Program DYNAFIT for the Analysis of Enzyme Kinetic Data: Application to HIV Proteinase

The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition

Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355

A PHGDH inhibitor reveals coordination of serine synthesis and one-carbon unit fate

Pacold, M. E., Brimacombe, K. R., Chan, S. H., Rohde, J. M., Lewis, C. A., Swier, L. J. Y. M., Possemato, R., Chen, W. W., Sullivan, L. B., Fiske, B. P., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2070 · Cited by 553

The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2

Fischbach, M. A., Lin, H., Zhou, L., Yu, Y., Abergel, R. J., Liu, D. R., Raymond, K. N., Wanner, B. L., Strong, R. K., Walsh, C. T., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604636103 · Cited by 319

Iron traffics in circulation bound to a siderocalin (Ngal)–catechol complex

Bao, G., Clifton, M., Hoette, T. M., Mori, K., Deng, S.-X., Qiu, A., Viltard, M., Williams, D., Paragas, N., Leete, T., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.402 · Cited by 307

The Mad2 spindle checkpoint protein has two distinct natively folded states

Luo, X., Tang, Z., Xia, G., Wassmann, K., Matsumoto, T., Rizo, J., & Yu, H. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb748 · Cited by 297

Novel metaheuristic for parameter estimation in nonlinear dynamic biological systems

Rodriguez-Fernandez, M., Egea, J. A., & Banga, J. R. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-483 · Cited by 278

Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance

Schwartz, P. A., Kuzmic, P., Solowiej, J., Bergqvist, S., Bolanos, B., Almaden, C., Nagata, A., Ryan, K., Feng, J., Dalvie, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313733111 · Cited by 281

Anthrax pathogen evades the mammalian immune system through stealth siderophore production

Abergel, R. J., Wilson, M. K., Arceneaux, J. E. L., Hoette, T. M., Strong, R. K., Byers, B. R., & Raymond, K. N. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607055103 · Cited by 198

Rac1 GTPase activates the WAVE regulatory complex through two distinct binding sites

Chen, B., Chou, H.-T., Brautigam, C. A., Xing, W., Yang, S., Henry, L., Doolittle, L. K., Walz, T., & Rosen, M. K. (2017) · eLife · doi:10.7554/elife.29795 · Cited by 173

The Response of Acinetobacter baumannii to Zinc Starvation

Nairn, B. L., Lonergan, Z. R., Wang, J., Braymer, J. J., Zhang, Y., Calcutt, M. W., Lisher, J. P., Gilston, B. A., Chazin, W. J., de Crécy-Lagard, V., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.05.007 · Cited by 148

Bacterial sensors define intracellular free energies for correct enzyme metalation

Osman, D., Martini, M. A., Foster, A. W., Chen, J., Scott, A. J. P., Morton, R. J., Steed, J. W., Lurie-Luke, E., Huggins, T. G., Lawrence, A. D., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-018-0211-4 · Cited by 147

The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects

Johnson, C. W., Reid, D., Parker, J. A., Salter, S., Knihtila, R., Kuzmic, P., & Mattos, C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778886 · Cited by 133

Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc homeostasis

Weiss, A., Murdoch, C. C., Edmonds, K. A., Jordan, M. R., Monteith, A. J., Perera, Y. R., Rodríguez Nassif, A. M., Petoletti, A. M., Beavers, W. N., Munneke, M. J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.04.011 · Cited by 113

Control of Copper Resistance and Inorganic Sulfur Metabolism by Paralogous Regulators in Staphylococcus aureus

Grossoehme, N., Kehl-Fie, T. E., Ma, Z., Adams, K. W., Cowart, D. M., Scott, R. A., Skaar, E. P., & Giedroc, D. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220012 · Cited by 101

Sequential binding and sensing of Zn(II) by Bacillus subtilis Zur

Ma, Z., Gabriel, S. E., & Helmann, J. D. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr625 · Cited by 98

