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
Flagged first, then by citations
1 of the 33 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 201–300 of 436
MAGT1-mediated disturbance of Mg2+ homeostasis lead to exhausted of HBV-infected NK and CD8+ T cells
Diao, B., Huang, X., Guo, S., Yang, C., Liu, G., Chen, Y., & Wu, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-11522-4 · Cited by 17
Maruyama, T., Imai, S., Kusakizako, T., Hattori, M., Ishitani, R., Nureki, O., Ito, K., Maturana, A. D., Shimada, I., & Osawa, M. (2018) · eLife · doi:10.7554/elife.31596 · Cited by 17
Roske, Y., Cappel, C. C., Cremer, N., Hoffmann, P., Koudelka, T., Tholey, A., Heinemann, U., Daumke, O., & Daμμe, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1114 · Cited by 17
Two-photon probes for biomedical imaging
Lim, C. S., & Cho, B. R. (2015) · Tetrahedron · doi:10.1016/j.tet.2015.06.083 · Cited by 17
Magnesium: The Neglected Electrolyte? A Clinical Review
Sharma, P., Chung, C., & Vizcaychipi, M. P. (2014) · Pharmacology & Pharmacy · doi:10.4236/pp.2014.57086 · Cited by 17
Hix, M. A., Leddin, E. M., & Cisneros, G. A. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.1c00313 · Cited by 17
Lu, S., Jiang, Y., Zou, J., & Wu, T. (2011) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp02498h · Cited by 17
Hu, P., Mo, Z., Chen, Y., Wu, Y., Song, L., Zhang, L., Li, Z., Fu, L., Liang, H., Tao, Y., et al. (2021) · Renal Failure · doi:10.1080/0886022x.2021.1960563 · Cited by 16
Etude diagnostique des technologies de transformation de la pomme de cajou en jus au Bénin
Dedehou, E., Dossou, J., & Soumanou, M. (2015) · International Journal of Biological and Chemical Sciences · doi:10.4314/ijbcs.v9i1.32 · Cited by 16
Bertiger, G., Jones, E. S., Dahdal, D. N., Marshall, D. C., & Joseph, R. E. (2015) · Clinical and Experimental Gastroenterology · doi:10.2147/ceg.s79216 · Cited by 16
The UK geochemical environment and cardiovascular diseases: magnesium in food and water
Davies, B. E. (2014) · Environmental Geochemistry and Health · doi:10.1007/s10653-014-9671-y · Cited by 16
Schmidt, M. A., Goodwin, T. J., & Pelligra, R. (2016) · Metabolomics · doi:10.1007/s11306-015-0942-0 · Cited by 16
Feng, G., Liu, C., Zeng, Z., Hou, G., Xu, H., & Zheng, W. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp02965a · Cited by 16
Rude, R. K. (2010) · CRC Press eBooks · doi:10.1201/b14669-63 · Cited by 16
Shiraz, M. F., Arif, Y., Imtiaz, H., Azam, A., Alam, P., & Hayat, S. (2025) · PROTOPLASMA · doi:10.1007/s00709-025-02060-2 · Cited by 15
Identification and functional analysis of the CorA/MGT/MRS2-type magnesium transporter in banana
Tong, M., Liu, W., He, H., Hu, H., Ding, Y., Xin-guo, L., Huang, J., & Yin, L. (2020) · PLoS ONE · doi:10.1371/journal.pone.0239058 · Cited by 15
Khayachi, A., Schorova, L., Alda, M., Rouleau, G. A., & Milnerwood, A. J. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.05.002 · Cited by 15
Wu, R., Meng, B., Corredig, M., & Griffiths, M. W. (2023) · Food and Environmental Virology · doi:10.1007/s12560-022-09548-7 · Cited by 15
Klatka, M., Grywalska, E., Partyka, M., Charytanowicz, M., & Roliński, J. (2013) · Biological Trace Element Research · doi:10.1007/s12011-013-9690-z · Cited by 15
Akutsu, M., Abe, N., Sakamoto, C., Kurimoto, Y., Sugita, H., Tanaka, M., Higuchi, Y., Sakamoto, K., Kamimura, N., Kurihara, H., et al. (2022) · Bioresource Technology · doi:10.1016/j.biortech.2022.127479 · Cited by 15
