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1. Full Text Coordination of hydroxyquinolines to a ruthenium bis-dimethyl-phenanthroline scaffold radically improves potency for potential as antineoplastic agents
by Heidary, David K and Howerton, Brock S and Glazer, Edith C
Journal of Medicinal Chemistry, ISSN 0022-2623, 11/2014, Volume 57, Issue 21, pp. 8936 - 8946
A series of ruthenium coordination complexes containing hydroxyquinoline ligands were synthesized that exhibited radically improved potencies up to 86-fold... 
CLIOQUINOL | CHEMISTRY, MEDICINAL | ALZHEIMERS-DISEASE | COMPLEXES | 8-HYDROXYQUINOLINE | CELL-PROTEINS | DEGRADATION | COPPER | ANTITUMOR-ACTIVITY | PROTEASOME INHIBITORS | APOPTOSIS INDUCERS | Proteasome Inhibitors - pharmacology | Apoptosis - drug effects | Antineoplastic Agents - chemical synthesis | Humans | Copper - pharmacology | Structure-Activity Relationship | Hydroxyquinolines - chemical synthesis | Clioquinol - pharmacology | Quinolines - pharmacology | Ruthenium - pharmacology | Quinolines - chemical synthesis | Cell Line, Tumor | Coordination Complexes - chemical synthesis | Coordination Complexes - pharmacology | HL-60 Cells | Inhibitory Concentration 50 | Antineoplastic Agents - pharmacology | Hydroxyquinolines - pharmacology | Index Medicus
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2. Full Text Administration of zinc chelators improves survival of mice infected with Aspergillus fumigatus both in monotherapy and in combination with caspofungin
by Laskaris, Paris and Atrouni, Ahmad and Calera, José Antonio and D'Enfert, Christophe and Munier-Lehmann, Hélène and Cavaillon, Jean-Marc and Latgé, Jean-Paul and Ibrahim-Granet, Oumaïma
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 10/2016, Volume 60, Issue 10, pp. 5631 - 5639
Aspergillus fumigatus can infect immunocompromised patients, leading to high mortality rates due to the lack of reliable treatment options. This pathogen... 
HUMAN-SERUM | INVASIVE ASPERGILLOSIS | HOMEOSTASIS | 1,10-PHENANTHROLINE | PULMONARY ASPERGILLOSIS | DEFERASIROX | SUSCEPTIBILITY | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | ANTIFUNGAL THERAPY | IRON CHELATION | CELL | Aspergillus fumigatus - drug effects | Lipopeptides - pharmacology | Pneumonia - pathology | Male | Phenanthrolines - pharmacology | Aspergillosis - mortality | Drug Therapy, Combination | Echinocandins - pharmacology | Aspergillosis - drug therapy | Antifungal Agents - pharmacology | Immune Sera - pharmacology | Ethylamines - pharmacology | Treatment Outcome | Pneumonia - microbiology | Chelating Agents - pharmacology | Aspergillus fumigatus - pathogenicity | Clioquinol - pharmacology | Zinc | Animals | Aspergillosis - microbiology | Aspergillus fumigatus - growth & development | Mice, Inbred BALB C | Pyridines - pharmacology | Immunocompromised Host | Aspergillosis - immunology | Index Medicus | Life Sciences | Microbiology and Parasitology | Mycology
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3. Full Text The inhalation anesthetic isoflurane induces a vicious cycle of apoptosis and amyloid β-protein accumulation
by Xie, Zhongcong and Dong, Yuanlin and Maeda, Uta and Moir, Robert D and Xia, Weiming and Culley, Deborah J and Crosby, Gregory and Tanzi, Rudolph E
Journal of Neuroscience, ISSN 0270-6474, 02/2007, Volume 27, Issue 6, pp. 1247 - 1254
The anesthetic isoflurane has been reported to induce apoptosis and increase A beta generation and aggregation. However, the molecular mechanism underlying... 
