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 101–200 of 436
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 International Edition · doi:10.1002/anie.202424316 · Cited by 42
Craig, S. N., Gao, L., Lee, I. J.-A., Gray, T., & Berdis, A. J. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm2005942 · Cited by 42
The human "magnesome": detecting magnesium binding sites on human proteins
Piovesan, D., Profiti, G., Martelli, P. L., & Casadio, R. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-s14-s10 · Cited by 41
McNae, I. W., Martínez‐Oyanedel, J., Keillor, J. W., Michels, P. A. M., Fothergill‐Gilmore, L. A., & Walkinshaw, M. D. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.047 · Cited by 41
Hassan, N., Krieg, T. M., Zinser, M. J., Schröder, K., & Kröger, N. (2023) · Polymers · doi:10.3390/polym15193854 · Cited by 40
Chatterjee, A., Dixit, M. K., & Tembe, B. L. (2013) · The Journal of Physical Chemistry A · doi:10.1021/jp4031706 · Cited by 40
Selective “off-on” detection of magnesium (II) ions using a naphthalimide-derived fluorescent probe
Zhang, H., Yin, C., Liu, T., Chao, J., Zhang, Y., & Huo, F. (2017) · Dyes and Pigments · doi:10.1016/j.dyepig.2017.07.033 · Cited by 40
Carbon-based single-atom catalysts: impacts of atomic coordination on the oxygen reduction reaction
Kang, Z., Wang, X., Wang, D., Bai, B., Zhao, Y., Xiang, X., Zhang, B., & Shang, H. (2023) · Nanoscale · doi:10.1039/d3nr01272g · Cited by 39
l-Proline promoted fluorescent sensor for Mg2+ detection in a multicomponent sensory system
Dong, Y., Mao, X., Jiang, X., Hou, J., Cheng, Y., & Zhu, C. (2011) · Chemical Communications · doi:10.1039/c1cc12957k · Cited by 39
Cabral-Marques, O., Schimke, L. F., de Oliveira, E. B., Khawanky, N. E., Ramos, R. N., al-Ramadi, B. K., Segundo, G. R. S., Ochs, H. D., & Condino‐Neto, A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02742 · Cited by 39
Mutagenesis Studies of Protein Farnesyltransferase Implicate Aspartate β352 as a Magnesium Ligand
Pickett, J. S., Bowers, K. E., & Fierke, C. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309226200 · Cited by 39
Promiscuous restriction is a cellular defense strategy that confers fitness advantage to bacteria
Vasu, K., Nagamalleswari, E., & Nagaraja, V. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119226109 · Cited by 39
Magnesium deficiency: Does it have a role to play in cataractogenesis?
Agarwal, R., Iezhitsa, I. N., Agarwal, P., & Спасов, А. А. (2012) · Experimental Eye Research · doi:10.1016/j.exer.2012.05.008 · Cited by 38
Wang, J., Zhang, B., Zhang, J., Wang, H., Zhao, M., Wang, N., Dong, L., Zhou, X., & Wang, D. (2014) · Bioresource Technology · doi:10.1016/j.biortech.2014.07.081 · Cited by 37
Bone resorption: supporting immunometabolism
van Niekerk, G., Mitchell, M., & Engelbrecht, A. (2018) · Biology Letters · doi:10.1098/rsbl.2017.0783 · Cited by 37
Berta, D., Buigues, P. J., Badaoui, M., & Rosta, E. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.01.002 · Cited by 37
Short-Term Magnesium Deficiency Triggers Nutrient Retranslocation in Arabidopsis thaliana
Ogura, T., Kobayashi, N. I., Hermans, C., Ichihashi, Y., Shibata, A., Shirasu, K., Aoki, N., Sugita, R., Ogawa, T., Suzuki, H., et al. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00563 · Cited by 37
Anyasor, G. N., Onajobi, F. D., Osilesi, O., & Adebawo, O. O. (2014) · Journal of Intercultural Ethnopharmacology · doi:10.5455/jice.20140527085848 · Cited by 37
Pardun, K., Treccani, L., Volkmann, E., Streckbein, P., Heiß, C., Gerlach, J. W., Maendl, S., & Rezwan, K. (2015) · Journal of Biomaterials Applications · doi:10.1177/0885328215572428 · Cited by 36