Contribution of Intramolecular NH···O Hydrogen Bonds to Magnesium–Carboxylate Bonds
Okamura, T., & Nakagawa, J. (2013) · Inorganic Chemistry · doi:10.1021/ic400671v · Cited by 15
Li, P., Liu, S., Wallerstein, J., Villones, R. L. E., Huang, P., Lindkvist‐Petersson, K., Meloni, G., Lu, K., Jensen, K. S., Liin, S. I., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01432-1 · Cited by 14
Dietary magnesium and copper affect survival time and neuroinflammation in chronic wasting disease
Nichols, T. A., Spraker, T. R., Gidlewski, T., Cummings, B. A., Hill, D., Kong, Q., Balachandran, A., VerCauteren, K. C., & Zabel, M. D. (2016) · Prion · doi:10.1080/19336896.2016.1181249 · Cited by 14
Khan, A. A. P., Bazan, G. C., Alhogbi, B. G., Marwani, H. M., Khan, A., Alam, M. M., Rahman, M. M., & Asiri, A. M. (2020) · Journal of Materials Research and Technology · doi:10.1016/j.jmrt.2020.06.052 · Cited by 14
Yang, Y., Li, X., Kan, B., He, H., Li, T., Ding, Y., Du, P., Lai, W., Hu, H., & Huang, J. (2021) · Planta · doi:10.1007/s00425-021-03769-z · Cited by 14
Effects of magnesium application on the arbuscular mycorrhizal symbiosis in tomato
Liu, J., Fang, L., Pei, W., Li, F., & Zhao, J. (2023) · Symbiosis · doi:10.1007/s13199-022-00862-z · Cited by 14
Hung, S. T., Roget, S. A., Zheng, W., & Fayer, M. D. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c00300 · Cited by 14
Ouattara, G. S., Soro, D., Chatigre, K. O., & Koffi, E. K. (2017) · International Journal of Biological and Chemical Sciences · doi:10.4314/ijbcs.v10i6.4 · Cited by 14
Tavasoli, S., Taheri, M., Taheri, F., Basiri, A., & Amiri, F. B. (2018) · International Urology and Nephrology · doi:10.1007/s11255-018-2036-1 · Cited by 14
Kodzhahinchev, V., Drago, K., & Bucking, C. (2017) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2017.01.016 · Cited by 14
Late-stage conversion of carboxylic acids to nitriles with Mg and Pd cocatalysis
Meng, J., Madhusudhanan, M. C., Wang, T., Cheng, Z., Zhao, B., Shi, H., Yang, L., Liu, P., & Jiao, N. (2025) · Nature Catalysis · doi:10.1038/s41929-025-01446-y · Cited by 13
Zang, J., Wang, T., Dziugan, P., Zhao, H., & Zhang, B. (2020) · Food Science & Nutrition · doi:10.1002/fsn3.2076 · Cited by 13
Hussain, A., Sajid, M., Potter, D., Rasheed, H., Hassan, M., Akhtar, N., Ahmad, B., & Bokhari, S. A. I. (2022) · Biological Trace Element Research · doi:10.1007/s12011-022-03469-z · Cited by 13
Corona-Martínez, D. O., Gómez-Tagle, P., & Yatsimirsky, A. K. (2012) · The Journal of Organic Chemistry · doi:10.1021/jo301649u · Cited by 13
Nuclease activity as a specific biomarker for breast cancer
Hernandez, L. I., Özalp, V. C., & Hernández, F. J. (2016) · Chemical Communications · doi:10.1039/c6cc07108b · Cited by 13
The role of calcium in plant signal transduction under macronutrient deficiency stress
Sharma, A., Shankhdhar, D., & Shankhdhar, S. C. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811308-0.00010-7 · Cited by 13
Kinetic characterization of Vibrio cholerae ApbE: Substrate specificity and regulatory mechanisms
Fang, X., Liang, P., Raba, D. A., Rosas‐Lemus, M., Chakravarthy, S., Tuz, K., & Juárez, O. X. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186805 · Cited by 13
Ab initio molecular dynamics studies of hydroxide coordination of alkaline earth metals and uranyl
Lynes, O., Austin, J. P., & Kerridge, A. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp00142e · Cited by 13
