Page last updated: 2024-08-17

aspartic acid and 1,7-phenanthroline

aspartic acid has been researched along with 1,7-phenanthroline in 13 studies

Research

Studies (13)

TimeframeStudies, this research(%)All Research%
pre-19907 (53.85)18.7374
1990's1 (7.69)18.2507
2000's4 (30.77)29.6817
2010's1 (7.69)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Balch, WE; Gilchrist, PS; Taylor, ML; Taylor, WH1
Levkovitz, H; Loyter, A; Ofer, L1
Berkner, KL; Derian, CK; Friedman, PA; Kaufman, RJ; Przysiecki, CT; VanDusen, W; Walsh, PN1
Ivanova, V; Tomova, N1
Dimitrov, GD1
Olson, MS; Schuster, SM1
Eckelman, W; Meinken, G; Richards, P1
Kim, SH; Koshland, DE; Milburn, MV; Milligan, DL; Privé, GG; Scott, WG; Yeh, J1
Li, RA; Tian, Y; Tomaselli, GF; Xiong, W1
Kang, K; Kinjo, TG; Schnetkamp, PP; Szerencsei, RT; Winkfein, RJ1
Betté, S; Castagna, M; Mandela, PG; Mari, SA; Peres, A; Rudnick, G; Sacchi, VF; Santacroce, M; Soragna, A1
Kanner, BI; Qu, S1
Qu, S; Zhang, X; Zhang, Y1

Other Studies

13 other study(ies) available for aspartic acid and 1,7-phenanthroline

ArticleYear
Purification of properties of dihydroorotase, a zinc-containing metalloenzyme in Clostridium oroticum.
    Journal of bacteriology, 1976, Volume: 127, Issue:2

    Topics: Amidohydrolases; Aspartic Acid; Cell-Free System; Clostridium; Edetic Acid; Hydrogen-Ion Concentration; Metalloproteins; Molecular Weight; Orotic Acid; Phenanthrolines; Phosphates; Zinc

1976
Conjugation in Tetrahymena pyriformis. The effect of polylysine, concanavalin A, and bivalent metals on the conjugation process.
    The Journal of cell biology, 1976, Volume: 70, Issue:2 pt 1

    Topics: Animals; Aspartic Acid; Concanavalin A; Conjugation, Genetic; Dextrans; Edetic Acid; Egtazic Acid; Glucosamine; Methylmannosides; Peptides; Phenanthrolines; Polylysine; Tetrahymena pyriformis

1976
Inhibitors of 2-ketoglutarate-dependent dioxygenases block aspartyl beta-hydroxylation of recombinant human factor IX in several mammalian expression systems.
    The Journal of biological chemistry, 1989, Apr-25, Volume: 264, Issue:12

    Topics: 2,2'-Dipyridyl; Animals; Aspartic Acid; Cell Line; Cricetinae; Endothelium, Vascular; Factor IX; Hydrolases; Hydroxylation; Phenanthrolines; Protein Processing, Post-Translational; Pyridines; Recombinant Proteins; Structure-Activity Relationship

1989
Significance of Cys-153 for the phosphatase activity of glyceraldehyde-3-phosphate dehydrogenase.
    Biomedica biochimica acta, 1985, Volume: 44, Issue:9

    Topics: Acid Anhydride Hydrolases; Acylphosphatase; Animals; Aspartic Acid; Cystine; Edetic Acid; Enzyme Activation; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycine; Ligands; NAD; Phenanthrolines; Phosphoric Monoester Hydrolases; Swine

1985
A spectrophotometric method for qualitative and quantitative determination of sialic acid in glycoproteins and glycopeptides.
    Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 1973, Volume: 354, Issue:2

    Topics: Aspartic Acid; Binding Sites; Evaluation Studies as Topic; Female; Fetal Proteins; Glycopeptides; Glycoproteins; Humans; Methods; Phenanthrolines; Pregnancy; Protein Binding; Sialic Acids; Spectrophotometry, Ultraviolet

1973
Effect of magnesium chelators on the regulation of pyruvate oxidation by rabbit heart mitochondria.
    Biochemistry, 1972, Oct-24, Volume: 11, Issue:22