A new structural paradigm in copper resistance in Streptococcus pneumoniae

Fu, Y., Tsui, H.-C. T., Bruce, K. E., Sham, L.-T., Higgins, K. A., Lisher, J. P., Kazmierczak, K. M., Maroney, M. J., Dann, C. E., Winkler, M. E., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1168 · Cited by 93

Isoform-Specific Destabilization of the Active Site Reveals a Molecular Mechanism of Intrinsic Activation of KRas G13D

Johnson, C. W., Lin, Y.-J., Reid, D., Parker, J., Pavlopoulos, S., Dischinger, P., Graveel, C., Aguirre, A. J., Steensma, M., Haigis, K. M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.026 · Cited by 89

An Acinetobacter baumannii, Zinc-Regulated Peptidase Maintains Cell Wall Integrity during Immune-Mediated Nutrient Sequestration

Lonergan, Z. R., Nairn, B. L., Wang, J., Hsu, Y.-P., Hesse, L. E., Beavers, W. N., Chazin, W. J., Trinidad, J. C., VanNieuwenhze, M. S., Giedroc, D. P., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.089 · Cited by 76

Origins of specificity and cross‐talk in metal ion sensing by Bacillus subtilisFur

Ma, Z., Faulkner, M. J., & Helmann, J. D. (2012) · Molecular Microbiology · doi:10.1111/mmi.12049 · Cited by 62

Multiple steps determine the overall rate of the reduction of 5α-dihydrotestosterone catalyzed by human type 3 3α-hydroxysteroid dehydrogenase: implications for the elimination of androgens

Jin, Y., & Penning, T. M. (2006) · Biochemistry · doi:10.1021/bi060591r · Cited by 60

Fine control of metal concentrations is necessary for cells to discern zinc from cobalt

Osman, D., Foster, A. W., Chen, J., Svedaite, K., Steed, J. W., Lurie-Luke, E., Huggins, T. G., & Robinson, N. J. (2017) · Nature Communications · doi:10.1038/s41467-017-02085-z · Cited by 58

Design of Gallinamide A Analogs as Potent Inhibitors of the Cysteine Proteases Human Cathepsin L and Trypanosoma cruzi Cruzain

Boudreau, P. D., Miller, B. W., McCall, L.-I., Almaliti, J., Reher, R., Hirata, K., Le, T., Siqueira-Neto, J. L., Hook, V., & Gerwick, W. H. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00294 · Cited by 57

YeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasis

Blaby-Haas, C. E., Flood, J. A., Crécy-Lagard, V. D., & Zamble, D. B. (2012) · Metallomics · doi:10.1039/c2mt20012k · Cited by 54

Comprehensive Experimental and Computational Analysis of Binding Energy Hot Spots at the NF-κB Essential Modulator/IKKβ Protein–Protein Interface

Golden, M. S., Cote, S. M., Sayeg, M., Zerbe, B. S., Villar, E. A., Beglov, D., Sazinsky, S. L., Georgiadis, R. M., Vajda, S., Kozakov, D., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja400914z · Cited by 47

SNAP-tag2 for faster and brighter protein labeling

Kühn, S., Nasufovic, V., Wilhelm, J., Kompa, J., de Lange, E. M. F., Lin, Y.-H., Egoldt, C., Fischer, J., Lennoi, A., Tarnawski, M., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01942-z · Cited by 44

The zinc efflux activator Scz A protects Streptococcus pneumoniae serotype 2 D 39 from intracellular zinc toxicity

Martin, J. E., Edmonds, K. A., Bruce, K. E., Campanello, G. C., Eijkelkamp, B. A., Brazel, E. B., McDevitt, C. A., Winkler, M. E., & Giedroc, D. P. (2017) · Molecular Microbiology · doi:10.1111/mmi.13654 · Cited by 38

Cofactor Specificity of Glucose-6-Phosphate Dehydrogenase Isozymes in Pseudomonas putida Reveals a General Principle Underlying Glycolytic Strategies in Bacteria

