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Spatially Resolved Elemental Analysis, Spectroscopy and Diffraction at the GSECARS Sector at the Advanced Photon Source

Sutton, S. R., Lanzirotti, A., Newville, M. G., Rivers, M. L., Eng, P. J., & Lefticariu, L. (2017) · Journal of Environmental Quality · doi:10.2134/jeq2016.10.0401 · Cited by 34 · see citing works

Focal adhesion kinase tyrosine phosphorylation is associated with myogenesis and modulated by insulin

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Brg1 Controls the Expression of Pax7 to Promote Viability and Proliferation of Mouse Primary Myoblasts

Padilla‐Benavides, T., Nasipak, B. T., & Imbalzano, A. N. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25031 · Cited by 32 · see citing works

Periplasmic response upon disruption of transmembrane Cu transport in Pseudomonas aeruginosa

Raimunda, D., Padilla‐Benavides, T., Vogt, S., Boutigny, S., Tomkinson, K. N., Finney, L. A., & ARGÜELLO, J. M. (2013) · Metallomics · doi:10.1039/c2mt20191g · Cited by 31 · see citing works

Differential expression of zinc transporters accompanies the differentiation of C2C12 myoblasts

Paskavitz, A. L., Quintana, J., Cangussu, D., Tavera‐Montañez, C., Xiao, Y., Ortiz‐Miranda, S., Navea, J. G., & Padilla‐Benavides, T. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.04.024 · Cited by 31 · see citing works

ZIP11 Regulates Nuclear Zinc Homeostasis in HeLa Cells and Is Required for Proliferation and Establishment of the Carcinogenic Phenotype

Olea‐Flores, M., Kan, J., Carlson, A., Syed, S. A., McCann, C., Mondal, V., Szady, C., Ricker, H. M., McQueen, A., Navea, J. G., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.895433 · Cited by 31 · see citing works

Lumenal Loop M672-P707 of the Menkes Protein (ATP7A) Transfers Copper to Peptidylglycine Monooxygenase

Otoikhian, A. A., Barry, A. N., Mayfield, M. B., Nilges, M. J., Huang, Y., Lutsenko, S., & Blackburn, N. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja301221s · Cited by 30 · see citing works

The absence of MyoD in regenerating skeletal muscle affects the expression pattern of basement membrane, interstitial matrix and integrin molecules that is consistent with delayed myotube formation

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Identifying metalloproteins through X-ray fluorescence mapping and mass spectrometry

Raimunda, D., Khare, T., Giometti, C. S., Vogt, S., ARGÜELLO, J. M., & Finney, L. A. (2012) · Metallomics · doi:10.1039/c2mt20095c · Cited by 23 · see citing works

Ouabain Enhances Cell-Cell Adhesion Mediated by β1 Subunits of the Na+,K+-ATPase in CHO Fibroblasts

Vilchis-Nestor, C. A., Roldán, M. L., Leonardi, A., Navea, J. G., Padilla‐Benavides, T., & Shoshani, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092111 · Cited by 21 · see citing works

Dramatic Electronic Perturbations of CuA Centers via Subtle Geometric Changes

Leguto, A. J., Smith, M. A., Morgada, M. N., Zitare, U. A., Murgida, D. H., Lancaster, K. M., & Vila, A. J. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b12335 · Cited by 15 · see citing works

Introduction to Human Disorders of Copper Metabolism

Graper, M. L., Hüster, D., Kaler, S. G., Lutsenko, S., Schilsky, M. L., & Thiele, D. J. (2014) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12448 · Cited by 15 · see citing works

Atomic Absorbance Spectroscopy to Measure Intracellular Zinc Pools in Mammalian Cells

Gordon, S. J. V., Xiao, Y., Paskavitz, A. L., Navarro‐Tito, N., Navea, J. G., & Padilla‐Benavides, T. (2019) · Journal of Visualized Experiments · doi:10.3791/59519 · Cited by 11 · see citing works

Assay of Copper Transfer and Binding to P1B-ATPases

Padilla‐Benavides, T., & ARGÜELLO, J. M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3179-8_24 · Cited by 4 · see citing works

Mammalian copper homeostasis: physiological roles and molecular mechanisms

Lutsenko, S., Roy, S., & Tsvetkov, P. (2024) · Physiological Reviews · doi:10.1152/physrev.00011.2024 · Cited by 206 · see citing works

