Page last updated: 2024-08-17

nad and dihydroxyphenylalanine

nad has been researched along with dihydroxyphenylalanine in 17 studies

Research

Studies (17)

TimeframeStudies, this research(%)All Research%
pre-199013 (76.47)18.7374
1990's3 (17.65)18.2507
2000's0 (0.00)29.6817
2010's1 (5.88)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Harris, EB; Prabhakaran, K1
Augusto, O; Bechara, EJ; Cilento, G; Sanioto, DL1
Lovstad, RA1
Birkmayer, W; Mentasti, M1
Hayaishi, O; Nozaki, M1
Birkmayer, W1
Odajima, T1
Wilson-Jones, E1
Black, MM; Wilson-Jones, E1
Gan, EV; Haberman, HF; Menon, IA1
Shichi, H1
Benoiton, NL; D'Iorio, A; Tong, JH1
Davies, DS; McManus, ME1
Blarzino, C; Coccia, R; De Marco, C; Mosca, L; Musci, G; Rosei, MA1
Rosei, MA1
Roskoski, R; Stokes, AH; Vrana, KE; Xu, Y1
García-Cánovas, F; Garcia-Molina, F; Garcia-Molina, M; Garcia-Ruiz, PA; Munoz-Munoz, JL; Rodriguez-Lopez, JN; Tudela, J1

Reviews

1 review(s) available for nad and dihydroxyphenylalanine

ArticleYear
The importance of monoamine metabolism for the pathology of the extrapyramidal system.
    Journal of neuro-visceral relations, 1969, Volume: 31

    Topics: Aged; Animals; Aromatic Amino Acid Decarboxylase Inhibitors; Brain; Catechol Oxidase; Catecholamines; Chorea; Dihydroxyphenylalanine; Dopamine; Humans; Kinetics; Methyltyrosines; Middle Aged; NAD; Parkinson Disease; Rats; Tritium; Tyrosine

1969

Other Studies

16 other study(ies) available for nad and dihydroxyphenylalanine

ArticleYear
A possible metabolic role for o-diphenoloxidase in Mycobacterium leprae.
    Experientia, 1985, Dec-15, Volume: 41, Issue:12

    Topics: Animals; Armadillos; Bacterial Proteins; Basidiomycota; Catechol Oxidase; Dihydroxyphenylalanine; Humans; Melanins; Melanoma; Monophenol Monooxygenase; Mycobacterium leprae; NAD; NADP; Oxidation-Reduction; Phenols; Quinones; Substrate Specificity

1985
The effect of o-diphenols upon the microsomal NADPH and NADH oxidase activities.
    Archives of biochemistry and biophysics, 1973, Volume: 158, Issue:1

    Topics: Animals; Catechols; Cytochrome Reductases; Dihydroxyphenylalanine; Electron Transport; Epinephrine; Kinetics; Male; Manometry; Microsomes, Liver; NAD; NADP; Oxidation-Reduction; Oxidoreductases; Rats; Spectrophotometry; Spectrophotometry, Ultraviolet; Time Factors

1973
Interaction of phenothiazine derivatives with human ceruloplasmin.
    Biochemical pharmacology, 1974, Mar-15, Volume: 23, Issue:6

    Topics: Antipsychotic Agents; Ascorbic Acid; Blood Proteins; Ceruloplasmin; Chlorpromazine; Dihydroxyphenylalanine; Dopamine; Glutathione; Humans; In Vitro Techniques; Iron; Kinetics; Magnetic Resonance Spectroscopy; Methotrimeprazine; NAD; NADP; Oxidation-Reduction; Promazine; Protein Binding; Spectrophotometry; Stimulation, Chemical; Sulfates; Triflupromazine

1974
[Further experimental studies on the catecholamine metabolism in extrapyramidal diseases (Parkinson and chorea syndromes)].
    Archiv fur Psychiatrie und Nervenkrankheiten, 1967, Aug-08, Volume: 210, Issue:1

    Topics: Aged; Carboxy-Lyases; Catecholamines; Chorea; Dihydroxyphenylalanine; Female; Humans; Hydrazines; Male; Middle Aged; NAD; Oxidoreductases; Parkinson Disease; Phenylalanine; Tyrosine

1967
Nature and mechanisms of oxygenases.
    Science (New York, N.Y.), 1969, Apr-25, Volume: 164, Issue:3878

    Topics: Amino Acids; Bacteria; Biotransformation; Catalysis; Catechol Oxidase; Chemical Phenomena; Chemistry; Cholesterol; Collagen; Dihydroxyphenylalanine; Flavin-Adenine Dinucleotide; Hydroxyproline; Lysine; NAD; Oxygen; Oxygenases; Phenylalanine; Plants; Prostaglandins; Squalene; Tryptophan Oxygenase; Tyrosine

1969
Myeloperoxidase of the leukocyte of normal blood. II. The oxidation-reduction reaction mechanism of the myeloperoxidase system.
    Journal de physiologie, 1970, Volume: 62

    Topics: Adrenochrome; Animals; Blood Platelets; Cytochromes; Dihydroxyphenylalanine; Dopamine; Epinephrine; Erythrocytes; Free Radicals; Hydrogen Peroxide; Iron; Leukocytes; Models, Chemical; NAD; Norepinephrine; Oxidation-Reduction; Oxidoreductases; Oxygen; Peroxidases; Phenols; Phenylalanine; Spectrophotometry; Swine; Time Factors; Tyrosine; Ultraviolet Rays