D’Egidio, S., Galieni, A., Stagnari, F., Pagnani, G., & Pisante, M. (2019) · Agronomy · doi:10.3390/agronomy9070379 · Cited by 13
Lee, K.-Y., Lee, K., Kim, J.-H., Lee, I.-G., Lee, S., Sim, D., Won, H., & Lee, B. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv348 · Cited by 13
Ellis, P. D., & Lipton, A. S. (2006) · Annual reports on NMR spectroscopy · doi:10.1016/s0066-4103(06)60001-x · Cited by 13
Xu, Y., Dong, C., Liu, X., Wei, D., Chen, Z., Zhou, H., Li, J., Yang, Y. P., & Tan, W. (2025) · Small · doi:10.1002/smll.202505750 · Cited by 12
Guo, X., Zhu, Y., Bai, L., & Yang, D. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.9b00508 · Cited by 12
Ion selectivity mechanism of the MgtE channel for Mg2+ over Ca2+
Teng, X., Sheng, D., Wang, J., Yu, Y., & Hattori, M. (2022) · iScience · doi:10.1016/j.isci.2022.105565 · Cited by 12
Maheswari, P. U., Renuga, D., Henry, L. J. K., & Kandasamy, R. (2018) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2018.01.025 · Cited by 12
Dynamics of soil metallic nutrients across a 6000-km temperature transect in China
Tan, Q., Chen, Y., Han, W., & Wang, G. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.140888 · Cited by 12
Loading rat heart myocytes with Mg2+ using low‐[Na+] solutions
Almulla, H. A., Bush, P. G., Steele, M., Ellis, D. H., & Flatman, P. W. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.109850 · Cited by 12
Ajilore, B. S., Alli, A. A., & Oluwadairo, T. O. (2018) · Pharmacology Research & Perspectives · doi:10.1002/prp2.401 · Cited by 12
Macromolecular crowding effects on transcription and translation are regulated by free magnesium ion
Ge, X., & Xu, J. (2019) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1827 · Cited by 12
Wang, Y., Wu, X., An, Y., Xie, H., Hao, F., & Tang, H. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00236 · Cited by 12
Feng, Z., Nagao, H., Li, B., Sotta, N., Shikanai, Y., Yamaguchi, K., Shigenobu, S., Kamiya, T., & Fujiwara, T. (2020) · PLANT PHYSIOLOGY · doi:10.1104/pp.20.00109 · Cited by 12
Ning, J., Chang, Y., Liu, W., Song, J., Zhang, W., & Ding, J. (2015) · Aquaculture · doi:10.1016/j.aquaculture.2015.06.035 · Cited by 11
Capillary electrophoresis-based assay of phosphofructokinase-1
Malina, A., Bryant, S. K., Chang, S. H., Waldrop, G. L., & Gilman, S. D. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.10.028 · Cited by 11
OMOTOSHO, O. E., Iheagwam, F. N., ADEBOLA, N. I., & Omini, J. J. (2018) · Current Research in Nutrition and Food Science Journal · doi:10.12944/crnfsj.6.3.23 · Cited by 11
Vasu, K., Matheshwaran, S., & Nagaraja, V. (2011) · ACS Chemical Biology · doi:10.1021/cb200107y · Cited by 11
Wu, X., Su, Y., Xu, Y., Hu, Q., Jiao, J., Ma, J., Liu, X., Sun, C., Guo, W. H., & Zhou, L. (2025) · ACS Sensors · doi:10.1021/acssensors.5c01021 · Cited by 10
Nugroho, A. D. W., van Olst, B., Bachtiar, S. A., Boeren, S. A., Kleerebezem, M., & Bachmann, H. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02708-21 · Cited by 10
Schweigel, M., Voigt, J., & Möhr, E. (2008) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/j.1439-0396.2007.00787.x · Cited by 10
Kavitha, S., Deepa, P., Karthika, M., & Kanakaraju, R. (2018) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2018.07.004 · Cited by 10
Dobrowsky, P. H., Khan, S., Cloete, T. E., & Khan, W. (2017) · Water Air & Soil Pollution · doi:10.1007/s11270-017-3270-3 · Cited by 10