The molecular mechanism and therapeutic landscape of copper and cuproptosis in cancer

Guo, Z., Chen, D., Yao, L., Sun, Y., Li, D., Le, J., Dian, Y., Zeng, F., Chen, X., & Deng, G. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02192-0 · Cited by 201 · see citing works

Copper homeostasis and cuproptosis in cancer immunity and therapy

Liu, W., Lin, W., Li, Y., Xu, W., & Yang, J. H. (2023) · Immunological Reviews · doi:10.1111/imr.13276 · Cited by 175 · see citing works

The physiological and pathophysiological roles of copper in the nervous system

Gale, J. R., & Aizenman, E. (2024) · European Journal of Neuroscience · doi:10.1111/ejn.16370 · Cited by 80 · see citing works

Copper homeostasis and copper-induced cell death in tumor immunity: implications for therapeutic strategies in cancer immunotherapy

Zhang, S., Huang, Q., Ji, T., Li, Q., & Hu, C. (2024) · Biomarker Research · doi:10.1186/s40364-024-00677-8 · Cited by 53 · see citing works

Cuproptosis and its potential role in musculoskeletal disease

Xiang, Z., Mei, H., Wang, H., Yao, X., Rao, J., Zhang, W., Xu, A., & Lü, L. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1570131 · Cited by 23 · see citing works

Cuproptosis: Current insights into its multifaceted role in disease, cancer, and translational/therapeutic opportunities

Boaru, D. L., León-Oliva, D. D., Castro-Martinez, P. D., Montero, C. G., Fraile‐Μartinez, O., García-González, B., Pérez-González, I., Alhaddadin, M. N. M., Barrena-Blázquez, S., López-González, L., et al. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118422 · Cited by 23 · see citing works

Exploring Copper’s role in stroke: progress and treatment approaches

Peng, G., Huang, Y., Xie, G., & Tang, J. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1409317 · Cited by 21 · see citing works

Roles of Copper Transport Systems Members in Breast Cancer

Chen, Y., Li, C., Li, M., & Han, B. (2024) · Cancer Medicine · doi:10.1002/cam4.70498 · Cited by 18 · see citing works

A primer on copper biology in the brain

Lane, A. R., Roberts, B. R., Fahrni, C. J., & Faúndez, V. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106974 · Cited by 15 · see citing works

Emerging perspectives of copper-mediated transcriptional regulation in mammalian cell development

Fitisemanu, F. M., & Padilla‐Benavides, T. (2024) · Metallomics · doi:10.1093/mtomcs/mfae046 · Cited by 14 · see citing works

Engineered biosynthesis of plant heteroyohimbine and corynantheine alkaloids in Saccharomyces cerevisiae

Dror, M. J., Misa, J., Yee, D. A., Chu, A. M., Yu, R. K., Chan, B. B., Aoyama, L. S., Chaparala, A. P., O'Connor, S. E., & Tang, Y. (2023) · Journal of Industrial Microbiology & Biotechnology · doi:10.1093/jimb/kuad047 · Cited by 12 · see citing works

Identification of immune characteristic biomarkers and therapeutic targets in cuproptosis for sepsis by integrated bioinformatics analysis and single-cell RNA sequencing analysis

Wang, T., Fang, X., Sheng, X., Li, M., Mei, Y., Mei, Q., & Pan, A. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e27379 · Cited by 9 · see citing works

Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation and metal homeostasis

Verdejo-Torres, O., Klein, D. C., Novoa-Aponte, L., Carrazco-Carrillo, J., Bonilla-Pinto, D., Rivera, A., Bakhshian, A., Fitisemanu, F. M., Jiménez-González, M. L., Flinn, L., et al. (2024) · PLOS Genetics · doi:10.1371/journal.pgen.1011495 · Cited by 10 · see citing works

The Oncopig as an Emerging Model to Investigate Copper Regulation in Cancer

Carlson, A. L., Carrazco-Carrillo, J., Loder, A., Elkhadragy, L., Schachtschneider, K., & Padilla-Benavides, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214012 · Cited by 5 · see citing works

The mediating role of inflammatory biomarkers in the association between serum copper and sarcopenia

Zeng, D., Chen, B., Wang, H., Xu, S., Liu, S., Yu, Z., Pan, X., Tang, X., & Qin, Y. (2025) · Scientific Reports · doi:10.1038/s41598-024-84011-0 · Cited by 7 · see citing works

