Mammalian Siderophores, Siderophore-binding Lipocalins, and the Labile Iron Pool

Two to tango: Regulation of Mammalian iron metabolism

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Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron

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Microorganisms pumping iron: anaerobic microbial iron oxidation and reduction

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Siderophore-Based Iron Acquisition and Pathogen Control

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Siderophores: Structure and Function of Microbial Iron Transport Compounds

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

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Microbial Iron Compounds

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Bacterial Iron Sources: From Siderophores to Hemophores

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Enterobactin: an archetype for microbial iron transport.

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Iron withholding: a defense against infection and neoplasia

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Nutritional immunity: the battle for nutrient metals at the host–pathogen interface

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Lipocalin 2: an emerging player in iron homeostasis and inflammation

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Iron transport and its regulation in plants

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Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans

Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306

Diverging roles of bacterial siderophores during infection

Holden, V. I., & Bachman, M. A. (2015) · Metallomics · doi:10.1039/c4mt00333k · Cited by 274

The Role of Iron and Siderophores in Infection, and the Development of Siderophore Antibiotics

Page, M. G. P. (2019) · Clinical Infectious Diseases · doi:10.1093/cid/ciz825 · Cited by 259

Metal limitation and toxicity at the interface between host and pathogen

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The Yin and Yang of copper during infection

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Diverse functional roles of lipocalin-2 in the central nervous system

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Host resistance factor SLC11A1 restricts Salmonella growth through magnesium deprivation

Cunrath, O., & Bumann, D. (2019) · Science · doi:10.1126/science.aax7898 · Cited by 177

“Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels

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The Iron Tug-of-War between Bacterial Siderophores and Innate Immunity

Golonka, R. M., Yeoh, B. S., & Vijay–Kumar, M. (2019) · Journal of Innate Immunity · doi:10.1159/000494627 · Cited by 180

Iron speciation in the cytosol: an overview

Hider, R. C., & Kong, X. (2012) · Dalton Transactions · doi:10.1039/c2dt32149a · Cited by 172

Selective and Efficient Biomacromolecular Extraction of Rare-Earth Elements using Lanmodulin

Deblonde, G. J. ‐., Mattocks, J. A., Park, D. M., Reed, D. W., Cotruvo, J. A., & Jiao, Y. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c01303 · Cited by 173

Molecular basis of mycobacterial survival in macrophages

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The Metallophore Staphylopine Enables Staphylococcus aureus To Compete with the Host for Zinc and Overcome Nutritional Immunity

Grim, K. P., San Francisco, B., Radin, J. N., Brazel, E. B., Kelliher, J. L., Párraga Solórzano, P. K., Kim, P. C., McDevitt, C. A., & Kehl-Fie, T. E. (2017) · mBio · doi:10.1128/mbio.01281-17 · Cited by 152

Iron: the hard player in diabetes pathophysiology

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Lipocalin 2 Deficiency Dysregulates Iron Homeostasis and Exacerbates Endotoxin-Induced Sepsis

Srinivasan, G., Aitken, J. D., Zhang, B., Carvalho, F. A., Chassaing, B., Shashidharamurthy, R., Borregaard, N., Jones, D. P., Gewirtz, A. T., & Vijay–Kumar, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200892 · Cited by 143

In vivo bioluminescence imaging of labile iron accumulation in a murine model of Acinetobacter baumannii infection

Aron, A. T., Heffern, M. C., Lonergan, Z. R., Wal, M. N. V., Blank, B. R., Spangler, B., Zhang, Y., Park, H. M., Stahl, A., Renslo, A. R., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708747114 · Cited by 135

Transition metal ions at the crossroads of mucosal immunity and microbial pathogenesis

Diaz-Ochoa, V. E., Jellbauer, S., Klaus, S., & Raffatellu, M. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00002 · Cited by 129

The Iron Metallome in Eukaryotic Organisms

Dlouhy, A. C., & Outten, C. E. (2012) · Metal ions in life sciences · doi:10.1007/978-94-007-5561-1_8 · Cited by 129

Wearing Red for Signaling: The Heme-Bach Axis in Heme Metabolism, Oxidative Stress Response and Iron Immunology

Igarashi, K., & Watanabe‐Matsui, M. (2014) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.232.229 · Cited by 115

Targeting iron acquisition blocks infection with the fungal pathogens Aspergillus fumigatus and Fusarium oxysporum

Leal, S. M., Roy, S., Vareechon, C., Carrion, S. D., Clark, H., Lopez-Berges, M. S., diPietro, A., Schrettl, M., Beckmann, N., Redl, B., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003436 · Cited by 111

