Molybdenum cofactor and human disease

The mononuclear molybdenum enzymes

Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738

The Mononuclear Molybdenum Enzymes

Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501

Molybdenum cofactors, enzymes and pathways

Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872

The emerging biology of the nitrite anion

Gladwin, M. T., Schechter, A. N., Kim-Shapiro, D. B., Patel, R. P., Hogg, N., Shiva, S., Cannon, R. O., Kelm, M., Wink, D. A., Espey, M. G., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio1105-308 · Cited by 609

Gephyrin: a master regulator of neuronal function?

Tyagarajan, S. K., & Fritschy, J. (2014) · Nature reviews. Neuroscience · doi:10.1038/nrn3670 · Cited by 442

Cystathionine γ-lyase deficiency mediates neurodegeneration in Huntington’s disease

Paul, B. D., Sbodio, J. I., Xu, R., Vandiver, M. S., Cha, J. Y., Snowman, A. M., & Snyder, S. H. (2014) · Nature · doi:10.1038/nature13136 · Cited by 407

Hydrogen peroxide is the major oxidant product of xanthine oxidase

Kelley, E. E., Khoo, N. K. H., Hundley, N. J., Malik, U. Z., Freeman, B. Α., & Tarpey, M. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.11.012 · Cited by 399

Successful Treatment of Molybdenum Cofactor Deficiency Type A With cPMP

Veldman, A., Santamaria‐Araujo, J. A., Sollazzo, S., Pitt, J. J., Gianello, R., Yaplito‐Lee, J., Wong, F. Y., Ramsden, C. A., Reiss, J., Cook, I., et al. (2010) · PEDIATRICS · doi:10.1542/peds.2009-2192 · Cited by 195

Rare exonic deletions implicate the synaptic organizer Gephyrin (GPHN) in risk for autism, schizophrenia and seizures

Lionel, A. C., Vaags, A. K., Sato, D., Gazzellone, M. J., Mitchell, E. B., Chen, H. Y., Costain, G., Walker, S., Egger, G., Thiruvahindrapuram, B., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt056 · Cited by 176

Molybdenum cofactor deficiency: Mutations in GPHN, MOCS1, and MOCS2

Reiss, J., & Hahnewald, R. (2010) · Human Mutation · doi:10.1002/humu.21390 · Cited by 172

An Update on the Nitrogen Heterocycle Compositions and Properties of U.S. FDA-Approved Pharmaceuticals (2013–2023)

Marshall, C. M., Federice, J. G., Bell, C. N., Cox, P. B., & Njardarson, J. T. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01122 · Cited by 1,112

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

Cysteine Metabolism in Neuronal Redox Homeostasis

Paul, B. D., Sbodio, J. I., & Snyder, S. H. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.02.007 · Cited by 356

A State-of-the-Science Review on Metal Biomarkers

Martínez-Morata, I., Sobel, M., Téllez-Plaza, M., Navas‐Acién, A., Howe, C. G., & Sanchez, T. R. (2023) · Current Environmental Health Reports · doi:10.1007/s40572-023-00402-x · Cited by 273

Multi-omics signatures of the human early life exposome

Maître, L., Bustamante, M., Hernandéz-Ferrer, C., Thiel, D., Lau, C. E., Siskos, A., Vives-Usano, M., Ruiz-Arenas, C., Pelegrí-Sisó, D., Robinson, O., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34422-2 · Cited by 242

Role of molybdenum in material immunomodulation and periodontal wound healing: Targeting immunometabolism and mitochondrial function for macrophage modulation

He, X., Li, X., Zhang, M., Tian, B., Sun, L., Bi, C., Deng, D., Zhou, H., Qu, H., Wu, C., et al. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121439 · Cited by 131

Why cells need iron: a compendium of iron utilisation

Teh, M. R., Armitage, A. E., & Drakesmith, H. (2024) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2024.04.015 · Cited by 114

Homeostatic impact of sulfite and hydrogen sulfide on cysteine catabolism

Kohl, J. B., Mellis, A., & Schwarz, G. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14464 · Cited by 89