Unveiling the metal-driven death: ferroptosis and cuproptosis in leukemia

Chen, Z., Yu, J., Fu, L., Fu, J., Zhang, Z., Hong, P., & Feng, W. (2025) · European journal of medical research · doi:10.1186/s40001-025-03518-y · Cited by 5 · see citing works

Mechanisms associated with cuproptosis and implications for ovarian cancer

Chen, B., & Liu, J. (2024) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2024.112578 · Cited by 5 · see citing works

Changes in cuproptosis-related gene expression in periodontitis: An integrated bioinformatic analysis

Liu, N., He, Y., Chen, X., Qiu, G., Wu, Y., & Shen, Y. (2024) · Life Sciences · doi:10.1016/j.lfs.2023.122388 · Cited by 5 · see citing works

METTL14-mediated methylation of SLC25A3 mitigates mitochondrial damage in osteoblasts, leading to the improvement of osteoporosis

Wang, P., Zhou, W., Chen, F., Zhang, X., Chen, Y., Zhang, N., & Zhang, Q. (2024) · Experimental Gerontology · doi:10.1016/j.exger.2024.112496 · Cited by 5 · see citing works

Endothelial Cu Uptake Transporter CTR1 Senses Disturbed Flow to Promote Atherosclerosis through CuproptosisPreprint

Varadarajan, S., Xiao, Z., Das, A., Ash, D., Yadav, S., Matier, C. D., Pezacki, A. T., Chatterjee, B., Antipova, O. A., Vogt, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.27.634587 · Cited by 6 · see citing works

Human cytomegalovirus protein UL13 targets to mitochondria to induce cuproptosis

Yang, X., Lei, Y.-L., Zhang, Y., Wang, S., Ren, P., Li, S., & Yi, X.-M. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152330 · Cited by 4 · see citing works

Knockdown of KDM5B Leads to DNA Damage and Cell Cycle Arrest in Granulosa Cells via MTF1

Yang, Y., Cai, Y., Guo, J., Dai, K., Liu, L., Chen, Z., Wang, F., & Deng, M. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45040210 · Cited by 4 · see citing works

Decoding Potential Cuproptosis-Related Genes in Sarcopenia: A Multi-Omics Network Analysis

Yan, H., Shi, L., Li, Y., & Zhang, Z. (2025) · Biology · doi:10.3390/biology14121642 · Cited by 3 · see citing works

Serum-free media for cultivated meat: from cellular mechanisms to cost-effective bioprocess design

Liu, Y., Sun, Y., Song, X., Zhang, R., Qiao, T., Wang, S., Pan, K., Wu, H., Zheng, H., & Xue, C. (2026) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2026.2645261 · Cited by 3 · see citing works

Photocatalytic iron dissolution and speciation in Cu-modified TiO 2 aerosol proxies

Flinn, L., Hambuchen, R., Kazanjian, O., Wilson, N. A., O'Neill, N., Karataikyzy, M., Dis, H. V., Roca, M., & Navea, J. G. (2026) · Environmental Science Atmospheres · doi:10.1039/d6ea00087h · Cited by 1 · see citing works

A new family with a case of severe early-onset muscle fatigue and a peculiar maternally inherited painful swelling in chewing muscles associated with homoplasmic m.15992A>T mutation in mitochondrial tRNAPro

Ghirigato, E., Terenzi, F., Baglivo, M., Zanetti, N., Baldo, F., Murru, F. M., Bobbo, M., Barbi, E., Zeviani, M., Bruno, I., et al. (2023) · Neuromuscular Disorders · doi:10.1016/j.nmd.2023.11.001 · Cited by 1 · see citing works

Neutrophil Depletion Reduced the Relative Abundance of Unsaturated Long‐Chain Fatty Acid Synthesis Microbiota and Intestinal Lipid Absorption

Lu, X., Xu, Y., Liu, Y., Li, F., Feng, Q., Gao, C., Liu, D., Zhou, L., Yang, H., Zhang, J., et al. (2025) · Cell Biochemistry and Function · doi:10.1002/cbf.70060

The PBAF chromatin remodeling complex contributes to metal homeostasis through MTF1 regulation

Carulli, N., Johnston, E. E., Klein, D. C., Verdejo‐Torres, O., Parikh, A., McDaniels, A., Rivera, A., Quinteros, M., Pezacki, A. T., Chang, C. J., et al. (2026) · Metallomics · doi:10.1093/mtomcs/mfag019