APP | Anesthesia | Alzheimer's disease | Isoflurane | Apoptosis | PRESENILIN | GAMMA | ALZHEIMERS-DISEASE | INVOLVEMENT | apoptosis | NEURONAL CELL-DEATH | CLEAVAGE | NEUROSCIENCES | PEPTIDE | anesthesia | A beta | CALCIUM | PRECURSOR PROTEIN | isoflurane | CEREBRAL-ISCHEMIA | Neuroglia - ultrastructure | Isoflurane - pharmacology | Apoptosis - drug effects | Amyloid beta-Peptides - pharmacology | Humans | Caspase 3 - metabolism | Isoflurane - adverse effects | Peptide Fragments - pharmacology | Cell Line, Tumor - drug effects | Anesthetics, Inhalation - adverse effects | Recombinant Fusion Proteins - metabolism | Neuroglia - drug effects | Amyloid beta-Peptides - genetics | Ganglioglioma - pathology | Isoflurane - toxicity | Amyloid beta-Peptides - metabolism | Alzheimer Disease - chemically induced | Copper | Anesthetics, Inhalation - toxicity | Anesthetics, Inhalation - pharmacology | Aspartic Acid Endopeptidases - drug effects | Chelating Agents - pharmacology | Recombinant Fusion Proteins - chemistry | Enzyme Activation - drug effects | Clioquinol - pharmacology | Zinc | Amyloid Precursor Protein Secretases - metabolism | Amyloid Precursor Protein Secretases - drug effects | Aspartic Acid Endopeptidases - metabolism | Cysteine Proteinase Inhibitors - pharmacology | Neuroglia - metabolism | Amyloid beta-Peptides - chemistry | Oligopeptides - pharmacology | Index Medicus
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4. Full Text Small-molecule aggregates inhibit amyloid polymerization
by Toyama, Brandon H and Prusiner, Stanley B and Collins, Sean R and Wille, Holger and Shoichet, Brian K and Colby, David W and Feng, Brian Y and Weissman, Jonathan and May, Barnaby C H
Nature Chemical Biology, ISSN 1552-4450, 03/2008, Volume 4, Issue 3, pp. 197 - 199
Many amyloid inhibitors resemble molecules that form chemical aggregates, which are known to inhibit many proteins. Eight known chemical aggregators inhibited... 
FIBRIL FORMATION | YEAST | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISEASE | PROMISCUOUS INHIBITORS | NEUROTOXICITY | Molecular Weight | Detergents - chemistry | Microscopy, Electron, Transmission - methods | Phthalimides - chemistry | Structure-Activity Relationship | Benzopyrans - chemistry | Saccharomyces cerevisiae - metabolism | Clioquinol - chemistry | Phthalimides - pharmacology | Flavanones - chemistry | Sensitivity and Specificity | Acetophenones - pharmacology | Molecular Structure | Prions - pharmacokinetics | beta-Lactamase Inhibitors | Benzopyrans - pharmacology | Saccharomyces cerevisiae Proteins - pharmacokinetics | Recombinant Proteins - metabolism | Prions - metabolism | Recombinant Proteins - antagonists & inhibitors | Phenolphthaleins - chemistry | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Congo Red - pharmacology | Flavanones - pharmacology | Recombinant Proteins - chemistry | Prions - chemistry | Clioquinol - pharmacology | Prions - antagonists & inhibitors | Saccharomyces cerevisiae - chemistry | Particle Size | Phenolphthaleins - pharmacology | beta-Lactamases - chemistry | Animals | Acetophenones - chemistry | Peptide Termination Factors | Mice | Congo Red - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Biochemistry | Inhibitor drugs | Molecular biology | Prions | Index Medicus
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5. Full Text A novel proteasome inhibitor suppresses tumor growth via targeting both 19S proteasome deubiquitinases and 20S proteolytic peptidases
by Liu, Ningning and Liu, Chunjiao and Li, Xiaofen and Liao, Siyan and Song, Wenbin and Yang, Changshan and Zhao, Chong and Huang, Hongbiao and Guan, Lixia and Zhang, Peiquan and Liu, Shouting and Hua, Xianliang and Chen, Xin and Zhou, Ping and Lan, Xiaoying and Yi, Songgang and Wang, Shunqing and Wang, Xuejun and Dou, Q. Ping and Liu, Jinbao
Scientific Reports, ISSN 2045-2322, 06/2014, Volume 4, Issue 1, pp. 5240 - 5240
The successful development of bortezomib-based therapy for treatment of multiple myeloma has established proteasome inhibition as an effective therapeutic... 