Molybdenum cofactor biology, evolution and deficiency

Mayr, S. J., Mendel, R. R., & Schwarz, G. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118883 · Cited by 80

Nitrite‐dependent nitric oxide synthesis by molybdenum enzymes

Bender, D. A., & Schwarz, G. (2018) · FEBS Letters · doi:10.1002/1873-3468.13089 · Cited by 76

Multicellular Bioprinting of Biomimetic Inks for Tendon‐to‐Bone Regeneration

Du, L., Chen, Q., Zhang, H., Han, F., Xue, J., Wang, Y., Wu, J., Xiao, Y., Huan, Z., & Wu, C. (2023) · Advanced Science · doi:10.1002/advs.202301309 · Cited by 73

Tuning GABAergic Inhibition: Gephyrin Molecular Organization and Functions

Pizzarelli, R., Griguoli, M., Zacchi, P., Petrini, E. M., Barberis, A., Cattaneo, A., & Cherubini, E. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2019.07.036 · Cited by 69

Bezafibrate prevents mitochondrial dysfunction, antioxidant system disturbance, glial reactivity and neuronal damage induced by sulfite administration in striatum of rats: Implications for a possible therapeutic strategy for sulfite oxidase deficiency

Grings, M., Moura, A. P., Parmeggiani, B., Pletsch, J. T., Cardoso, G. M. F., August, P. M., Matté, C., Wyse, Â. T. D. S., Wajner, M., & Leipnitz, G. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.05.019 · Cited by 61

Molybdenum Cofactor Deficiency in Humans

Johannes, L., Fu, C.-Y., & Schwarz, G. (2022) · Molecules · doi:10.3390/molecules27206896 · Cited by 59

Therapeutic potential of pteridine derivatives: A comprehensive review

Carmona‐Martínez, V., Ruiz‐Alcaraz, A. J., Vera, M., Guirado, A., Martinez‐Esparza, M., & García–Peñarrubia, P. (2018) · Medicinal Research Reviews · doi:10.1002/med.21529 · Cited by 63

The sulfite oxidase Shopper controls neuronal activity by regulating glutamate homeostasis in Drosophila ensheathing glia

Otto, N., Marelja, Z., Schoofs, A., Kranenburg, H., Bittern, J., Yildirim, K., Berh, D., Bethke, M., Thomas, S., Rode, S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05645-z · Cited by 61

Impact of Ecklonia maxima Seaweed Extract and Mo Foliar Treatments on Biofortification, Spinach Yield, Quality and NUE

Bella, S. L., Consentino, B. B., Rouphael, Y., Ntatsi, G., PASQUALE, C. D., Iapichino, G., & Sabatino, L. (2021) · Plants · doi:10.3390/plants10061139 · Cited by 55

Protein Hydrolysates and Mo-Biofortification Interactively Modulate Plant Performance and Quality of ‘Canasta’ Lettuce Grown in a Protected Environment

Sabatino, L., Consentino, B. B., Rouphael, Y., PASQUALE, C. D., Iapichino, G., D’Anna, F., & Bella, S. L. (2021) · Agronomy · doi:10.3390/agronomy11061023 · Cited by 53

Cysteine residues in mitochondrial intermembrane space proteins: more than just import

Habich, M., Salscheider, S. L., & Riemer, J. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14480 · Cited by 50

Interactive Effects of Genotype and Molybdenum Supply on Yield and Overall Fruit Quality of Tomato

Sabatino, L., D’Anna, F., Iapichino, G., Moncada, A., D'Anna, E., & PASQUALE, C. D. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01922 · Cited by 49

Prosthetic Metals: Release, Metabolism and Toxicity

Zhong, Q., Pan, X., Chen, Y., Lian, Q., Gao, J., Xu, Y., Wang, J., Shi, Z., & Cheng, H. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s459255 · Cited by 47

Molecular Dockings and Molecular Dynamics Simulations Reveal the Potency of Different Inhibitors against Xanthine Oxidase

Pan, Y., Lu, Z., Li, C., Qi, R., Chang, H., Han, L., & Han, W. (2021) · ACS Omega · doi:10.1021/acsomega.1c00968 · Cited by 45