Schwartz, S. C., Pinto‐Pacheco, B., Pitteloud, J., & Buccella, D. (2014) · Inorganic Chemistry · doi:10.1021/ic5000606 · Cited by 36
Structural and Biochemical Properties of Novel Self-Cleaving Ribozymes
Lee, K.-Y., & Lee, B. (2017) · Molecules · doi:10.3390/molecules22040678 · Cited by 36
Highly selective, red emitting BODIPY-based fluorescent indicators for intracellular Mg 2+ imaging
Lin, Q., & Buccella, D. (2018) · Journal of Materials Chemistry B · doi:10.1039/c8tb01599f · Cited by 36
Multivariate analysis on the distribution of elements in plants
Kumar, V., Sharma, A., Bakshi, P., Bhardwaj, R., & Thukral, A. K. (2018) · Acta Physiologiae Plantarum · doi:10.1007/s11738-018-2765-x · Cited by 35
Magnesium induced structural reorganization in the active site of adenylate kinase
Nam, K., Thodika, A. R. A., Tischlik, S., Phoeurk, C., Nagy, T. M., Schierholz, L., Ådén, J., Rogne, P., Drescher, M., Sauer-Eriksson, A. E., et al. (2024) · Science Advances · doi:10.1126/sciadv.ado5504 · Cited by 35
Balatsos, N. A. A., Vlachakis, D., Maragozidis, P., Manta, S., Anastasakis, D. G., Kyritsis, A. P., Vlassi, M., Komiotis, D., & Stathopoulos, C. (2009) · Biochemistry · doi:10.1021/bi900236k · Cited by 35
In crystallo observation of three metal ion promoted DNA polymerase misincorporation
Chang, C., Luo, C. L., & Gao, Y. (2022) · Nature Communications · doi:10.1038/s41467-022-30005-3 · Cited by 35
Zhang, K., Zhang, L., Zhang, T., Mao, M., & Fu, J. (2016) · Environmental Pollution · doi:10.1016/j.envpol.2016.10.042 · Cited by 35
Diverse relationships between metal ions and the ribosome
Akanuma, G. (2021) · Bioscience, Biotechnology, and Biochemistry · doi:10.1093/bbb/zbab070 · Cited by 34
Mihaylova, D. S., Popova, A. T., Desseva, I., Manolov, I., Petkova, N. T., Vrancheva, R. Z., Peltekov, A., Slavov, A. M., & Zhivondov, A. (2021) · Molecules · doi:10.3390/molecules26092818 · Cited by 34
Recent Advances in the Structural Biology of Mg2+ Channels and Transporters
Jin, F., Huang, Y., & Hattori, M. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167729 · Cited by 34
Magnesium and embryonic development
Komiya, Y., Su, L.-T., Chen, H.-C., Habas, R., & Runnels, L. W. (2014) · Magnesium Research · doi:10.1684/mrh.2014.0356 · Cited by 34
Yang, M., & Wang, X. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.12.089 · Cited by 33
Mg deficiency affects leaf Mg remobilization and the proteome in Brassica napus
Billard, V., Maillard, A., Coquet, L., Jouenne, T., Cruz, F., García‐Mina, J. M., Yvin, J., Ourry, A., & Étienne, P. (2016) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2016.06.025 · Cited by 33
Zhang, Q., Ma, R., Li, Z., & Liu, Z. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117857 · Cited by 33
Schumacher, S., Roth, I., Stahl, J., Bäumer, W., & Kietzmann, M. (2013) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.10.030 · Cited by 32
Reciprocal effects of huanglongbing infection and nutritional status of citrus trees: a review
Mattos, D., Kadyampakeni, D. M., da Silva, J. R., Vashisth, T., & Boaretto, R. M. (2020) · Tropical Plant Pathology · doi:10.1007/s40858-020-00389-y · Cited by 32
Liu, J., Liu, R., Cao, Y., & Chen, M. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp04105g · Cited by 32
Dietary magnesium restriction reduces amygdala–hypothalamic GluN1 receptor complex levels in mice
Ghafari, M., Whittle, N., Miklósi, A. G., Kotlowsky, C., Schmuckermair, C., Berger, J., Bennett, K. L., Singewald, N., & Lübec, G. (2014) · Brain Structure and Function · doi:10.1007/s00429-014-0779-8 · Cited by 32
