Compounds > vanadates
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vanadates and leukotriene c4

vanadates has been researched along with leukotriene c4 in 12 studies

Research

Studies (12)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (8.33)18.2507
2000's11 (91.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bakos, E; Borst, P; de Haas, M; Evers, R; Sarkadi, B; Szabó, K; Szakács, G; Tusnády, GE; van Deemter, L; Váradi, A; Welker, E1
Almquist, KC; Cole, SP; Cui, HR; Deeley, RG; Gao, M; Grant, CE; Loe, DW1
Cole, SP; Deeley, RG; Leslie, EM; Mao, Q; Oleschuk, CJ1
Cai, J; Daoud, R; Georges, E; Gros, P1
Cole, SP; Deeley, RG; Gao, M; Qian, YM; Qiu, W; Westlake, CJ1
Cole, SP; Dantzig, AH; Deeley, RG; Lander, PA; Mao, Q; Qiu, W; Shepard, RL; Tabas, LB; Weigl, KE1
Cole, SP; Deeley, RG; Gao, M; Payen, LF; Westlake, CJ1
Akiyama, S; Aoki, S; Furukawa, T; Haraguchi, M; Kobayashi, M; Ren, XQ; Sumizawa, T1
Cole, SP; Conseil, G; Deeley, RG; Haimeur, A; Situ, D; Sparks, KE; Zhang, D1
Cole, SP; Deeley, RG; Gao, M; Payen, L; Westlake, CJ1
Cole, SP; Conseil, G; Deeley, RG1
Cole, SP; Deeley, RG; Létourneau, IJ; Slot, AJ1

Other Studies

12 other study(ies) available for vanadates and leukotriene c4

ArticleYear
Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain.
    The Journal of biological chemistry, 1998, Nov-27, Volume: 273, Issue:48

    Topics: Animals; Baculoviridae; Base Pair Mismatch; Cell Membrane; Cloning, Molecular; DNA-Binding Proteins; Dogs; Glutathione; Humans; Kinetics; Leukotriene C4; Maleimides; Models, Molecular; Multidrug Resistance-Associated Proteins; MutS Homolog 3 Protein; Protein Structure, Secondary; Recombinant Proteins; Sequence Deletion; Spodoptera; Transfection; Vanadates

1998
Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1.
    The Journal of biological chemistry, 2000, Apr-28, Volume: 275, Issue:17

    Topics: Adenosine Triphosphate; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Baculoviridae; Cell Line; Immunoblotting; Insecta; Leukotriene C4; Lysine; Mutagenesis, Site-Directed; Nucleotides; Plasmids; Protein Binding; Protein Structure, Tertiary; Time Factors; Vanadates

2000
Modulation of multidrug resistance protein 1 (MRP1/ABCC1) transport and atpase activities by interaction with dietary flavonoids.
    Molecular pharmacology, 2001, Volume: 59, Issue:5

    Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Antineoplastic Agents, Phytogenic; ATP-Binding Cassette Transporters; Azides; Binding, Competitive; Biological Transport; Cell Division; Chromatography, High Pressure Liquid; Drug Interactions; Estradiol; Estrogen Antagonists; Flavanones; Flavonoids; Glutathione; HeLa Cells; Humans; Kaempferols; Kinetics; Leukotriene C4; Multidrug Resistance-Associated Proteins; Phosphorus Radioisotopes; Quercetin; Transfection; Tritium; Vanadates; Vincristine

2001
Functional expression of multidrug resistance protein 1 in Pichia pastoris.
    Biochemistry, 2001, Jul-27, Volume: 40, Issue:28

    Topics: Adenosine Triphosphate; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Cell Fractionation; Cell Membrane; Humans; Iodine Radioisotopes; Leukotriene C4; Phosphorus Radioisotopes; Photoaffinity Labels; Pichia; Plasmids; Protein Binding; Protein Transport; Recombinant Proteins; Rhodamine 123; Tritium; Vanadates

2001
Characterization of binding of leukotriene C4 by human multidrug resistance protein 1: evidence of differential interactions with NH2- and COOH-proximal halves of the protein.
    The Journal of biological chemistry, 2001, Oct-19, Volume: 276, Issue:42