Targeting the human gut microbiome with small-molecule inhibitors

Woo, A. Y. M., Aguilar Ramos, M. A., Narayan, R., Richards-Corke, K. C., Wang, M. L., Sandoval-Espinola, W. J., & Balskus, E. P. (2023) · Nature Reviews Chemistry · doi:10.1038/s41570-023-00471-4 · Cited by 42

Trace Elements Levels in Major Depressive Disorder—Evaluation of Potential Threats and Possible Therapeutic Approaches

Baj, J., Bargieł, J., Cabaj, J., Skierkowski, B., Hunek, G., Portincasa, P., Flieger, J., & Smoleń, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015071 · Cited by 49

ETHE1 and MOCS1 deficiencies: Disruption of mitochondrial bioenergetics, dynamics, redox homeostasis and endoplasmic reticulum-mitochondria crosstalk in patient fibroblasts

Grings, M., Seminotti, B., Karunanidhi, A., Ghaloul‐Gonzalez, L., Mohsen, A.-W. A., Wipf, P., Palmfeldt, J., Vockley, J. E., & Leipnitz, G. (2019) · Scientific Reports · doi:10.1038/s41598-019-49014-2 · Cited by 42

MoS2 Nanoclusters-based biomaterials for disease- impaired wound therapy

Ma, B., Dang, W., Yang, Z., Chang, J., & Wu, C. (2020) · Applied Materials Today · doi:10.1016/j.apmt.2020.100735 · Cited by 40

The Role of Oxidative Stress and Bioenergetic Dysfunction in Sulfite Oxidase Deficiency: Insights from Animal Models

Wyse, Â. T. D. S., Grings, M., Wajner, M., & Leipnitz, G. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9986-z · Cited by 39

The role of glutamate oxaloacetate transaminases in sulfite biosynthesis and H2S metabolism

Mellis, A., Misko, A. L., Arjune, S., Liang, Y., Erdélyi, K., Ditrói, T., Kaczmarek, A. T., Nagy, P., & Schwarz, G. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101800 · Cited by 38

Beyond the Mind—Serum Trace Element Levels in Schizophrenic Patients: A Systematic Review

Baj, J., Forma, A., Sitarz, R., Karakuła, K. H., Flieger, W., Sitarz, M., Grochowski, C., Maciejewski, R., & Karakuła‐Juchnowicz, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249566 · Cited by 40

Shared function and moonlighting proteins in molybdenum cofactor biosynthesis

Leimkühler, S. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0110 · Cited by 39

Compositional determinants of fruit and vegetable quality and nutritional value

Vicente, A. R., Manganaris, G., Darré, M., Ortiz, C., Sozzi, G. O., & Crisosto, C. (2022) · Postharvest Handling · doi:10.1016/b978-0-12-822845-6.00019-1 · Cited by 21

Controllable Adaptive Molybdate‐Oligosaccharide Nanoparticles Regulate M2 Macrophage Mitochondrial Function and Promote Angiogenesis via PI3K/HIF‐1α/VEGF Pathway to Accelerate Diabetic Wound Healing

Huang, X., Zheng, L., Zhou, Y., Hu, S., Ning, W., Li, S., Lin, Z., & Huang, S. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202302256 · Cited by 31

Evaluation of biological response induced by molybdenum oxide nanocolloids on in vitro cultured NIH/3T3 fibroblast cells by micro-Raman spectroscopy

Fazio, E., Speciale, A., Spadaro, S., Bonsignore, M., Cimino, F., Cristani, M., Trombetta, D., Saija, A., & Neri, F. (2018) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2018.06.028 · Cited by 31

Structural basis for the role of mammalian aldehyde oxidases in the metabolism of drugs and xenobiotics

Romão, M. J., Coelho, C., Santos‐Silva, T., Foti, A., Terao, M., Garattini, E., & Leimkühler, S. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.01.005 · Cited by 30

New metal cofactors and recent metallocofactor insights

Hausinger, R. P. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.12.008 · Cited by 32

Molybdenum – a scoping review for Nordic Nutrition Recommendations 2023

Oskarsson, A., & Kippler, M. J. (2023) · Food & Nutrition Research · doi:10.29219/fnr.v67.10326 · Cited by 28