Bacterial siderophores promote plant growth: Screening of catechol and hydroxamate siderophores

Grobelak, A., & Hiller, J. (2017) · International Journal of Phytoremediation · doi:10.1080/15226514.2017.1290581 · Cited by 107

The Iron hand of Uropathogenic Escherichia Coli : The Role of Transition Metal Control in Virulence

Robinson, A. E., Heffernan, J. R., & Henderson, J. P. (2018) · Future Microbiology · doi:10.2217/fmb-2017-0295 · Cited by 95

Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development

Marchetti, M., Bei, O. D., Bettati, S., Campanini, B., Kovachka, S., Gianquinto, E., Spyrakis, F., & Ronda, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062145 · Cited by 93

Dual Inhibition of Klebsiella pneumoniae and Pseudomonas aeruginosa Iron Metabolism Using Gallium Porphyrin and Gallium Nitrate

Choi, S., Britigan, B. E., & Narayanasamy, P. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00100 · Cited by 92

A manganese-rich environment supports superoxide dismutase activity in a Lyme disease pathogen, Borrelia burgdorferi

Aguirre, J. D., Clark, H. M., McIlvin, M., Vazquez, C., Palmere, S. L., Grab, D. J., Seshu, J., Hart, P. J., Saito, M., & Culotta, V. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.433540 · Cited by 82

Iron and zinc exploitation during bacterial pathogenesis

Ma, L. M., Terwilliger, A. L., & Maresso, A. W. (2015) · Metallomics · doi:10.1039/c5mt00170f · Cited by 87

Prospects for treating osteoarthritis: enzyme–protein interactions regulating matrix metalloproteinase activity

Meszaros, E. C., & Malemud, C. (2012) · Therapeutic Advances in Chronic Disease · doi:10.1177/2040622312454157 · Cited by 90

Dinitrosyl iron complexes with glutathione as NO and NO+ donors

Borodulin, R. R., Kubrina, L. N., Mikoyan, V. D., Poltorakov, А. P., Shvydkiy, V. O., Burbaev, D. S., Сереженков, В. А., Yakhontova, E. R., & Vanin, A. F. (2012) · Nitric Oxide · doi:10.1016/j.niox.2012.11.001 · Cited by 73

Combinatorial Design of an Anticalin Directed against the Extra-Domain B for the Specific Targeting of Oncofetal Fibronectin

Gebauer, M., Schiefner, A., Matschiner, G., & Skerra, A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.12.004 · Cited by 71

Bacterial Siderophores That Evade or Overwhelm Lipocalin 2 Induce Hypoxia Inducible Factor 1α and Proinflammatory Cytokine Secretion in Cultured Respiratory Epithelial Cells

Holden, V. I., Lenio, S., Kuick, R. D., Ramakrishnan, S. K., Shah, Y. M., & Bachman, M. A. (2014) · Infection and Immunity · doi:10.1128/iai.01849-14 · Cited by 65

Lipocalin 2 regulates iron homeostasis, neuroinflammation, and insulin resistance in the brains of patients with dementia: Evidence from the current literature

Lim, D., Jeong, J., & Song, J. (2021) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13653 · Cited by 64

An overview of the biological metal uptake pathways in P seudomonas aeruginosa

Schalk, I. J., & Cunrath, O. (2016) · Environmental Microbiology · doi:10.1111/1462-2920.13525 · Cited by 65

Pseudomonas aeruginosa zinc homeostasis: Key issues for an opportunistic pathogen

Gonzalez, M. R., Ducret, V., Leoni, S., & Perron, K. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.01.018 · Cited by 57

Human Urinary Composition Controls Antibacterial Activity of Siderocalin*

Shields-Cutler, R. R., Crowley, J. R., Hung, C. S., Stapleton, A. E., Aldrich, C. C., Marschall, J., & Henderson, J. P. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645812 · Cited by 56

Lipocalin 2 stimulates bone fibroblast growth factor 23 production in chronic kidney disease

Courbon, G., Francis, C. P., Gerber, C., Neuburg, S., Wang, X., Lynch, E. P., Isakova, T., Babitt, J. L., Wolf, M. S., Martin, A., et al. (2021) · Bone Research · doi:10.1038/s41413-021-00154-0 · Cited by 57

Gallium Porphyrin and Gallium Nitrate Synergistically Inhibit Mycobacterial Species by Targeting Different Aspects of Iron/Heme Metabolism

Choi, S., Switzer, B. L., Britigan, B. E., & Narayanasamy, P. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00113 · Cited by 55

Iron in intracellular infection: to provide or to deprive?