Hasanah, Y., Mawarni, L., Hanum, H., Hanum, C., & Nasution, M. R. (2020) · IOP Conference Series Earth and Environmental Science · doi:10.1088/1755-1315/454/1/012158 · Cited by 10
Standard Gibbs energy of metabolic reactions: VI. Glyceraldehyde 3-phosphate dehydrogenase reaction
Greinert, T., Vogel, K., Mühlenweg, J.-K., Sadowski, G., Maskow, T., & Held, C. (2020) · Fluid Phase Equilibria · doi:10.1016/j.fluid.2020.112597 · Cited by 10
Role of Magnesium in the Regulation of Hepatic Glucose Homeostasis
Voma, C., & Romani, A. (2014) · InTech eBooks · doi:10.5772/57564 · Cited by 10
Kobayashi, N. I., Takagi, H., Yang, X., Nishizawa‐Yokoi, A., Segawa, T., Hoshina, T., Oonishi, T., Suzuki, H., Iwata, R., Toki, S., et al. (2023) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiad051 · Cited by 9
Endostatin and Cystatin C as Potential Biomarkers for Early Prediction of Preeclampsia
Alshannag, F., Zaki, R. M. M., Hemida, E. H. A., ElBakry, M. M. M., & Noureldeen, A. F. H. (2023) · ACS Omega · doi:10.1021/acsomega.3c05586 · Cited by 9
Raza, S., Sanober, G., Rungrotmongkol, T., & Azam, S. S. (2017) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2017.07.086 · Cited by 9
Effect of Kieserite on Physiological Characteristics of Soybean Varieties under Dryland Conditions
Hasanah, Y., Mawarni, L., Hanum, H., Sitepu, F. E., & Ardi, B. (2019) · Asian Journal of Plant Sciences · doi:10.3923/ajps.2020.21.25 · Cited by 9
Riemerella anatipestifer AS87_RS02955 Acts as a Virulence Factor and Displays Endonuclease Activity
Zhu, M., Chen, Z., Shen, R., Niu, P., Feng, Y., Liu, D., & Yu, S. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.01276-22 · Cited by 9
Bueren‐Calabuig, J. A., Coderch, C., Rico, E., Jiménez-Ruı́z, A., & Gago, F. (2011) · ChemBioChem · doi:10.1002/cbic.201100485 · Cited by 9
Ogrizek, M., Konc, J., Bren, U., Hodošček, M., & Janežič, D. (2016) · Chemistry Central Journal · doi:10.1186/s13065-016-0188-6 · Cited by 9
Ghorbanian, A. R., Khoshgoftarmanesh, A. H., & Zahedi, M. (2019) · Physiology and Molecular Biology of Plants · doi:10.1007/s12298-019-00695-z · Cited by 9
Effects of Cu on the corrosion behavior and microstructure of Mg–Zn–Ca bulk metallic glass
Xu, S., Hu, Y. M., Yang, W., & Liu, B. (2021) · Materials and Corrosion · doi:10.1002/maco.202112415 · Cited by 9
Garba, I. H., & Ubom, G. A. (2006) · Biological Trace Element Research · doi:10.1385/bter:114:1:115 · Cited by 9
Timuçin, E., & Sezerman, O. U. (2018) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00655 · Cited by 9
Jawla, J., & Chatli, M. K. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.103939 · Cited by 8
Kondratowicz-Maciejewska, K., Lemanowicz, J., & Jaskulska, I. (2025) · Sustainability · doi:10.3390/su17073252 · Cited by 8
Tan, Q., Li, J., Chen, Z., Ma, Y., Wang, G., Jia, Y., Yao, H., & Han, W. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.07.312 · Cited by 8
Ebuzoeme, C., Etim, I., Ikimi, A., Song, J., Du, T., Hu, M., Liang, D., & Gao, S. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13071043 · Cited by 8
Role of Polyamine-Induced Dimerization of Antizyme in Its Cellular Functions
Hyvönen, M. T., Smirnova, O. A., Mitkevich, V. A., Tunitskaya, V. L., Хомутов, М. А., Karpov, D. S., Korolev, S. P., Häkkinen, M. R., Pietilä, M., Gottikh, M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094614 · Cited by 8
da Costa, L. M., Ferreira, G. B., & Carneiro, J. W. D. M. (2013) · Journal of Molecular Modeling · doi:10.1007/s00894-013-1811-2 · Cited by 8