    Topics: Adenine Nucleotides; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Asparagine; Aspartic Acid; Barbiturates; Chelating Agents; Depression, Chemical; Heart; Magnesium; Mitochondria, Muscle; Myocardium; Nitriles; Oxygen Consumption; Phenanthrolines; Phenylhydrazines; Pyridines; Pyruvates; Rabbits; Structure-Activity Relationship; Uncoupling Agents

1972
Chemical state of 99mTc in biomedical products.
    Journal of nuclear medicine : official publication, Society of Nuclear Medicine, 1971, Volume: 12, Issue:9

    Topics: Ascorbic Acid; Aspartic Acid; Chelating Agents; Chromatography, Gel; Citrates; Electrolysis; Humans; Iron; Malates; Pentetic Acid; Phenanthrolines; Serum Albumin; Technetium; Zirconium

1971
Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium.
    Journal of molecular biology, 1993, Jul-20, Volume: 232, Issue:2

    Topics: Aspartic Acid; Bacterial Proteins; Chemotaxis; Escherichia coli; Escherichia coli Proteins; Gold; Membrane Proteins; Mercury; Models, Molecular; Peptide Fragments; Phenanthrolines; Platinum; Protein Conformation; Receptors, Amino Acid; Salmonella typhimurium; Signal Transduction; X-Ray Diffraction

1993
Molecular motions of the outer ring of charge of the sodium channel: do they couple to slow inactivation?
    The Journal of general physiology, 2003, Volume: 122, Issue:3

    Topics: Amino Acid Substitution; Animals; Aspartic Acid; Cysteine; Electrophysiology; Glutamic Acid; Ion Channel Gating; Molecular Conformation; Muscle, Skeletal; Mutation; Oocytes; Phenanthrolines; Rats; Sodium Channels; Xenopus laevis

2003
Site-directed disulfide mapping of residues contributing to the Ca2+ and K+ binding pocket of the NCKX2 Na+/Ca2+-K+ exchanger.
    Biochemistry, 2005, May-31, Volume: 44, Issue:21

    Topics: Amino Acid Sequence; Aspartic Acid; Binding Sites; Calcium; Cell Line; Cell Membrane; Cross-Linking Reagents; Cysteine; Disulfides; Glutamic Acid; Humans; Hydrolysis; Hydrophobic and Hydrophilic Interactions; Molecular Sequence Data; Mutagenesis, Insertional; Peptide Mapping; Phenanthrolines; Potassium; Protein Sorting Signals; Protein Structure, Secondary; Repetitive Sequences, Amino Acid; Serine; Sodium-Calcium Exchanger

2005
Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1.
    American journal of physiology. Cell physiology, 2007, Volume: 293, Issue:4

    Topics: Amino Acid Sequence; Amino Acid Substitution; Amino Acid Transport Systems, Neutral; Animals; Aspartic Acid; Binding Sites; Biological Transport; Cross-Linking Reagents; Cysteine; Dithiothreitol; Female; Insect Proteins; Kinetics; Lepidoptera; Lysine; Models, Molecular; Molecular Sequence Data; Oocytes; Phenanthrolines; Potassium; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Sodium; Tryptophan; Xenopus laevis

2007
Substrates and non-transportable analogues induce structural rearrangements at the extracellular entrance of the glial glutamate transporter GLT-1/EAAT2.
    The Journal of biological chemistry, 2008, Sep-26, Volume: 283, Issue:39

    Topics: Amino Acid Substitution; Aspartic Acid; Cadmium; Chelating Agents; Excitatory Amino Acid Agonists; Excitatory Amino Acid Transporter 2; HeLa Cells; Humans; Kainic Acid; Mutation, Missense; Phenanthrolines; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Substrate Specificity

2008
Cysteine mutagenesis reveals alternate proximity between transmembrane domain 2 and hairpin loop 1 of the glutamate transporter EAAT1.
    Amino acids, 2014, Volume: 46, Issue:7

    Topics: Amino Acid Sequence; Aspartic Acid; Cadmium Chloride; Cross-Linking Reagents; Cysteine; Dithiothreitol; Excitatory Amino Acid Transporter 1; Glutamic Acid; HeLa Cells; Humans; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenanthrolines; Protein Structure, Tertiary; Structure-Activity Relationship

2014