CLIOQUINOL | ENZYME | GAMBOGIC ACID | MULTIDISCIPLINARY SCIENCES | COMPLEXES | ZINC PYRITHIONE | COPPER | BORTEZOMIB | CANCER | APOPTOSIS INDUCERS | CELL-DEATH | Humans | Ubiquitin - metabolism | Male | Protease Inhibitors - pharmacology | Proteolysis - drug effects | Multiple Myeloma - drug therapy | HEK293 Cells | Antineoplastic Agents - pharmacology | Ubiquitin-Specific Proteases - metabolism | Peptide Hydrolases - metabolism | Cell Line | Bortezomib | Proteasome Inhibitors - pharmacology | Multiple Myeloma - metabolism | Hep G2 Cells | Animals | Mice, Nude | Cell Line, Tumor | Mice | Mice, Inbred BALB C | Pyridines - pharmacology | Proteasome Endopeptidase Complex - metabolism | Pyrazines - pharmacology | Organometallic Compounds - pharmacology | Boronic Acids - pharmacology | Ubiquitin | Multiple myeloma | Cytotoxicity | Pyrithione | Cancer therapies | Biocides | Protease inhibitors | Proteolysis | Proteasomes | Tributyltin | Copper | Cancer | Index Medicus
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6. Full Text Nanoscale reaction vessels designed for synthesis of copper-drug complexes suitable for preclinical development
by Wehbe, Mohamed and Anantha, Malathi and Backstrom, Ian and Leung, Ada and Chen, Kent and Malhotra, Armaan and Edwards, Katarina and Bally, Marcel B and Teknisk-naturvetenskapliga vetenskapsområdet and Uppsala universitet and Analytisk kemi and Institutionen för kemi - BMC and Kemiska sektionen
PLoS ONE, ISSN 1932-6203, 04/2016, Volume 11, Issue 4, pp. e0153416 - e0153416
The development of copper-drug complexes (CDCs) is hindered due to their very poor aqueous solubility. Diethyldithiocarbamate (DDC) is the primary metabolite... 
DISULFIRAM | LARGE UNILAMELLAR VESICLES | BREAST-CANCER CELLS | INHIBITION | REACTIVATES LATENT HIV-1 | ANTICANCER AGENTS | MULTIDISCIPLINARY SCIENCES | PH GRADIENTS | RNA-POLYMERASE I | SODIUM DIETHYLDITHIOCARBAMATE | LIPOSOMAL SYSTEMS | Antioxidants - chemistry | Antineoplastic Agents - chemical synthesis | Humans | Ditiocarb - metabolism | Clioquinol - chemistry | Copper - chemistry | Copper - metabolism | Female | Antineoplastic Agents - pharmacology | Tumor Cells, Cultured | Cell Survival - drug effects | Naphthyridines - chemistry | Quercetin - chemistry | Benzothiazoles - pharmacology | Antioxidants - pharmacology | Clioquinol - pharmacology | Neoplasms - drug therapy | Xenograft Model Antitumor Assays | Ditiocarb - chemistry | Animals | Quercetin - pharmacology | Benzothiazoles - chemistry | Mice | Liposomes | Neoplasms - pathology | Nanotechnology | Naphthyridines - pharmacology | Drugs | Complications and side effects | Drug delivery systems | Alcoholism | Disulfiram | Dosage and administration | Research | Drug therapy | Vehicles | Drug abuse | Medical research | Laboratories | Research & development--R&D | Clioquinol | Cytotoxicity | Drug development | Anticancer properties | Antitumor agents | Quercetin | Antitumor activity | Copper | Alzheimers disease | Coordination compounds | Chemical synthesis | Pharmaceutical sciences | Cancer | Index Medicus | Naturvetenskap | Natural Sciences | Kemi | Annan kemi | Chemical Sciences | Other Chemistry Topics | Research & development | R&D
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7. Full Text Inhibition of aminoglycoside 6′-N-acetyltransferase type Ib-mediated amikacin resistance by zinc complexed with clioquinol, an ionophore active against tumors and neurodegenerative diseases
by Chiem, Kevin and Hue, Fong and Magallon, Jesus and Tolmasky, Marcelo E
International Journal of Antimicrobial Agents, ISSN 0924-8579, 02/2018, Volume 51, Issue 2, pp. 271 - 273
INFECTIOUS DISEASES | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | Acetyltransferases - metabolism | Amikacin - pharmacology | Neurodegenerative Diseases - drug therapy | Zinc - chemistry | Clioquinol - pharmacology | Ionophores | Microbial Sensitivity Tests | Clioquinol - chemistry | Acetyltransferases - antagonists & inhibitors | Anti-Bacterial Agents - pharmacology | Antineoplastic Agents - pharmacology | Zinc - pharmacology | Acinetobacter baumannii - drug effects | Drug Resistance, Bacterial - genetics | Index Medicus
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8. Full Text Clioquinol-ruthenium complex impairs tumour cell invasion by inhibiting cathepsin B activity
by Mitrovi, Ana and Kljun, Jakob and Sosi, Izidor and Gobec, Stanislav and Turel, Iztok and Kos, Janko
Dalton Transactions, ISSN 1477-9226, 10/2016, Volume 45, Issue 42, pp. 16913 - 16921
Over the past few years, the organometalled compounds, including ruthenium, gained a lot of attention as anticancer agents. We report on the... 