Mg(II) and Ca(II) Microsolvation by Ammonia: Born–Oppenheimer Molecular Dynamics Studies
León-Pimentel, C. I., Saint-Martín, H., & Ramírez-Solís, A. (2021) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.1c02815 · Cited by 8
Bukhvostov, A. A., Napolov, J. K., Buchachenko, A. L., & Kuznetsov, D. A. (2014) · British Journal of Pharmacology and Toxicology · doi:10.19026/bjpt.5.5414 · Cited by 8
Roy, A., & Cisneros, G. A. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c00435 · Cited by 7
Unveiling microbial diversity in slightly and moderately magnesium deficient acidic soils
Dash, M., Thiyageshwari, S., Selvi, D. T., Johnson, H. K. V., Ariyan, M., Rajan, K., & Anandham, R. (2025) · Scientific Reports · doi:10.1038/s41598-025-87943-3 · Cited by 7
Xie, S., Tian, S., Yang, J., Wang, N., Wan, Q., Wang, M., Liu, J., Zhou, J., Qi, P., Sui, K., et al. (2025) · Angewandte Chemie · doi:10.1002/ange.202424316 · Cited by 7
Akçay, M., Yazıcılar, B., Kassa, S. B., İlhan, D., Shadidizaji, A., & Bezırganoğlu, İ. (2025) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/s11240-025-03097-0 · Cited by 7
Functional dissection of magnesium nutrition and use efficiency in common bean
Youssef, I., & Krouma, A. (2020) · Agronomy Journal · doi:10.1002/agj2.20506 · Cited by 7
Relative Contributions of Base Stacking and Electrostatic Repulsion on DNA Nicks and Gaps
Harris, P. D., Hamdan, S. M., & Habuchi, S. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c06941 · Cited by 7
THE APPLICATION OF MG-L-ASPARAGINATE AND COMBINATIONS OF MG SALTS WITH VITAMIN B6 IN MEDICINE
Спасов, А. А., & Косолапов, В. А. (2017) · Russian Medicine · doi:10.18821/0869-2106-2017-23-2-89-95 · Cited by 7
Ando, I., Karasawa, K., Shioya, T., Matsuda, H., & Tanaka, A. (2020) · Veterinary and Animal Science · doi:10.1016/j.vas.2020.100129 · Cited by 7
Nada, M., & Metwaly, E. E. (2020) · Journal of Plant Production · doi:10.21608/jpp.2020.79990 · Cited by 7
Hu, P., Mo, Z., Chen, Y., Wu, Y., Song, L., Zhang, L., Li, Z., Fu, L., Liang, H., Tao, Y., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15139047 · Cited by 7
Zhao, S., Wang, Y., Liu, H., Jia, X., Zhang, Y., Zhang, L., Da, B., Wang, Q., Zheng, H., Li, H., et al. (2025) · Journal of Catalysis · doi:10.1016/j.jcat.2025.116502 · Cited by 6
Jin, Y., Chen, S., Zhao, Q., Yang, N., Ning, Y., & Xu, X. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.106316 · Cited by 6
Mechanisms and Management Strategies for Satsuma Mandarin Fruit Cracking
Li, Y., Jin, G., Wen, M., Zhu, X., & Zheng, Y. (2025) · Agronomy · doi:10.3390/agronomy15030698 · Cited by 6
Multi-spectroscopic characterization of organic salt components in medicinal plant
Han, L., Ma, F., He, P., Zhou, Q., Li, Z., & Sun, S.-Q. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.139195 · Cited by 6
Zhu, C., Xu, Y., & Wang, D. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141617 · Cited by 6
Okamura, T., Furuya, R., & Onitsuka, K. (2015) · Dalton Transactions · doi:10.1039/c5dt00053j · Cited by 6
Imai, S., Maruyama, T., Osawa, M., Hattori, M., Ishitani, R., Nureki, O., & Shimada, I. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.06.008 · Cited by 6
Ammar, F. F., Hobaika, Z., Abdel‐Azeim, S., Zargarian, L., Maroun, R. G., & Fermandjian, S. (2015) · FEBS Open Bio · doi:10.1002/2211-5463.12025 · Cited by 6
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