Silva-Gomes, S., Vale-Costa, S., Appelberg, R., & Gomes, M. S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00096 · Cited by 51

Lipocalin‐2—The myth of its expression and function

Li, D., Sun, W. Y., Fu, B., Xu, A., & Wang, Y. (2019) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13332 · Cited by 54

A turn-on fluorescent chemodosimeter based on detelluration for detecting ferrous iron (Fe 2+ ) in living cells

Qu, Z., Li, P., Zhang, X., & Han, K. (2015) · Journal of Materials Chemistry B · doi:10.1039/c5tb02090e · Cited by 50

Siderophores as tools and treatments

Gräff, Á. T., & Barry, S. M. (2024) · npj Antimicrobials and Resistance · doi:10.1038/s44259-024-00053-4 · Cited by 50

ASP2397 Is a Novel Natural Compound That Exhibits Rapid and Potent Fungicidal Activity against Aspergillus Species through a Specific Transporter

Nakamura, I., Ohsumi, K., Takeda, S., Katsumata, K., Matsumoto, S., 赤松, 総., Mitori, H., & Nakai, T. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02689-18 · Cited by 44

New Perspectives on Circulating Ferritin: Its Role in Health and Disease

Fonseca, Ó., Ramos, H., Gomes, L. T. S., Gomes, M. S., & Moreira, A. C. (2023) · Molecules · doi:10.3390/molecules28237707 · Cited by 46

Human Metabolome-derived Cofactors Are Required for the Antibacterial Activity of Siderocalin in Urine

Shields‐Cutler, R. R., Crowley, J. R., Miller, C. D., Stapleton, A. E., Cui, W., & Henderson, J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.759183 · Cited by 38

Biological Roles of Lipocalins in Chemical Communication, Reproduction, and Regulation of Microbiota

Stopková, R., Otcenásková, T., Matějková, T., Kuntová, B., & Stopka, P. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.740006 · Cited by 33

The fate of siderophores: antagonistic environmental interactions in exudate-mediated micronutrient uptake

Harrington, J. M., Duckworth, O. W., & Haselwandter, K. (2015) · BioMetals · doi:10.1007/s10534-015-9821-4 · Cited by 33

The ligands of neutrophil gelatinase-associated lipocalin

Bao, G., Ho, C., & Barasch, J. M. (2015) · RSC Advances · doi:10.1039/c5ra18736b · Cited by 36

A systematic analysis of human lipocalin family and its expression in esophageal carcinoma

Du, Z., Wu, B., Wu, X., Lin, X., Qiu, X., Zhan, X.-F., Wang, S., Shen, J., Zheng, C.-P., Wu, Z., et al. (2015) · Scientific Reports · doi:10.1038/srep12010 · Cited by 34

Fluorescent sensors of siderophores produced by bacterial pathogens

Kumar, A., Yang, T., Chakravorty, S., Majumdar, A., Nairn, B. L., Six, D. A., Marcondes dos Santos, N., Price, S. L., Lawrenz, M. B., Actis, L. A., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101651 · Cited by 28

Lipocalin-2 as mediator of chemokine expression and granulocyte infiltration during ischemia and reperfusion

Sickinger, S., Maier, H. T., König, S., Vallant, N., Kofler, M., Schumpp, P., Schwelberger, H. G., Hermann, M., Obrist, P., Schneeberger, S., et al. (2013) · Transplant International · doi:10.1111/tri.12116 · Cited by 29

Siderophores; iron scavengers: the novel & promising targets for pathogen specific antifungal therapy

Balhara, M., Chaudhary, R., Ruhil, S., Singh, B., Dahiya, N. R., Parmar, V. S., Jaiwal, P. K., & Chhillar, A. K. (2016) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2016.1254196 · Cited by 29

Solvent free synthesis of ferrocene based rhodamine – hydrazone molecular probe with improved bioaccumulation for sensing and imaging applications

Dewangan, S., Barik, T., Parida, R., Mawatwal, S., Dhiman, R., Giri, S., & Chatterjee, S. (2019) · Journal of Organometallic Chemistry · doi:10.1016/j.jorganchem.2019.120999 · Cited by 27

Virulence factors of Klebsiella pneumoniae: Insights into canonical and emerging mechanisms driving pathogenicity and drug resistance

Singh, R. P., Kapoor, A., Sinha, A., Ma, Y., & Shankar, M. (2025) · The Microbe · doi:10.1016/j.microb.2025.100289 · Cited by 31

Understanding the Potential and Risk of Bacterial Siderophores in Cancer

Pita-Grisanti, V., Chasser, K. M., Sobol, T., & Cruz‐Monserrate, Z. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.867271 · Cited by 29

