spermine and heme

spermine has been researched along with heme in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19903 (37.50)18.7374
1990's2 (25.00)18.2507
2000's1 (12.50)29.6817
2010's1 (12.50)24.3611
2020's1 (12.50)2.80

Authors

AuthorsStudies
Butterfield, DA; Palmieri, DA; Rangachari, A1
Gross, M; Rubino, MS1
Dulaney, JT; Hatch, FE; Young, J1
Edwards, PM; Frankena, H; Schotman, P; Schrama, LH1
Antholine, W; Juckett, M; Pastor, T; Vercellotti, G; Weber, M; Yuan, H; Zheng, Y1
Ahmad, M; Chow, JL; Gupte, SA; Mingone, CJ; Wolin, MS1
Chanana, V; Gaur, V; Jain, A; Salunke, DM1
Bartlam, M; Che, S; Chen, Y; Liang, Y; Liu, R; Wu, W; Zhang, Q1

Other Studies

8 other study(ies) available for spermine and heme

ArticleYear
Effects of domain-specific erythrocyte membrane modulators on acetylcholinesterase and NADH:cytochrome b5 reductase activities.
    Archives of biochemistry and biophysics, 1990, Volume: 280, Issue:1

    Topics: Acetylcholinesterase; Benzyl Alcohol; Benzyl Alcohols; Cytochrome Reductases; Cytochrome-B(5) Reductase; Electron Spin Resonance Spectroscopy; Erythrocyte Membrane; Heme; Humans; Kinetics; Lectins; Phytic Acid; Spermine; Tacrine

1990
Regulation of eukaryotic initiation factor-2B activity by polyamines and amino acid starvation in rabbit reticulocyte lysate.
    The Journal of biological chemistry, 1989, Dec-25, Volume: 264, Issue:36

    Topics: Amino Acids; Animals; Cell-Free System; Cycloheximide; Eukaryotic Initiation Factor-2; Heme; Kinetics; Phosphorylation; Rabbits; Reticulocytes; Spermidine; Spermine

1989
Effect of amines on erythropoietin-stimulated heme synthesis in fetal mouse liver cells.
    Life sciences, 1985, Apr-29, Volume: 36, Issue:17

    Topics: Amines; Animals; Cell Survival; Diamines; Erythropoietin; Fetus; Heme; In Vitro Techniques; Iron Radioisotopes; L-Lactate Dehydrogenase; Liver; Mice; Molecular Weight; Polyamines; Spermine; Structure-Activity Relationship

1985
Cyclic nucleotide- and calcium-independent phosphorylation of proteins in rat brain polyribosome: effects of ACTH, spermine, and hemin.
    Neurochemical research, 1984, Volume: 9, Issue:9

    Topics: Adrenocorticotropic Hormone; Animals; Brain; Cyclic AMP; Cyclic GMP; Heme; Hemin; In Vitro Techniques; Nerve Tissue Proteins; Phosphoric Monoester Hydrolases; Phosphorylation; Protein Kinases; Rats; Spermine

1984
Heme and the endothelium. Effects of nitric oxide on catalytic iron and heme degradation by heme oxygenase.
    The Journal of biological chemistry, 1998, Sep-04, Volume: 273, Issue:36

    Topics: Adaptation, Physiological; Cell Survival; Cytosol; Drug Interactions; Electron Spin Resonance Spectroscopy; Endothelium, Vascular; Ferritins; Heme; Heme Oxygenase (Decyclizing); Hemin; Humans; Hydrogen Peroxide; Iron; Liver; Models, Biological; Nitric Oxide; Oxidative Stress; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Spermine

1998
Heme oxygenase-1 induction depletes heme and attenuates pulmonary artery relaxation and guanylate cyclase activation by nitric oxide.
    American journal of physiology. Heart and circulatory physiology, 2008, Volume: 294, Issue:3

    Topics: Acridines; Adrenergic beta-Agonists; Animals; Blotting, Western; Cattle; Cobalt; Enzyme Activation; Enzyme Induction; Guanylate Cyclase; Heme; Heme Oxygenase-1; Isoproterenol; Luminescence; Mesoporphyrins; Muscle Contraction; Muscle Relaxation; Muscle, Smooth, Vascular; Nitric Oxide; Organ Culture Techniques; Protoporphyrins; Pulmonary Artery; Spermine; Superoxides

2008
The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants.
    Acta crystallographica. Section F, Structural biology and crystallization communications, 2011, Feb-01, Volume: 67, Issue:Pt 2

    Topics: Amino Acid Motifs; Amino Acid Sequence; Base Sequence; Calibration; Conserved Sequence; Crystallization; Crystallography, X-Ray; Dimerization; Fabaceae; Heme; Hemopexin; Hydrolysis; Hydrophobic and Hydrophilic Interactions; Lathyrus; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Molecular Weight; Pisum sativum; Plant Proteins; Plants; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Subunits; Proteome; Reference Standards; Seeds; Sequence Analysis, Protein; Sequence Homology, Amino Acid; Spermine

2011
Structure of Pseudomonas aeruginosa spermidine dehydrogenase: a polyamine oxidase with a novel heme-binding fold.
    The FEBS journal, 2022, Volume: 289, Issue:7

    Topics: Heme; Oxidoreductases Acting on CH-NH Group Donors; Polyamine Oxidase; Pseudomonas aeruginosa; Spermidine; Spermine

2022
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