POTENTIAL ANTICANCER AGENTS | MULTIPLE ROLES | IN-VITRO | DNA | OCCLUDING LOOP | BIOLOGICAL EVALUATION | NITROXOLINE | CYSTEINE CATHEPSINS | CANCER | ANTITUMOR DRUGS | CHEMISTRY, INORGANIC & NUCLEAR | Neoplasms - metabolism | Clioquinol - analogs & derivatives | Humans | Neoplasm Invasiveness - prevention & control | Enzyme Inhibitors - pharmacology | Cathepsin B - antagonists & inhibitors | Cathepsin B - metabolism | Antineoplastic Agents - chemistry | Clioquinol - pharmacology | Ruthenium - chemistry | Ruthenium - pharmacology | Neoplasms - drug therapy | Monoterpenes - pharmacology | Neoplasm Invasiveness - pathology | Enzyme Inhibitors - chemistry | Cell Line, Tumor | Monoterpenes - chemistry | Organometallic Compounds - chemistry | Antineoplastic Agents - pharmacology | Neoplasms - pathology | Organometallic Compounds - pharmacology | Index Medicus | Peptidases | Cysteine | Ruthenium | Cathepsin B | Real time | Spheroids | Tumors | Anticancer properties
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9. Full Text Insights into Zn2+ homeostasis in neurons from experimental and modeling studies
by Robert A. Colvin and Ashley I. Bush and Irene Volitakis and Charles P. Fontaine and Dustin Thomas and Kazuya Kikuchi and William R. Holmes
American Journal of Physiology - Cell Physiology, ISSN 0363-6143, 03/2008, Volume 294, Issue 3, pp. 726 - 742
To understand the mechanisms of neuronal Zn2+ homeostasis better, experimental data obtained from cultured cortical neurons were used to inform a series of... 
Zinc buffering | Metal ion transport and homeostasis | Computational model | Muffler | Metallothionein | ALKALINE-PHOSPHATASES | PHYSIOLOGY | K562 ERYTHROLEUKEMIA-CELLS | ALZHEIMERS-DISEASE | CULTURED NEURONS | zinc buffering | GOLGI-APPARATUS | muffler | metallothionein | SECRETORY PATHWAY | CELL BIOLOGY | IN-VITRO | CORTICAL-NEURONS | computational model | MAMMALIAN ZINC TRANSPORTER | metal ion transport and homeostasis | Metallothionein - metabolism | Zinc - metabolism | Homeostasis | Cerebral Cortex - cytology | Cerebral Cortex - metabolism | Computer Simulation | Edetic Acid - pharmacology | Neurons - metabolism | Cerebral Cortex - drug effects | Neurons - drug effects | Reproducibility of Results | Cells, Cultured | Rats | Spectrometry, Fluorescence | Chelating Agents - pharmacology | Clioquinol - pharmacology | Rats, Sprague-Dawley | Ethylenediamines - pharmacology | Animals | Cerebral Cortex - embryology | Protein Binding | Pyridines - pharmacology | Kinetics | Models, Neurological | Thiones - pharmacology | Mass Spectrometry - methods | Index Medicus
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10. Full Text Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells
by Daniel, Kenyon G and Chen, Di and Orlu, Shirley and Cui, Qiuzhi C.indy and Miller, Fred R and Dou, Q Ping
Breast cancer research : BCR, ISSN 1465-5411, 2005, Volume 7, Issue 6, pp. R897 - R908
Introduction A physiological feature of many tumor tissues and cells is the tendency to accumulate high concentrations of copper. While the precise role of... 
