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 · see citing works

The Mononuclear Molybdenum Enzymes

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

Molybdenum cofactors, enzymes and pathways

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

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 · see citing works

Gephyrin: a master regulator of neuronal function?

Tyagarajan, S. K., & Fritschy, J. (2014) · Nature reviews. Neuroscience · doi:10.1038/nrn3670 · Cited by 425 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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

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

Nitrite Reductase and Nitric-oxide Synthase Activity of the Mitochondrial Molybdopterin Enzymes mARC1 and mARC2

Sparacino-Watkins, C. E., Tejero, J., Sun, B., Gauthier, M. C., Thomas, J., Ragireddy, V., Merchant, B. A., Wang, J., Azarov, I., Basu, P., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.555177 · Cited by 169 · see citing works

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 162 · see citing works

Efficacy and safety of cyclic pyranopterin monophosphate substitution in severe molybdenum cofactor deficiency type A: a prospective cohort study

Schwahn, B., van Spronsen, F. J., Belaidi, A. A., Bowhay, S., Christodoulou, J., Derks, T. G. J., Hennermann, J. B., Jameson, E., König, K., McGregor, T. L., et al. (2015) · The Lancet · doi:10.1016/s0140-6736(15)00124-5 · Cited by 146 · see citing works

A Mechanism of Sulfite Neurotoxicity

Zhang, X., Vincent, A. S., Halliwell, B. B., & Wong, K. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402759200 · Cited by 141 · see citing works

Mutations Associated with Functional Disorder of Xanthine Oxidoreductase and Hereditary Xanthinuria in Humans

Ichida, K., Amaya, Y., Okamoto, K., & Nishino, T. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131115475 · Cited by 119 · see citing works

The biosynthesis of the molybdenum cofactors

Mendel, R. R., & Leimkühler, S. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1173-y · Cited by 115 · see citing works

Glycyl radical activating enzymes: Structure, mechanism, and substrate interactions

Shisler, K. A., & Broderick, J. B. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.01.020 · Cited by 102 · see citing works

Rescue of lethal molybdenum cofactor deficiency by a biosynthetic precursor from Escherichia coli

Schwarz, G. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh136 · Cited by 98 · see citing works

The First Mammalian Aldehyde Oxidase Crystal Structure

Coelho, C., Mahro, M., Trincão, J., Carvalho, A. T. P., Ramos, M. J., Terao, M., Garattini, E., Leimkühler, S., & Romão, M. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390419 · Cited by 91 · see citing works

The Tetrahydropyranopterin Structure of the Sulfur-free and Metal-free Molybdenum Cofactor Precursor

Santamaria‐Araujo, J. A., Fischer, B., Otte, T., Nimtz, M., Mendel, R. R., Wray, V., & Schwarz, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311815200 · Cited by 89 · see citing works

Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases

Maia, L. B., & Moura, J. J. G. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1234-2 · Cited by 86 · see citing works

Molybdenum in Human Health and Disease

Schwarz, G., & Belaidi, A. A. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_13 · Cited by 86 · see citing works

Identification of a Cyclic Nucleotide as a Cryptic Intermediate in Molybdenum Cofactor Biosynthesis

Hover, B. M., Loksztejn, A., Ribeiro, A. A., & Yokoyama, K. (2013) · Journal of the American Chemical Society · doi:10.1021/ja401781t · Cited by 85 · see citing works

Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide

Wang, J., Krizowski, S., Fischer-Schrader, K., Niks, D., Tejero, J., Sparacino-Watkins, C., Wang, L., Ragireddy, V., Frizzell, S., Kelley, E. E., et al. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5397 · Cited by 84 · see citing works

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Fräsdorf, B., Radon, C., & Leimkühler, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.605733 · Cited by 82 · see citing works

The Mitochondrial Amidoxime-reducing Component (mARC1) Is a Novel Signal-anchored Protein of the Outer Mitochondrial Membrane

Klein, J. M., Busch, J. D., Potting, C., Baker, M. J., Langer, T., & Schwarz, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419424 · Cited by 79 · see citing works

The mammalian molybdenum enzymes of mARC

Ott, G., Havemeyer, A., & Clement, B. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1216-4 · Cited by 76 · see citing works

Molybdenum cofactor-deficient mice resemble the phenotype of human patients

Lee, H. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.26.3309 · Cited by 70 · see citing works

Aldehyde oxidase and its importance in novel drug discovery: present and future challenges

Garattini, E., & Terao, M. (2013) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2013.788497 · Cited by 68 · see citing works