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Binding Sites; Blotting, Western; Cell Line; Cell Membrane; Cytoplasm; DNA, Complementary; Humans; Hydrolysis; Insecta; Leukotriene C4; Multidrug Resistance-Associated Proteins; Mutation; Photoaffinity Labels; Plasmids; Protein Binding; Protein Structure, Tertiary; Protein Transport; Trypsin; Tumor Cells, Cultured; Vanadates

2001
GSH-dependent photolabeling of multidrug resistance protein MRP1 (ABCC1) by [125I]LY475776. Evidence of a major binding site in the COOH-proximal membrane spanning domain.
    The Journal of biological chemistry, 2002, Aug-09, Volume: 277, Issue:32

    Topics: Antibodies, Monoclonal; Azides; Binding Sites; Cell Membrane; DNA-Binding Proteins; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Glutathione; HeLa Cells; Humans; Immunoblotting; Isoxazoles; Leukotriene C4; Light; Models, Chemical; Multidrug Resistance-Associated Proteins; Mutation; MutS Homolog 3 Protein; Protein Binding; Protein Conformation; Transfection; Tumor Cells, Cultured; Vanadates

2002
Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1).
    The Journal of biological chemistry, 2003, Oct-03, Volume: 278, Issue:40

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Motifs; Amino Acid Sequence; Animals; Aspartic Acid; Biological Transport; Carboxylic Acids; Catalysis; Cell Line; Cell Membrane; DNA, Complementary; Drug Resistance, Multiple; Electrophoresis, Polyacrylamide Gel; Glutamic Acid; Humans; Hydrolysis; Insecta; Leukotriene C4; Light; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutation; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Time Factors; Vanadates

2003
Function of the ABC signature sequences in the human multidrug resistance protein 1.
    Molecular pharmacology, 2004, Volume: 65, Issue:6

    Topics: Adenosine Triphosphate; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; ATP-Binding Cassette Transporters; Azides; Biological Transport; Cells, Cultured; Humans; Insecta; Leukotriene C4; Mutation; Phosphorus Radioisotopes; Protein Structure, Tertiary; Vanadates

2004
Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter.
    The Journal of biological chemistry, 2004, Sep-10, Volume: 279, Issue:37

    Topics: Adenosine Triphosphate; Amino Acid Sequence; Anions; Arginine; Aspartic Acid; Biological Transport; Catalysis; Cell Line, Transformed; Cytoplasm; DNA Mutational Analysis; DNA, Complementary; Glutamic Acid; Humans; Ions; Leukotriene C4; Models, Molecular; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutagenesis, Site-Directed; Mutation; Organic Anion Transporters; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Time Factors; Transfection; Vanadates

2004
Identification and characterization of functionally important elements in the multidrug resistance protein 1 COOH-terminal region.
    The Journal of biological chemistry, 2004, Dec-17, Volume: 279, Issue:51

    Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Cell Line; Cell Membrane; Codon; Crystallography, X-Ray; Cytoplasm; Dogs; Dose-Response Relationship, Drug; Enhancer Elements, Genetic; Hydrolysis; Immunoblotting; Insecta; Kinetics; Leukotriene C4; Molecular Sequence Data; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Point Mutation; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport; Time Factors; Vanadates

2004
Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1).
    The Journal of biological chemistry, 2006, Jan-06, Volume: 281, Issue:1

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Arginine; Azides; Catalytic Domain; Cell Line; Cytosol; Estradiol; Humans; Kidney; Leukotriene C4; Lysine; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutagenesis, Site-Directed; Phosphorus Radioisotopes; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Tritium; Vanadates

2006
Mutational analysis of a highly conserved proline residue in MRP1, MRP2, and MRP3 reveals a partially conserved function.
    Drug metabolism and disposition: the biological fate of chemicals, 2007, Volume: 35, Issue:8

    Topics: Adenosine Triphosphate; Azides; Binding Sites; Cations, Divalent; Cell Line; Cell Membrane; Estradiol; Humans; Leukotriene C4; Membrane Transport Proteins; Methotrexate; Multidrug Resistance-Associated Protein 2; Multidrug Resistance-Associated Proteins; Mutagenesis, Site-Directed; Mutation, Missense; Photochemistry; Proline; Protein Binding; Transfection; Vanadates

2007