LUNG-CANCER | TRACE-ELEMENTS | RETINOBLASTOMA PROTEIN | ONCOLOGY | ALZHEIMERS-DISEASE | ANTICANCER THERAPY | CERULOPLASMIN | FACTOR-KAPPA-B | SERUM | DEATH | ZINC | Cell Proliferation | Anti-Infective Agents, Local - pharmacology | Apoptosis - drug effects | Humans | Antioxidants - pharmacology | Clioquinol - pharmacology | Pyrrolidines - pharmacology | Drug Interactions | Thiocarbamates - pharmacology | Breast Neoplasms - pathology | Copper - metabolism | Cell Line, Tumor | Female | Precancerous Conditions - pathology | Proteasome Inhibitors | Care and treatment | Clioquinol | Breast cancer | Monosaccharides | Proteins | Antioxidants | Alkaloids | Chymotrypsin | Cancer cells | Physiological aspects | Copper compounds | Drug therapy | Alzheimer's disease | Sugars | Apoptosis | Cancer | Index Medicus
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11. Full Text The antiparasitic clioquinol induces apoptosis in leukemia and myeloma cells by inhibiting histone deacetylase activity
by Cao, Biyin and Li, Jie and Zhu, Jingyu and Shen, Mingyun and Han, Kunkun and Zhang, Zubin and Yu, Yang and Wang, Yali and Wu, Depei and Chen, Suning and Sun, Aining and Tang, Xiaowen and Zhao, Yun and Qiao, Chunhua and Hou, Tingjun and Mao, Xinliang
Journal of Biological Chemistry, ISSN 0021-9258, 11/2013, Volume 288, Issue 47, pp. 34181 - 34189
Background: Clioquinol is a potent chelator of divalent metal ions including zinc. Results: Clioquinol fits the zinc-centered active pocket of HDACs and... 
CANCER-CELLS | Enzyme Inhibitors | DNA-BINDING | Computer Modeling | ACETYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | Clioquinol | Histone Deacetylase | P53 | PROTEASOME | THERAPEUTIC TARGETS | FORCE-FIELD | MALIGNANCIES | DISPLAYS PRECLINICAL ACTIVITY | Apoptosis | Multiple Myeloma | Leukemia - pathology | Apoptosis - drug effects | Chlorides - pharmacology | Humans | Leukemia - enzymology | Gene Expression Regulation, Leukemic - drug effects | Leukemia - drug therapy | Histone Deacetylases - metabolism | Male | Neoplasm Proteins - antagonists & inhibitors | Antipruritics - pharmacology | Down-Regulation - drug effects | Neoplasm Proteins - metabolism | Clioquinol - pharmacology | Mouthwashes - pharmacology | Multiple Myeloma - drug therapy | Multiple Myeloma - pathology | Zinc Compounds - pharmacology | U937 Cells | K562 Cells | Female | Histone Deacetylase Inhibitors - pharmacology | G1 Phase Cell Cycle Checkpoints - drug effects | Multiple Myeloma - enzymology | Index Medicus | Gene Regulation
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12. Full Text Changes in Intracellular Calcium and Glutathione in Astrocytes as the Primary Mechanism of Amyloid Neurotoxicity
by Abramov, Andrey Y and Canevari, Laura and Duchen, Michael R
Journal of Neuroscience, ISSN 0270-6474, 06/2003, Volume 23, Issue 12, pp. 5088 - 5095
Although the accumulation of the neurotoxic peptide beta amyloid (betaA) in the CNS is a hallmark of Alzheimer's disease, the mechanism of betaA neurotoxicity... 