Volke, D. C., Olavarría, K., & Nikel, P. I. (2021) · mSystems · doi:10.1128/msystems.00014-21 · Cited by 42

Deterministic global optimization algorithm based on outer approximation for the parameter estimation of nonlinear dynamic biological systems

Miró, A., Pozo, C., Guillén-Gosálbez, G., Egea, J. A., & Jiménez, L. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-90 · Cited by 41

Mechanistic Insights into the Metal-Dependent Activation of ZnII-Dependent Metallochaperones

Jordan, M. R., Wang, J., Weiss, A., Skaar, E. P., Capdevila, D. A., & Giedroc, D. P. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01173 · Cited by 39

Immune Interference in Mycobacterium tuberculosis Intracellular Iron Acquisition through Siderocalin Recognition of Carboxymycobactins

Hoette, T. M., Clifton, M. C., Zawadzka, A. M., Holmes, M. A., Strong, R. K., & Raymond, K. N. (2011) · ACS Chemical Biology · doi:10.1021/cb200331g · Cited by 31

Glutathione-complexed [2Fe-2S] clusters function in Fe–S cluster storage and trafficking

Fidai, I., Wachnowsky, C., & Cowan, J. A. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1387-2 · Cited by 29

Understanding the molecular basis of multiple mitochondrial dysfunctions syndrome 1 (MMDS1)—impact of a disease-causing Gly208Cys substitution on structure and activity of NFU1 in the Fe/S cluster biosynthetic pathway

Wachnowsky, C., Wesley, N. A., Fidai, I., & Cowan, J. A. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.01.021 · Cited by 25

Structural basis for Retriever-SNX17 assembly and endosomal sorting

Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54583-6 · Cited by 23

Fpa (YlaN) is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in Staphylococcus aureus

Boyd, J. M., Ryan Kaler, K., Esquilín-Lebrón, K., Pall, A., Campbell, C. J., Foley, M. E., Rios-Delgado, G., Mustor, E. M., Stephens, T. G., Bovermann, H., et al. (2024) · mBio · doi:10.1128/mbio.02310-24 · Cited by 14

Characterization of the Zinc Uptake Repressor (Zur) from Acinetobacter baumannii

Kim, M., Le, M. T., Fan, L., Campbell, C., Sen, S., Capdevila, D. A., Stemmler, T. L., & Giedroc, D. P. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00679 · Cited by 8

The intrinsically disordered cytoplasmic tail of a dendrite branching receptor uses two distinct mechanisms to regulate the actin cytoskeleton

Kramer, D. A., Narvaez-Ortiz, H. Y., Patel, U., Shi, R., Shen, K., Nolen, B. J., Roche, J., & Chen, B. (2023) · eLife · doi:10.7554/elife.88492 · Cited by 7

Bottom-up parameterization of enzyme rate constants: Reconciling inconsistent data

Zielinski, D. C., Matos, M. R. A., de Bree, J. E., Glass, K., Sonnenschein, N., & Palsson, B. O. (2024) · Metabolic Engineering Communications · doi:10.1016/j.mec.2024.e00234 · Cited by 6

YlaN is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in Staphylococcus aureus

Boyd, J. M., Esquilín-Lebrón, K., Campbell, C. J., Kaler, K. R., Norambuena, J., Foley, M. E., Stephens, T. G., Rios, G., Mereddy, G., Zheng, V., et al. (2023) · doi:10.1101/2023.10.03.560778 · Cited by 4

A De Novo Designed Protein with Versatile Metal Binding and Tunable Hydrolytic Activity

Hoffnagle, A. M., Srisantitham, S., Neeley, M., Tsai, C.-Y., & Tezcan, F. A. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00259 · Cited by 4

Archaeoglobus fulgidus CbiX S is a Cobalt Chelatase Where Co(II) is Ligated by His10 and His74

Morris, J. A., Ayodele-Davis, O. O. E., Lavigne, M. E., Martorelli Di Genova, B., & Liptak, M. D. (2026) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6c00056 · Cited by 3