Biologic activity of cyclic and caged phosphates: a review

Lorke, D. E., Stegmeier‐Petroianu, A., & Petroianu, G. A. (2016) · Journal of Applied Toxicology · doi:10.1002/jat.3369 · Cited by 27

Impaired mitochondrial maturation of sulfite oxidase in a patient with severe sulfite oxidase deficiency

Bender, D. A., Kaczmarek, A. T., Santamaria‐Araujo, J. A., Stueve, B., Waltz, S., Bartsch, D., Kurian, L., Çırak, S., & Schwarz, G. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz109 · Cited by 27

Synthetic Approaches to the New Drugs Approved During 2021

McInturff, E. L., France, S. P., Leverett, C. A., Flick, A. C., Lindsey, E. A., Berritt, S., Carney, D. W., DeForest, J. C., Ding, H. X., Fink, S. J., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00501 · Cited by 26

Does the Micronutrient Molybdenum Have a Role in Gestational Complications and Placental Health?

Foteva, V., Fisher, J. J., Qiao, Y., & Smith, R. (2023) · Nutrients · doi:10.3390/nu15153348 · Cited by 26

Modeling the acid-base properties of molybdate(VI) in different ionic media, ionic strengths and temperatures, by EDH, SIT and Pitzer equations

Crea, F., Stefano, C. D., Irto, A., Milea, D., Pettignano, A., & Sammartano, S. (2016) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2016.12.041 · Cited by 24

In utero and peripubertal metals exposure in relation to reproductive hormones and sexual maturation and progression among boys in Mexico City

Ashrap, P., Meeker, J. D., Sánchez, B. N., Basu, N., Tamayo‐Ortiz, M., Solano-González, M., Mercado‐García, A., Téllez‐Rojo, M. M., Peterson, K. E., & Watkins, D. J. (2020) · Environmental Health · doi:10.1186/s12940-020-00672-0 · Cited by 24

The peacefulness gene promotes aggression in Drosophila

Ramin, M., Li, Y., Chang, W.-T., Shaw, H. S., & Rao, Y. (2019) · Molecular Brain · doi:10.1186/s13041-018-0417-0 · Cited by 24

A mild case of molybdenum cofactor deficiency defines an alternative route of MOCS1 protein maturation

Mayr, S. J., Sass, J. O., Vry, J., Kirschner, J., Mader, I., Hövener, J., Reiss, J., Santamaria‐Araujo, J. A., Schwarz, G., & Grünert, S. C. (2018) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-018-0138-7 · Cited by 22

Anticancer Metallocenes and Metal Complexes of Transition Elements from Groups 4 to 7

Kostova, I. P. (2024) · Molecules · doi:10.3390/molecules29040824 · Cited by 21

Characterization of a Metal-Resistant Bacillus Strain With a High Molybdate Affinity ModA From Contaminated Sediments at the Oak Ridge Reservation

Ge, X., Thorgersen, M. P., Poole, F. L., Deutschbauer, A. M., Chandonia, J., Novichkov, P. S., Gushgari-Doyle, S., Lui, L. M., Nielsen, T., Chakraborty, R., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.587127 · Cited by 21

Sulfite Alters the Mitochondrial Network in Molybdenum Cofactor Deficiency

Mellis, A., Roeper, J., Misko, A. L., Kohl, J. B., & Schwarz, G. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2020.594828 · Cited by 21

Genetic dissection of cyclic pyranopterin monophosphate biosynthesis in plant mitochondria

Kruse, I., Maclean, A. E., Hill, L. M., & Balk, J. (2017) · Biochemical Journal · doi:10.1042/bcj20170559 · Cited by 19

Alteration of Trace Elements during Pathogenesis of N-Nitrosodimethylamine Induced Hepatic Fibrosis

George, J., Tsutsumi, M., & Tsuchishima, M. (2019) · Scientific Reports · doi:10.1038/s41598-018-37516-4 · Cited by 20

Remote Charge Effects on the Oxygen-Atom-Transfer Reactivity and Their Relationship to Molybdenum Enzymes

