that some of this Mg2+ may be functionally sequestered.”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [71]
Citations
Cites
A general two-metal-ion mechanism for catalytic RNA
Steitz, T. A., & Steitz, J. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6498 · Cited by 1,171
Wilcox, D. E. (1996) · Chemical Reviews · doi:10.1021/cr950043b · Cited by 893
STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP
Pelletier, H., Sawaya, M. R., Kumar, A., Wilson, S. H., & Kraut, J. (1994) · Worldwide Protein Data Bank · doi:10.2210/pdb2bpf/pdb · Cited by 694
Structures of Ternary Complexes of Rat DNA Polymerase β, a DNA Template-Primer, and ddCTP
Pelletier, H., Sawaya, M. R., Kumar, A., Wilson, S. H., & Kraut, J. (1994) · Science · doi:10.1126/science.7516580 · Cited by 598
Schlichting, I., Almo, S. C., Rapp, G., Wilson, K. S., Petratos, K., Lentfer, A., Wittinghofer, A., Kabsch, W., PAI, E. F., Petsko, G. A., et al. (1990) · Nature · doi:10.1038/345309a0 · Cited by 487
Metal Activation of Enzymes in Nucleic Acid Biochemistry
Cowan, J. A. (1998) · Chemical Reviews · doi:10.1021/cr960436q · Cited by 405
Self-citationRecognition and Cleavage of DNA by Type‐II Restriction Endonucleases
Pingoud, A. M., & Jeltsch, A. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-6-00001.x · Cited by 330
Novel subunit—subunit interactions in the structure of glutamine synthetase
Almassy, R. J., Janson, C. A., Hamlin, R. C., Xuong, N., & Eisenberg, D. S. (1986) · Nature · doi:10.1038/323304a0 · Cited by 303
Inorganic Biochemistry, An Introduction
(1994) · Synthesis and Reactivity in Inorganic and Metal-Organic Chemistry · doi:10.1080/00945719408001397 · Cited by 231
The Biological chemistry of magnesium
(1995) · Choice Reviews Online · doi:10.5860/choice.33-0936 · Cited by 219
Cited by
Sorted by citations
Small-Molecule Two-Photon Probes for Bioimaging Applications
Kim, H. M., & Cho, B. R. (2015) · Chemical Reviews · doi:10.1021/cr5004425 · Cited by 1,047
Nucleases: diversity of structure, function and mechanism
Yang, W. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000181 · Cited by 692
Magnesium deficiency in plants: An urgent problem
Guo, W., Nazim, H., Liang, Z., & Yang, D. (2015) · The Crop Journal · doi:10.1016/j.cj.2015.11.003 · Cited by 605
Second messenger role for Mg2+ revealed by human T-cell immunodeficiency
Li, F.-Y., Chaigne-Delalande, B., Kanellopoulou, C., Davis, J. C., Matthews, H. F., Douek, D. C., Cohen, J. I., Uzel, G., Su, H. C., & Lenardo, M. J. (2011) · Nature · doi:10.1038/nature10246 · Cited by 579
Liu, S., Li, Z., Wang, C., Tao, W., Huang, M., Zuo, M., Yang, Y., Kang, Y., Zhang, L., Chen, S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14565-w · Cited by 438
Metadata
- Authors
- Cowan, J. A.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Cowan, J.A.
- ORCID
- Cowan, J.A.
- Venue
- Biometals
- Published
- 2002-09
- Volume
- 15
- Issue
- 3
- Pages
- 225-235
- ISSN
- 0966-0844 (ISSN-L)
- 1572-8773
- OpenAlex
- W1537110470
- Cited by
- 428
- References
- 33
- Citations by year
- 2026: 25 · 2025: 34 · 2024: 23 · 2023: 24 · 2022: 25 · 2021: 22 · 2020: 28 · 2019: 17 · 2018: 36 · 2017: 20 · 2016: 14 · 2015: 25 · 2014: 26 · 2013: 16 · 2012: 25
- FWCI
- 0.27
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- BioMetals (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- magnesium-dependent enzyme, enzyme structure, enzyme catalysis, metalloenzymes, magnesium ions, enzyme active site
- MeSH terms
- Catalysis, Enzymes, Magnesium, Nucleic Acids, Phosphorylation, Molecular Structure
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