Copper deficiency drives OXPHOS impairment and mitochondrial hyperfusion via MTCH2 in skeletal musclePreprint

Lee, Y.-S., Kim, H. S., Nguyen, P. L., Lee, J., Kim, D., Lee, J., Moon, C., Cho, K., Kim, B.-E., Ahn, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.19.688750

Reciprocal regulation between the protein arginine deiminases and mSWI/SNF chromatin remodelers controls skeletal muscle differentiation and regenerationPreprint

Olea‐Flores, M., Sharma, T., Parikh, A., Barasa, L., Hachmer, S., Dilworth, F. J., Padilla‐Benavides, T., Thompson, P. R., & Imbalzano, A. N. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.20.700682

GPR162 Drives Obesity-Associated Lung Adenocarcinoma Suppression via Fatty Acid Oxidation-Induced Cuproptosis and Metabolic-Immune ReprogrammingPreprint

Tao, Y., Long, Y., Wang, W., Cao, C., Li, M. S. C., Li, L., Liu, S., & Xiao, D. (2026) · Research Square · doi:10.21203/rs.3.rs-8754789/v1

Mechanistic insights into hexavalent chromium-induced ferroptosis in mRTECs: a novel MTF1-IREB2-FTH1/DMT1 axis-mediated iron homeostasis dysregulation

Qi, C., Li, M., Yu, Y., Li, J., Xia, Y., Li, L., Cheng, G., Zheng, P., Liu, Y., Zhang, P., et al. (2026) · Journal of Advanced Research · doi:10.1016/j.jare.2026.04.040

Distinct signaling mechanisms and proteome phenotypes are elicited by compartment-specific genetic defects of copper homeostasis

Lane, A. R., Gonzalez, N., Gokhale, A., Zlatic, S. A., Allen, B. M., Scher, N. E., Roberts, A. M., Duong, D. M., Roberts, B. R., Vrailas‐Mortimer, A. D., et al. (2026) · Molecular Biology of the Cell · doi:10.1091/mbc.e26-01-0021

From Metal Stress to Regulated Cell Death: An Evidence Framework for Ferroptosis–Cuproptosis Crosstalk in Cancer

Belbe, A.-A., Pîrlog, L.-M., Sporiș, A., Pitforodeschi, A.-D., Pilatec, A.-N., Băilă, R.-M., Rusu, I., Dobrescu, M. A., Militaru, M.-S., Iordănescu, I. I., et al. (2026) · Cells · doi:10.3390/cells15151421

Balancing cellular copper levels via the post-translational regulation of copper transport

Kirn, L. A., & Burke, R. (2026) · BioMetals · doi:10.1007/s10534-026-00879-7

The role of cuproptosis in periodontitis: Current advances and future perspectives

Shi, Q., Qin, X., Jiang, C., & Zhu, G. (2026) · European Journal Of Oral Sciences · doi:10.1111/eos.70158

Copper transport to mitochondria by SLC25A3 contributes to skeletal myoblast differentiation and is required for survival of differentiated myotubesPreprint

Perez, A. M., Fivush, J. D., Cordill, B. M., Ferguson, N., Zhang, Y., Mezzell, A. T., Mattam, U., Chaudhry, O., Porter, K. G., Maadaadi, S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.03.729837

Abstract 1626: The mitochondrial Cu+ transporter PiC2 (SLC25A3) is a target of MTF1 and contributes to the development of skeletal muscle in vitro

Quinteros, M., Morgada, M. N., Castelblanco, A. R., Davis, E., Hainer, S. J., Vila, A. J., Navea, J. G., & Padilla-Benevides, T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104043

The mammalian phosphate carrier SLC25A3 is a mitochondrial copper transporter required for cytochrome c oxidase biogenesis

Boulet, A., Vest, K. E., Maynard, M. K., Gammon, M. G., Russell, A. C., Mathews, A. T., Cole, S. E., Zhu, X., Phillips, C. B., Kwong, J. Q., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000265 · Cited by 166 · see citing works

Getting out what you put in: Copper in mitochondria and its impacts on human disease

Cobine, P. A., Moore, S. A., & Leary, S. C. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118867 · Cited by 253 · see citing works

Filling the mitochondrial copper pool

Winge, D. R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.h118.001457 · Cited by 8 · see citing works