The fourth mammalian molybdenum enzyme mARC: current state of research

Havemeyer, A., Lang, J., & Clement, B. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.608682 · Cited by 67 · see citing works

Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis

Hover, B. M., Tonthat, N. K., Schumacher, M. A., & Yokoyama, K. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500697112 · Cited by 60 · see citing works

Molybdenum cofactor deficiency: Review of 12 cases (MoCD and review)

Bayram, E., Topçu, Y., Karakaya, P., Yiş, U., Çakmakçı, H., Ichida, K., & Kurul, S. H. (2012) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2012.10.003 · Cited by 60 · see citing works

Exonic microdeletions of the gephyrin gene impair GABAergic synaptic inhibition in patients with idiopathic generalized epilepsy

Dejanovic, B., Lal, D., Catarino, C. B., Arjune, S., Belaidi, A. A., Trucks, H., Vollmar, C., Surges, R., Kunz, W. S., Motameny, S., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.02.001 · Cited by 58 · see citing works

Metal insertion into the molybdenum cofactor: product–substrate channelling demonstrates the functional origin of domain fusion in gephyrin

Belaidi, A. A., & Schwarz, G. (2012) · Biochemical Journal · doi:10.1042/bj20121078 · Cited by 58 · see citing works

Ultra-orphan diseases: a quantitative analysis of the natural history of molybdenum cofactor deficiency

Mechler, K., Mountford, W. K., Hoffmann, G. F., & Ries, M. (2015) · Genetics in Medicine · doi:10.1038/gim.2015.12 · Cited by 58 · see citing works

Modern diagnostic approach to hereditary xanthinuria

Mraz, M., Hurba, O., Bártl, J., Doležel, Z., Marinaki, A. M., Fairbanks, L. D., & Stibůrková, B. (2014) · Urolithiasis · doi:10.1007/s00240-014-0734-4 · Cited by 54 · see citing works

The Involvement of Mitochondrial Amidoxime Reducing Components 1 and 2 and Mitochondrial Cytochrome b5 in N-Reductive Metabolism in Human Cells

Plitzko, B., Ott, G., Reichmann, D., Henderson, C. J., Wolf, C. R., Mendel, R. R., Bittner, F., Clement, B., & Havemeyer, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.474916 · Cited by 51 · see citing works

Sulphur shuttling across a chaperone during molybdenum cofactor maturation

Arnoux, P., Ruppelt, C., Oudouhou, F., Lavergne, J., Siponen, M. I., Toci, R., Mendel, R. R., Bittner, F., Pignol, D., Magalon, A., et al. (2015) · Nature Communications · doi:10.1038/ncomms7148 · Cited by 49 · see citing works

Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways

Klein, J. M., & Schwarz, G. (2012) · Journal of Cell Science · doi:10.1242/jcs.110114 · Cited by 49 · see citing works

Simultaneous impairment of neuronal and metabolic function of mutated gephyrin in a patient with epileptic encephalopathy

Dejanovic, B., Djémié, T., Grünewald, N., Suls, A., Kress, V., Hetsch, F., Craiu, D., Zemel, M., Gormley, P., Lal, D., et al. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201505323 · Cited by 49 · see citing works

Catalysis of a New Ribose Carbon-Insertion Reaction by the Molybdenum Cofactor Biosynthetic Enzyme MoaA

Mehta, A. P., Hanes, J. W., Abdelwahed, S. H., Hilmey, D. G., Hänzelmann, P., & Begley, T. P. (2013) · Biochemistry · doi:10.1021/bi3016026 · Cited by 45 · see citing works

Neurodegeneration in Huntington's disease involves loss of cystathionine γ-lyase

Paul, B. D., & Snyder, S. H. (2014) · Cell Cycle · doi:10.4161/15384101.2014.950538 · Cited by 43 · see citing works

Substrate Orientation and Specificity in Xanthine Oxidase: Crystal Structures of the Enzyme in Complex with Indole-3-acetaldehyde and Guanine

Cao, H., Hall, J. E., & Hille, R. (2014) · Biochemistry · doi:10.1021/bi401465u · Cited by 40 · see citing works

A GPHN point mutation leading to molybdenum cofactor deficiency

Reiss, J., Lenz, U., Acquaviva, C., Joriot-Chekaf, S., Mention-Mulliez, K., & Holder‐Espinasse, M. (2011) · Clinical Genetics · doi:10.1111/j.1399-0004.2011.01709.x · Cited by 36 · see citing works

Metabolic stroke in a late-onset form of isolated sulfite oxidase deficiency

Rizzo, M. D., Burlina, A. P., Sass, J. O., Beermann, F., Zanco, C., Cazzorla, C., Bordugo, A., Giordano, L., Manara, R., & Burlina, A. (2013) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2013.01.011 · Cited by 34 · see citing works