Prabhakar, S., & Melnik, R. (2017) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2017.12.009 · Cited by 32
Tsunaka, Y., Takano, K., Matsumura, H., Yamagata, Y., & Kanaya, S. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.11.007 · Cited by 32
Rapid Isolation of Arabidopsis Chloroplasts and Their Use for In Vitro Protein Import Assays
Aronsson, H., & Jarvis, P. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-234-2_17 · Cited by 32
Magnesium Transport and Magnesium Homeostasis
Papp-Wallace, K. M., & Maguire, M. E. (2008) · EcoSal Plus · doi:10.1128/ecosalplus.5.4.4.2 · Cited by 31
He, K., Yu, X., Qin, L., & Wu, Y. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.133116 · Cited by 31
Hou, Y., Lu, Y., Zhang, X., & Huang, Y. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.132409 · Cited by 31
Farruggia, G., Iotti, S., Prodi, L., Zaccheroni, N., Montalti, M., Savage, P. B., Andreani, G., Trapani, V., & Wolf, F. I. (2008) · Journal of Fluorescence · doi:10.1007/s10895-008-0374-6 · Cited by 31
Adou, M., Achille, T. F., Gbané, M., Koff, P. V. N., & Georges, A. N. (2011) · Pakistan Journal of Nutrition · doi:10.3923/pjn.2011.1109.1114 · Cited by 31
Flavin transferase: the maturation factor of flavin-containing oxidoreductases
Bogachev, A. V., Baykov, A. A., & Bertsova, Y. V. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180524 · Cited by 30
Influence of divalent magnesium ion on DNA: molecular dynamics simulation studies
Mukherjee, S., & Bhattacharyya, D. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.713780 · Cited by 30
Preferential binding of the magnesium ion by anthraquinone based chromogenic receptors
Kar, P., Suresh, M., Kumar, D. K., Jose, D. A., Ganguly, B., & Das, A. (2006) · Polyhedron · doi:10.1016/j.poly.2006.10.051 · Cited by 29
Synthesis of Toxicological Behavior of Oil Sands Process-Affected Water Constituents
Belosevic, M., Singh, A. P., Gamal El-Din, M., Li, C., McPhedran, K. N., Chelme‐Ayala, P., & Klamerth, N. (2014) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r34b2x69h · Cited by 29
Foliar Mineral Treatments for The Reduction of Melon (Cucumis melo L.) Fruit Cracking
López-Zaplana, A., Bárzana, G., Agudelo, A., & Carvajal, M. (2020) · Agronomy · doi:10.3390/agronomy10111815 · Cited by 28
Zang, Y., Wu, Q., Wang, S., Huang, B., Dai, Y., & Ma, Y. (2023) · Physical Review Applied · doi:10.1103/physrevapplied.19.024003 · Cited by 28
Physiological and transcriptomic responses to magnesium deficiency in Neolamarckia Cadamba
Wang, Y., Zhang, X., Zhang, W., Peng, M., Tan, G., Qaseem, M. F., Li, H., & Wu, A. (2023) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2023.107645 · Cited by 28
Akanuma, G., Yamazaki, K., Yagishi, Y., Iizuka, Y., Ishizuka, M., Kawamura, F., & Kato-Yamada, Y. (2018) · Journal of Bacteriology · doi:10.1128/jb.00212-18 · Cited by 27
Assessment of magnesium intake according to requirement in dairy cows
Märtens, H., & Stumpff, F. (2019) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/jpn.13106 · Cited by 27
Kundra, P., Rachmühl, C., Lacroix, C., & Geirnaert, A. (2020) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201901271 · Cited by 27
Improvement of Salinity Tolerance in Rice Seedlings by Exogenous Magnesium Sulfate Application
Xuan, T. D., Huong, C. T., Quan, N. V., Anh, L. H., Khanh, T. D., & Rayee, R. (2022) · Soil Systems · doi:10.3390/soilsystems6030069 · Cited by 27
Meng, X., Bai, S., Wang, S., Pan, Y., Chen, K., Xie, K., Wang, M., & Guo, S. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1164866 · Cited by 27