Paudel, J., Pokhrel, A., Kirk, M. L., & Li, F. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b03093 · Cited by 19

Fosdenopterin: First Approval

Kang, C. (2021) · Drugs · doi:10.1007/s40265-021-01520-2 · Cited by 19

Urinary metals and adipokines in midlife women: The Study of Women's Health Across the nation (SWAN)

Wang, X., Karvonen-Gutierrez, C. A., Mukherjee, B., Herman, W. H., & Park, S. K. (2020) · Environmental Research · doi:10.1016/j.envres.2020.110426 · Cited by 18

Protein-bound molybdenum cofactor is bioavailable and rescues molybdenum cofactor-deficient C. elegansPreprint

Warnhoff, K., Hercher, T. W., Mendel, R. R., & Ruvkun, G. (2021) · Genes & Development · doi:10.1101/gad.345579.120 · Cited by 18

Structure, Function, and Mechanism of Pyranopterin Molybdenum and Tungsten Enzymes

Ingersol, L. J., & Kirk, M. L. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14929-7 · Cited by 16

Engineering metabolism to modulate immunity

Kapnick, S. M., Martin, C. A., & Jewell, C. M. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.115122 · Cited by 18

Transition metals and host-microbe interactions in the inflamed intestine

Zhu, W., Spiga, L., & Winter, S. (2019) · BioMetals · doi:10.1007/s10534-019-00182-8 · Cited by 17

Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase

Bender, D. A., Kaczmarek, A. T., Niks, D., Hille, R., & Schwarz, G. (2019) · Biochemical Journal · doi:10.1042/bcj20190143 · Cited by 18

Epigenetic Effects of Dietary Trace Elements

Lau, A. T. Y., Tan, H. W., & Xu, Y. (2017) · Current Pharmacology Reports · doi:10.1007/s40495-017-0098-x · Cited by 19

9. Molybdenum and Tungsten Cofactors and the Reactions They Catalyze

Kirk, M. L., & Khadanand, K. C. (2020) · De Gruyter eBooks · doi:10.1515/9783110589757-015 · Cited by 17

Chemical Information in the L3 X-ray Absorption Spectra of Molybdenum Compounds by High-Energy-Resolution Detection and Density Functional Theory

Svyazhin, A., Nalbandyan, V. B., Rovezzi, M., Chumakova, A., Detlefs, B., Guda, A. A., Santambrogio, A., Manceau, A., & Glatzel, P. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c02600 · Cited by 15

Enrichment mechanisms of Mo in soil in the karst region Guangxi, China

Lin, K., Yang, Z., Yu, T., Ji, W., Liu, X., Li, B., Wu, Z., Li, X., Ma, X., Wang, L., et al. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.114808 · Cited by 14

Microporous surface containing flower-like molybdenum disulfide submicro-spheres of sulfonated polyimide with antibacterial effect and promoting bone regeneration and osteointegration

Kaewmanee, R., Wang, F., Pan, Y., Mei, S., Meesane, J., Li, F., Wu, Z., & Wei, J. (2022) · Biomaterials Science · doi:10.1039/d2bm00622g · Cited by 14

Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis

Burgmayer, S. J. N., & Kirk, M. L. (2023) · Molecules · doi:10.3390/molecules28227456 · Cited by 16

S-Sulfocysteine Induces Seizure-Like Behaviors in Zebrafish

Plate, J., Sassen, W. A., Hassan, A. H., Lehne, F., Köster, R. W., & Kruse, T. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00122 · Cited by 14

The Role of the Pyranopterin Dithiolene Component of Moco in Molybdoenzyme Catalysis

Burgmayer, S. J. N., & Kirk, M. L. (2019) · Structure and bonding · doi:10.1007/430_2019_31 · Cited by 14

Sulfite Impairs Bioenergetics and Redox Status in Neonatal Rat Brain: Insights into the Early Neuropathophysiology of Isolated Sulfite Oxidase and Molybdenum Cofactor Deficiencies

Pramio, J., Grings, M., da Rosa, A. G., Ribeiro, R. T., Glänzel, N. M., Signori, M. F., Marcuzzo, M. B., Bobermin, L. D., Wyse, Â. T. D. S., Quincozes‐Santos, A., et al. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01328-6 · Cited by 13