1970
Pigmented nodular hidradenoma.
    Archives of dermatology, 1971, Volume: 104, Issue:2

    Topics: Adenoma, Sweat Gland; Adenosine Triphosphatases; Adult; Alkaline Phosphatase; Dihydroxyphenylalanine; Electron Transport Complex IV; Esterases; Female; Glucosyltransferases; Glucuronidase; Histocytochemistry; Humans; Leucyl Aminopeptidase; Male; Melanocytes; Middle Aged; NAD; Oxidoreductases; Succinate Dehydrogenase; Sweat Gland Neoplasms

1971
The role of the epidermis in the histopathogenesis of lichen planus. Histochemical correlations.
    Archives of dermatology, 1972, Volume: 105, Issue:1

    Topics: Acid Phosphatase; Acute Disease; Biopsy; Catechol Oxidase; Chronic Disease; Depression, Chemical; Dihydrolipoamide Dehydrogenase; Dihydroxyphenylalanine; Electron Transport Complex IV; Esterases; Histocytochemistry; Humans; Lichen Planus; Melanocytes; NAD; Necrosis; Oxygen Consumption; Skin; Succinate Dehydrogenase

1972
Oxidation of NADH by melanin and melanoproteins.
    Biochimica et biophysica acta, 1974, Nov-25, Volume: 370, Issue:1

    Topics: Amino Acids; Animals; Catechol Oxidase; Cattle; Chymotrypsin; Dihydroxyphenylalanine; Kinetics; Melanins; Melanoma; Mice; Mice, Inbred Strains; NAD; Neoplasms, Experimental; Oxidation-Reduction; Pepsin A; Peptide Hydrolases; Peptides; Phosphoproteins; Plants; Serum Albumin, Bovine; Time Factors; Trypsin

1974
Microsomal electron transfer system of bovine retinal pigment epithelium.
    Experimental eye research, 1969, Volume: 8, Issue:1

    Topics: Animals; Cattle; Dihydroxyphenylalanine; Electron Transport; Epithelium; Eye Proteins; In Vitro Techniques; Microsomes; NAD; NADP; Retina

1969
Formation of meta-tyrosine form L-phenylalanine by beef adrenal medulla. A new biosynthetic route to catecholamines.
    Biochemical and biophysical research communications, 1971, Jul-02, Volume: 44, Issue:1

    Topics: Adrenal Medulla; Animals; Aromatic Amino Acid Decarboxylase Inhibitors; Carbon Isotopes; Catecholamines; Cattle; Chromatography, Ion Exchange; Cresols; Dihydroxyphenylalanine; Female; Hydroxylamines; Iron; Kinetics; Methyltyrosines; Monoiodotyrosine; NAD; Phenols; Phenylalanine; Pteridines; Rats; Stereoisomerism; Tyrosine; Tyrosine 3-Monooxygenase

1971
Paraquat-stimulated binding of dopa to liver and lung microsomal protein.
    Xenobiotica; the fate of foreign compounds in biological systems, 1980, Volume: 10, Issue:10

    Topics: Animals; Bridged Bicyclo Compounds; Dihydroxyphenylalanine; Lung; Male; Microsomes; Microsomes, Liver; NAD; NADP; Paraquat; Piperazines; Rats; Superoxide Dismutase

1980
Some biochemical properties of melanins from opioid peptides.
    Biochimica et biophysica acta, 1994, Mar-02, Volume: 1199, Issue:2

    Topics: Amino Acid Sequence; Aminopeptidases; Basidiomycota; Carboxypeptidases; Carboxypeptidases A; CD13 Antigens; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Endorphins; Enkephalins; Kinetics; Melanins; Molecular Sequence Data; Monophenol Monooxygenase; NAD; Oxidation-Reduction; Pronase; Solubility

1994
Melanins from opioid peptides.
    Pigment cell research, 1996, Volume: 9, Issue:6

    Topics: Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Melanins; Monophenol Monooxygenase; NAD; Opioid Peptides; Oxidation-Reduction; Photochemistry; Solubility; Spectrophotometry; Structure-Activity Relationship; Substrate Specificity; Ultraviolet Rays

1996
Dopamine, in the presence of tyrosinase, covalently modifies and inactivates tyrosine hydroxylase.
    Journal of neuroscience research, 1998, Dec-01, Volume: 54, Issue:5

    Topics: Animals; Antioxidants; Chromatography, Gel; Dihydroxyphenylalanine; Dithiothreitol; Dopamine; Electrophoresis, Polyacrylamide Gel; Feedback; Glutathione; Monophenol Monooxygenase; NAD; Neoplasm Proteins; Nerve Tissue Proteins; Parkinson Disease; PC12 Cells; Plant Proteins; Precipitin Tests; Rats; Tyrosine 3-Monooxygenase

1998
Melanogenesis inhibition due to NADH.
    Bioscience, biotechnology, and biochemistry, 2010, Volume: 74, Issue:9

    Topics: Agaricales; Benzoquinones; Dihydroxyphenylalanine; Fungal Proteins; Indoles; Kinetics; Melanins; Monophenol Monooxygenase; NAD; Oxidation-Reduction; Substrate Specificity

2010