Kumari, S., Kumar, R. R., Mendiratta, S. K., Kumar, D., Rana, P., Kumar, D., & Jawla, J. (2019) · 3 Biotech · doi:10.1007/s13205-019-1595-x · Cited by 27
Cytotoxic effect of galvanically coupled magnesium–titanium particles
Kim, J., & Gilbert, J. L. (2015) · Acta Biomaterialia · doi:10.1016/j.actbio.2015.11.030 · Cited by 27
Zhou, D., Wang, C., Zhu, L., Chen, Y., Gao, S., Guo, J., Lu, W., Su, Y., Xu, L., & Que, Y. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00279 · Cited by 27
Sun, L., Yu, Q., Peng, F., Sun, C., Wang, D., Pu, L., Xiong, F., Tian, Y., Peng, C. Y., & Zhou, Q. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1276383 · Cited by 26
Structural and Functional Characteristics of Homing Endonucleases
Guhan, N., & Muniyappa, K. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609235 · Cited by 26
Disorders of Calcium, Magnesium, and Phosphate Balance
Smogorzewski, M. J., Robert K. Rude, & Yu, A. S. L. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4160-6193-9.10018-1 · Cited by 25
Functional Nucleic Acid Enzymes: Nucleic Acid-Based Catalytic Factories
Yang, M., Xie, Y., Zhu, L., Li, X., & Xu, W. (2024) · ACS Catalysis · doi:10.1021/acscatal.4c02670 · Cited by 25
Solt, I., Simon, I., Császár, A. G., & Fuxreiter, M. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp0668192 · Cited by 25
Nehra, A., Hinge, V. K., & Rao, C. P. (2014) · The Journal of Organic Chemistry · doi:10.1021/jo500892r · Cited by 25
Variation in Properties of Bioactive Glasses After Surface Modification
Stanić, V. D. (2017) · Springer eBooks · doi:10.1007/978-3-319-56059-5_2 · Cited by 25
Chaudret, R., Piquemal, J., & Cisneros, G. A. (2011) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp02550j · Cited by 25
Ge, M., Zhong, R., Sadeghnezhad, E., Hakeem, A., Xiao, X., Wang, P., & Fang, J. (2022) · BMC Plant Biology · doi:10.1186/s12870-022-03599-5 · Cited by 24
Response of Medical Cannabis to Magnesium (Mg) Supply at the Vegetative Growth Phase
Morad, D., & Bernstein, N. (2023) · Plants · doi:10.3390/plants12142676 · Cited by 24
León-Pimentel, C. I., Amaro-Estrada, J. I., Hernández‐Cobos, J., Saint-Martín, H., & Ramírez-Solís, A. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5021348 · Cited by 24
Double-strand hydrolysis of DNA by a magnesium(II) complex with diethylenetriamine
Yang, P., Ren, R., Guo, M., Song, A., Meng, X., Yuan, C., Zhou, Q., Chen, H., Xiong, Z., & Gao, X. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0548-x · Cited by 24
Dehnavi, A. R., Zahedi, M., Razmjoo, J., & Eshghizadeh, H. R. (2019) · Journal of Plant Nutrition · doi:10.1080/01904167.2019.1617307 · Cited by 23
Evaluation of eggshell powder as an experimental direct pulp capping material
Salah, M., Kataia, M. M., Kataia, E. M., Din, E. A. E., & Essa, M. (2018) · Future Dental Journal · doi:10.1016/j.fdj.2018.05.008 · Cited by 23
Potential antiosteoporosis effect of biodegradable magnesium implanted in STZ‐induced diabetic rats
Yang, W., Zhang, Y., Yang, J., Tan, L., & Yang, K. (2011) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.33201 · Cited by 23
Wang, Z., Sapienza, P. J., Abeysinghe, T., Luzum, C., Lee, A. L., Finer-Moore, J. S., Stroud, R. M., & Kohen, A. (2013) · Journal of the American Chemical Society · doi:10.1021/ja400761x · Cited by 22
Concentrations and distributions of Al, Ca, Cl, K, Mg and Mn in a Scots pine forest in Belgium
Gielen, S., Batlle, J. V. I., Vincke, C., Hees, M. V., & Vandenhove, H. (2016) · Ecological Modelling · doi:10.1016/j.ecolmodel.2015.12.015 · Cited by 22
Liu, Y., Guo, Y., Wang, Z., & Nie, W. (2007) · Archives of Animal Nutrition · doi:10.1080/17450390701432019 · Cited by 22