Siderophore-inspired nanoparticle-based biosensor for the selective detection of Fe 3+

Phillips, D. J., Davies, G., & Gibson, M. I. (2014) · Journal of Materials Chemistry B · doi:10.1039/c4tb01501k · Cited by 27

Correction: Targeting Iron Acquisition Blocks Infection with the Fungal Pathogens Aspergillus fumigatus and Fusarium oxysporum

Leal, S. M., Roy, S., Vareechon, C., Carrion, S. D. J., Clark, H., López‐Berges, M. S., Pietro, A. D., Schrettl, M., Beckmann, N., Redl, B., et al. (2013) · PLoS Pathogens · doi:10.1371/annotation/4f388450-90fe-4c65-9b9b-71a2b7935ac0 · Cited by 27

Parsing the functional specificity of Siderocalin/Lipocalin 2/NGAL for siderophores and related small-molecule ligands

Clifton, M. C., Rupert, P. B., Hoette, T. M., Raymond, K. N., Abergel, R. J., & Strong, R. K. (2019) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2019.100008 · Cited by 25

Nanoparticulate β-Cyclodextrin with Gallium Tetraphenylporphyrin Demonstrates in Vitro and in Vivo Antimicrobial Efficacy against Mycobacteroides abscessus and Mycobacterium avium

Choi, S., Talmon, G. A., Britigan, B. E., & Narayanasamy, P. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00896 · Cited by 24

Tonicity inversely modulates lipocalin-2 (Lcn2/24p3/NGAL) receptor (SLC22A17) and Lcn2 expression via Wnt/β-catenin signaling in renal inner medullary collecting duct cells: implications for cell fate and bacterial infection

Betten, R., Scharner, B., Probst, S., Edemir, B., Wolff, N. A., Langelueddecke, C., Lee, W., & Thévenod, F. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0285-3 · Cited by 22

Metal-antimicrobial peptides combo: promising weapons to combat bacteria invaders

Falcigno, L., Braccia, S., Bellavita, R., D’Auria, G., Falanga, A., & Galdiero, S. (2024) · Frontiers in Drug Discovery · doi:10.3389/fddsv.2024.1440378 · Cited by 23

An engineered lipocalin that tightly complexes the plant poison colchicine for use as antidote and in bioanalytical applications

Barkovskiy, M., Ilyukhina, E., Dauner, M., Eichinger, A., & Skerra, A. (2018) · Biological Chemistry · doi:10.1515/hsz-2018-0342 · Cited by 22

Purification and structural characterization of “simple catechol”, the NGAL-siderocalin siderophore in human urine

Bao, G., Barasch, J. M., Xu, J., Wang, W., Hu, F., & Deng, S. (2015) · RSC Advances · doi:10.1039/c5ra02509e · Cited by 21

Synthesis, spectroscopy, and binding constants of ketocatechol-containing iminodiacetic acid and its Fe(iii), Cu(ii), and Zn(ii) complexes and reaction of Cu(ii) complex with H2O2 in aqueous solution

Gao, J., Xing, F., Bai, Y., & Zhu, S. (2014) · Dalton Transactions · doi:10.1039/c4dt00118d · Cited by 22

Yersiniabactin is a quorum-sensing autoinducer and siderophore in uropathogenic Escherichia coli

Heffernan, J. R., Wildenthal, J. A., Tran, H. D., Katumba, G. L., McCoy, W. H., & Henderson, J. P. (2024) · mBio · doi:10.1128/mbio.00277-23 · Cited by 22

Iron Scavenging in Aspergillus Species: Structural and Biochemical Insights into Fungal Siderophore Esterases

Ecker, F., Haas, H., Groll, M., & Huber, E. M. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201807093 · Cited by 19

The Tricky Ways Bacteria Cope with Iron Limitation

Braun, V., & Hantke, K. (2013) · Springer briefs in molecular science · doi:10.1007/978-94-007-6088-2_2 · Cited by 18

Ligand binding‐dependent functions of the lipocalin NLaz: an in vivo study in Drosophila

Ruiz, M., Ganfornina, M. D., Correnti, C., Strong, R. K., & Sánchez, D. (2013) · The FASEB Journal · doi:10.1096/fj.13-240556 · Cited by 18

Modulation of urinary siderophores by the diet, gut microbiota and inflammation in mice

Xiao, X., Yeoh, B. S., Saha, P., Tian, Y., Singh, V., Patterson, A. D., & Vijay-Kumar, M. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.11.014 · Cited by 16