Synthesis of Cyclic Pyranopterin Monophosphate, a Biosynthetic Intermediate in the Molybdenum Cofactor Pathway

Clinch, K., Watt, D. K., Dixon, R., Baars, S. M., Gainsford, G. J., Tiwari, A., Schwarz, G., Saotome, Y., Storek, M., Belaidi, A. A., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301855r · Cited by 32 · see citing works

Expression and Function of mARC: Roles in Lipogenesis and Metabolic Activation of Ximelagatran

Neve, E. P. A., Köfeler, H. C., Hendriks, D. F. G., Nordling, Å., Gogvadze, V. G., Mkrtchian, S., Näslund, E. B., & Ingelman‐Sundberg, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138487 · Cited by 31 · see citing works

Structure and stability of the molybdenum cofactor intermediate cyclic pyranopterin monophosphate

Santamaria‐Araujo, J. A., Wray, V., & Schwarz, G. (2011) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-011-0835-2 · Cited by 30 · see citing works

Molybdenum Cofactor Deficiency: A New HPLC Method for Fast Quantification of S-Sulfocysteine in Urine and Serum

Belaidi, A. A., Arjune, S., Santamaria‐Araujo, J. A., Sass, J. O., & Schwarz, G. (2011) · JIMD Reports · doi:10.1007/8904_2011_89 · Cited by 29 · see citing works

Oxygen reactivity of mammalian sulfite oxidase provides a concept for the treatment of sulfite oxidase deficiency

Belaidi, A. A., Roeper, J., Arjune, S., Krizowski, S., Trifunović, A., & Schwarz, G. (2015) · Biochemical Journal · doi:10.1042/bj20140768 · Cited by 29 · see citing works

Molybdenum cofactor deficiency presenting with a parkinsonism‐dystonia syndrome

Alkufri, F., Harrower, T., Rahman, Y., Hughes, E., Mundy, H. R., Knibb, J. A., Moriarty, J., Connor, S. E. J., & Samuel, M. (2013) · Movement Disorders · doi:10.1002/mds.25276 · Cited by 25 · see citing works

C-Terminal Glycine-Gated Radical Initiation by GTP 3′,8-Cyclase in the Molybdenum Cofactor Biosynthesis

Hover, B. M., & Yokoyama, K. (2015) · Journal of the American Chemical Society · doi:10.1021/ja512997j · Cited by 21 · see citing works

In vitro evidence that sulfite impairs glutamatergic neurotransmission and inhibits glutathione metabolism‐related enzymes in rat cerebral cortex

Parmeggiani, B., Moura, A. P., Grings, M., Bumbel, A. P., Alvorcem, L. D. M., Pletsch, J. T., Fernandes, C. G., Wyse, Â. T. D. S., Wajner, M., & Leipnitz, G. (2015) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2015.03.005 · Cited by 19 · see citing works

Molybdenum Cofactor Deficiency: Metabolic Link Between Taurine and S-Sulfocysteine

Belaidi, A. A., & Schwarz, G. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-6093-0_2 · Cited by 15 · see citing works

Mechanistic Investigation of cPMP Synthase in Molybdenum Cofactor Biosynthesis Using an Uncleavable Substrate Analogue

Hover, B. M., Lilla, E. A., & Yokoyama, K. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00857 · Cited by 15 · see citing works

Dextrometorphan in molybdenum cofactor deficiency

Kurlemann, G., Debus, O., & Schuierer, G. R. (1996) · European Journal of Pediatrics · doi:10.1007/bf01955280 · Cited by 13 · see citing works

Isolated sulfite oxidase deficiency

Relinque, B., Bardallo, L., Asencio, M. G., Jiménez, P. J., & Luna, S. A. (2015) · Journal of Neonatal-Perinatal Medicine · doi:10.3233/npm-15814029 · Cited by 13 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 250 · see citing works

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 230 · see citing works

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 · see citing works

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 · see citing works

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 86 · see citing works

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 75 · see citing works

Nitrite‐dependent nitric oxide synthesis by molybdenum enzymes

Bender, D. A., & Schwarz, G. (2018) · FEBS Letters · doi:10.1002/1873-3468.13089 · Cited by 73 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Molybdenum Cofactor Deficiency in Humans

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

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 59 · see citing works

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 57 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 46 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 38 · see citing works

Shared function and moonlighting proteins in molybdenum cofactor biosynthesis

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Compositional determinants of fruit and vegetable quality and nutritional value

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