Sugita, M., Onishi, I., Irisa, M., Yoshida, N., & Hirata, F. (2021) · Molecules · doi:10.3390/molecules26020271 · Cited by 21
Nucleic Acid Isolation and Downstream Applications
Sirkov, I. N. (2016) · InTech eBooks · doi:10.5772/61833 · Cited by 21
Grotz, K. K., & Schwierz, N. (2022) · The Journal of Chemical Physics · doi:10.1063/5.0087292 · Cited by 21
Qi, J., Shen, X., Chen, M., Shangguan, E., Zhang, W., & Cao, R. (2022) · Chemical Communications · doi:10.1039/d2cc03755f · Cited by 21
The structure of MgtE in the absence of magnesium provides new insights into channel gating
Jin, F., Sun, M., Fujii, T., Yamada, Y., Wang, J., Maturana, A. D., WADA, M., Su, S., Ma, J., Takeda, H., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001231 · Cited by 20
Cui, Y., Gao, J., Guo, Y., Li, Z., Wang, Z., & Zhao, Y. (2022) · Environmental Research · doi:10.1016/j.envres.2022.114263 · Cited by 20
The Mechanisms of Mg2+ and Co2+ Transport by the CorA Family of Divalent Cation Transporters
Guskov, A., & Eshaghi, S. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394390-3.00014-8 · Cited by 20
Liu, L., Chen, F., Wei, T., Chen, R., Min, D., Yu, S., Wu, J., Chen, J., & Xiong, Y. (2025) · Environmental Science & Technology · doi:10.1021/acs.est.5c05354 · Cited by 19
Okamura, T., Furuya, R., & Onitsuka, K. (2014) · Journal of the American Chemical Society · doi:10.1021/ja509006x · Cited by 19
Seiffert, F., Bandow, N., Kalbe, U., Milke, R., & Gorbushina, A. A. (2016) · Frontiers in Earth Science · doi:10.3389/feart.2016.00031 · Cited by 19
Vashishtha, A. K., & Konigsberg, W. H. (2018) · AIMS Biophysics · doi:10.3934/biophy.2018.2.125 · Cited by 19
The Effect of Admission Serum Magnesium on the Acute Kidney Injury Among Patients with Malignancy
Shen, D., Wang, Y., Xu, J., Yang, L., Chen, X., Guo, M., Geng, X., Ding, X., & Xu, X. (2020) · Cancer Management and Research · doi:10.2147/cmar.s262674 · Cited by 19
Production of γ-terpinene by metabolically engineered Escherichia coli using glycerol as feedstock
Qi, C., Zhao, H., Li, W., Li, X., Xiang, H., Zhang, G., Liu, H., Wang, Q., Wang, Y., Xian, M., et al. (2018) · RSC Advances · doi:10.1039/c8ra02076k · Cited by 19
Hoppert, M. (2011) · Encyclopedia of earth sciences series/Encyclopedia of earth sciences · doi:10.1007/978-1-4020-9212-1_134 · Cited by 19
Djukić‐Vuković, A., Jokic, B. M., Kocić‐Tanackov, S., Pejin, J. D., & Mojović, L. V. (2015) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2015.07.035 · Cited by 18
Wang, T., Chen, Y., Kao, L., Chang, C., Wang, Y., Liu, Y.-H., Feng, J.-M., & Wu, T. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06635.x · Cited by 18
Giri, N. A., & Sajeev, M. S. (2019) · Agricultural Research · doi:10.1007/s40003-019-00411-z · Cited by 18
Microbial ingress and in vitro degradation enhanced by glucose on bioabsorbable Mg–Li–Ca alloy
Li, L., Han, Z.-Z., Zeng, R., Qi, W., Zhai, X., Yang, Y., Lou, Y., Gu, T., Xu, D., & Duan, J. (2020) · Bioactive Materials · doi:10.1016/j.bioactmat.2020.06.014 · Cited by 18
Taran, O., Medrano, F., & Yatsimirsky, A. K. (2008) · Dalton Transactions · doi:10.1039/b807030j · Cited by 18
Strategic nutrient sourcing for biomanufacturing intensification
Noroozi, K., & Jarboe, L. R. (2023) · Journal of Industrial Microbiology & Biotechnology · doi:10.1093/jimb/kuad011 · Cited by 17
Specificity of LTR DNA recognition by a peptide mimicking the HIV-1 integrase α4 helix
Hobaika, Z., Zargarian, L., Boulard, Y., Maroun, R. G., Mauffret, O., & Fermandjian, S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp824 · Cited by 17
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