A systematic analysis of diet-induced nephroprotection reveals overlapping changes in cysteine catabolism

Koehler, F. C., Fu, C.-Y., Späth, M. R., Hoyer-Allo, K. J. R., Bohl, K., Göbel, H., Lackmann, J., Grundmann, F., Osterholt, T., Gloistein, C., et al. (2022) · Translational research · doi:10.1016/j.trsl.2022.02.003 · Cited by 15

Whole exome sequencing identified a homozygous novel mutation in SUOX gene causes extremely rare autosomal recessive isolated sulfite oxidase deficiency

Zhang, R., Hao, Y., Xu, Y. C., Qin, J., Wang, Y., Dey, S. K., Li, C., Wang, H., & Banerjee, S. (2022) · Clinica Chimica Acta · doi:10.1016/j.cca.2022.06.005 · Cited by 13

Functional Complementation Studies Reveal Different Interaction Partners of Escherichia coli IscS and Human NFS1

Bühning, M., Friemel, M., & Leimkühler, S. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00627 · Cited by 13

Selective Oxyfunctionalisation Reactions Driven by Sulfite Oxidase‐Catalysed In Situ Generation of H2O2

van Schie, M. M. C. H., Kaczmarek, A. T., Tieves, F., de Santos, P. G., Paul, C. E., Arends, I. W. C. E., Alcalde, M., Schwarz, G., & Hollmann, F. (2020) · ChemCatChem · doi:10.1002/cctc.201902297 · Cited by 12

8-Hydroxyquinoline-2-Carboxylic Acid as Possible Molybdophore: A Multi-Technique Approach to Define Its Chemical Speciation, Coordination and Sequestering Ability in Aqueous Solution

Arena, K., Brancato, G., Cacciola, F., Crea, F., Cataldo, S., Stefano, C. D., Gama, S., Lando, G., Milea, D., Mondello, L., et al. (2020) · Biomolecules · doi:10.3390/biom10060930 · Cited by 12

A defect in molybdenum cofactor binding causes an attenuated form of sulfite oxidase deficiency

Kaczmarek, A. T., Bender, D. A., Gehling, T., Kohl, J. B., Daimagüler, H., Santamaria‐Araujo, J. A., Liebau, M. C., Koy, A., Çırak, S., & Schwarz, G. (2021) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12454 · Cited by 12

EPR Spectroscopy on Mononuclear Molybdenum-Containing Enzymes

Maia, L. B., Moura, I., & Moura, J. J. G. (2017) · Biological magnetic resonance · doi:10.1007/978-3-319-59100-1_4 · Cited by 11

Oxygen and nitrite reduction by heme‐deficient sulphite oxidase in a patient with mild sulphite oxidase deficiency

Bender, D. A., Kaczmarek, A. T., Kuester, S., Burlina, A., & Schwarz, G. (2020) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12216 · Cited by 10

Machine learning-based identification and characterization of 15 novel pathogenic SUOX missense mutations

Kaczmarek, A. T., Bahlmann, N., Thaqi, B., May, P., & Schwarz, G. (2021) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2021.07.011 · Cited by 10

Rhodanese-Fold Containing Proteins in Humans: Not Just Key Players in Sulfur Trafficking

Alsohaibani, R., Claudel, A.-L., Perchat-Varlet, R., Boutserin, S., Talfournier, F., Boschi‐Müller, S., & Selles, B. (2023) · Antioxidants · doi:10.3390/antiox12040843 · Cited by 9

Exploring the nature’s discriminating factors behind the selection of molybdoenzymes and tungstoenzymes depending on the biological environment

Das, U., Das, A., & Das, A. K. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.216290 · Cited by 8

Mineral and Amino Acid Profiling of Different Hematopoietic Populations from the Mouse Bone Marrow

Girotra, M., Monnard, C., Konz, T., Sizzano, F., Goulet, L., Godin, J., Coukos, G., Rezzi, S., & Vannini, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176444 · Cited by 9

The levels, single and multiple health risk assessment of 23 metals in enteral nutrition formulas

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