Neuron | Astrocyte | Intracellular calcium | Alzheimer | β-amyloid | Glutathione | OXIDATIVE STRESS | HOMEOSTASIS | glutathione | ALZHEIMERS-DISEASE | neuron | GLIAL-CELLS | HIPPOCAMPAL-NEURONS | NEUROSCIENCES | beta-amyloid | CORTICAL-NEURONS | GLUTAMATE | A-BETA | BETA-PROTEIN | intracellular calcium | CHANNELS | astrocyte | Alzheimer Disease - etiology | Calcium - metabolism | Glutathione - metabolism | Amyloid beta-Peptides - pharmacology | Coculture Techniques | Neurons - cytology | Peptide Fragments - pharmacology | Extracellular Space | Amyloid - toxicity | Neuroprotective Agents - pharmacology | Neurons - metabolism | Neurons - drug effects | Intracellular Fluid - metabolism | Astrocytes - cytology | Astrocytes - drug effects | Cell Survival - drug effects | Cells, Cultured | Rats | Chelating Agents - pharmacology | Hippocampus - cytology | Clioquinol - pharmacology | Rats, Sprague-Dawley | Animals | Calcium Signaling - drug effects | Alzheimer Disease - metabolism | Zinc - pharmacology | Astrocytes - metabolism | Index Medicus
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13. Full Text 8-Hydroxyquinolines are boosting agents of copper-related toxicity in Mycobacterium tuberculosis
by Shah, Santosh and Dalecki, Alex G and Malalasekera, Aruni P and Crawford, Cameron L and Michalek, Suzanne M and Kutsch, Olaf and Sun, Jim and Bossmann, Stefan H and Wolschendorf, Frank
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 10/2016, Volume 60, Issue 10, pp. 5765 - 5776
Copper (Cu) ions are likely the most important immunological metal-related toxin utilized in controlling bacterial infections. Impairment of bacterial Cu... 
DRUG | CLIOQUINOL | SMEGMATIS | GENE | MACROPHAGES | STABILITY | COMPLEXES | SUSCEPTIBILITY | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | INFECTION | MICE | Oxyquinoline - pharmacology | Antitubercular Agents - chemistry | Mice, Inbred C57BL | Antitubercular Agents - pharmacology | Cells, Cultured | Copper - pharmacology | Mycobacterium tuberculosis - drug effects | Drug Synergism | Microbial Sensitivity Tests | Mycobacterium tuberculosis - pathogenicity | Animals | Copper - chemistry | Macrophages, Peritoneal - microbiology | Tuberculosis - drug therapy | Coordination Complexes - pharmacology | Female | Macrophages, Peritoneal - drug effects | Oxyquinoline - chemistry | Disease Models, Animal | Index Medicus
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14. Full Text Ionophore and Biometal Modulation of P-glycoprotein Expression and Function in Human Brain Microvascular Endothelial Cells
by McInerney, Mitchell P and Volitakis, Irene and Bush, Ashley I and Banks, William A and Short, Jennifer L and Nicolazzo, Joseph A
Pharmaceutical Research, ISSN 0724-8741, 4/2018, Volume 35, Issue 4, pp. 1 - 12
Biometals such as zinc and copper have been shown to affect tight junction expression and subsequently blood-brain barrier (BBB) integrity. Whether these... 
Biochemistry, general | Biomedical Engineering | blood-brain barrier | P-glycoprotein | Biomedicine | ionophore | Pharmacy | transporter | Medical Law | Pharmacology/Toxicology | clioquinol | CLEARANCE | HOMEOSTASIS | ALZHEIMERS-DISEASE | BARRIER | COPPER | CHEMISTRY, MULTIDISCIPLINARY | BETA | MOUSE MODEL | PHARMACOLOGY & PHARMACY | CENTRAL-NERVOUS-SYSTEM | ABC TRANSPORTERS | TRANSGENIC MICE | Endothelium, Vascular - cytology | Microvessels - cytology | Cell Line | Endothelial Cells | Humans | Microvessels - metabolism | Microvessels - drug effects | Trace Elements - pharmacology | Blood-Brain Barrier - drug effects | Clioquinol - pharmacology | ATP Binding Cassette Transporter, Subfamily B - metabolism | Blood-Brain Barrier - metabolism | Ionophores - pharmacology | Drugs | Brain | Drug delivery systems | Resveratrol | Mass spectrometry | Vehicles | Endothelium | Efflux | Rhodamine | Incubation | Trafficking | Glycoprotein | Fluorescence | Clioquinol | Mass spectroscopy | Glycoproteins | Bioavailability | Zinc | Substrates | Endothelial cells | Western blotting | Inductively coupled plasma | Blood-brain barrier | Modulation | Microvasculature | Copper | P-Glycoprotein | Index Medicus
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