N-Octanoyl Dopamine Inhibits the Expression of a Subset of κB Regulated Genes: Potential Role of p65 Ser276 Phosphorylation

Hottenrott, M. C., Wedel, J., Gaertner, S., Stamellou, E., Kraaij, T., Mandel, L., Lösel, R., Sticht, C., Hoeger, S., Ait-Hsiko, L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073122 · Cited by 16

Half sandwich based rhodamine ‐ hydrazone single molecule probe: Light responsive, metal sensing and imaging properties

Dewangan, S., Barik, T., Mishra, S., Mawatwal, S., Kumari, S., Giri, S., Das, S., Dhiman, R., Wölper, C., & Chatterjee, S. (2018) · Applied Organometallic Chemistry · doi:10.1002/aoc.4612 · Cited by 16

The diversity of lipocalin receptors

Redl, B., & Habeler, M. (2021) · Biochimie · doi:10.1016/j.biochi.2021.09.008 · Cited by 15

Inverse Regulation of Lipocalin-2/24p3 Receptor/SLC22A17 and Lipocalin-2 Expression by Tonicity, NFAT5/TonEBP and Arginine Vasopressin in Mouse Cortical Collecting Duct Cells mCCD(cl.1): Implications for Osmotolerance

Probst, S., Scharner, B., McErlean, R., Lee, W., & Thévenod, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215398 · Cited by 15

Infection metallomics for critical care in the post‐COVID era

Patil, R. H., Luptáková, D., & Havlı́ček, V. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21755 · Cited by 15

Boosting AMPs’ Power: From Structural Engineering to Nanotechnology-Based Delivery

Ajayi, O. E., Bellavita, R., Imbò, L. E., Palladino, S., Braccia, S., Falanga, A., & Galdiero, S. (2025) · Molecules · doi:10.3390/molecules30142979 · Cited by 14

Surface Plasmon Resonance Identifies High-Affinity Binding of l -DOPA to Siderocalin/Lipocalin-2 through Iron–Siderophore Action: Implications for Parkinson’s Disease Treatment

Alhassen, S., Şenel, M., & Alachkar, A. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00693 · Cited by 14

Fungal NRPS-Dependent Siderophores: From Function to Prediction

Sørensen, J. L., Knudsen, M., Hansen, F. T., Olesen, C., Fuertes, P. R., Lee, T. V., Søndergaard, T. E., Pedersen, C. N. S., Brodersen, D. E., & Giese, H. (2014) · Fungal biology · doi:10.1007/978-1-4939-1191-2_15 · Cited by 14

Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu

Yang, T., Zou, Y., Ng, H. L., Kumar, A., Newton, S. M., & Klebba, P. E. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1355253 · Cited by 11

Stealthy microbes: How Neisseria gonorrhoeae hijacks bulwarked iron during infection

Stoudenmire, J. L., Greenawalt, A. N., & Cornelissen, C. N. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1017348 · Cited by 12

Stable, triplet ground state BODIPY-TEMPO diradical as a selective turn on fluorescence sensor for intracellular labile iron pool

Pachpatil, P. K., Kanojia, S. V., Ghosh, A., Majumdar, A. G., Wadawale, A., Mohapatra, M., Patro, B. S., Ghanty, T. K., & Goswami, D. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.132474 · Cited by 11

Siderophores and their Applications in Wood, Textile, and Paper Conservation

Rapti, S., Boyatzis, S. C., Rivers, S., & Πούρνου, Α. (2021) · Springer eBooks · doi:10.1007/978-3-030-69411-1_14 · Cited by 12

Lipopolysaccharide-induced inflammation or unilateral ureteral obstruction yielded multiple types of glycosylated Lipocalin 2

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Augmentation of antioxidant and iron(III) chelation properties of tertiary mixture of bioactive ligands

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Research Progress on Lipocalin-2 in Diabetic Encephalopathy

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Naphthalimide Assemblies for Simultaneous Detection of Ferrous Ion and H 2 O 2 to Prevent Fenton Reaction

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Iron depletion strategy for targeted cancer therapy: utilizing the dual roles of neutrophil gelatinase-associated lipocalin protein

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Preparation of 3-benzyloxy-2-pyridinone functional linkers: tools for the synthesis of 3,2-hydroxypyridinone (HOPO) and HOPO/hydroxamic acid chelators

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Photo‐release of Metal Ions in Living Cells

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Investigating possible association between multidrug resistance and isolate origin with some virulence factors ofEscherichia colistrains isolated from infant faeces and fresh green vegetables

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Gemeinsames Kolloquium - Wintersemester 2010/11 Interdisciplinary Lecture Series

Raymond, K. N. (2010)

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