spermine and heme
spermine has been researched along with heme in 8 studies
Research
Studies (8)
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 3 (37.50) | 18.7374 |
1990's | 2 (25.00) | 18.2507 |
2000's | 1 (12.50) | 29.6817 |
2010's | 1 (12.50) | 24.3611 |
2020's | 1 (12.50) | 2.80 |
Authors
Authors | Studies |
---|---|
Butterfield, DA; Palmieri, DA; Rangachari, A | 1 |
Gross, M; Rubino, MS | 1 |
Dulaney, JT; Hatch, FE; Young, J | 1 |
Edwards, PM; Frankena, H; Schotman, P; Schrama, LH | 1 |
Antholine, W; Juckett, M; Pastor, T; Vercellotti, G; Weber, M; Yuan, H; Zheng, Y | 1 |
Ahmad, M; Chow, JL; Gupte, SA; Mingone, CJ; Wolin, MS | 1 |
Chanana, V; Gaur, V; Jain, A; Salunke, DM | 1 |
Bartlam, M; Che, S; Chen, Y; Liang, Y; Liu, R; Wu, W; Zhang, Q | 1 |
Other Studies
8 other study(ies) available for spermine and heme
Article | Year |
---|---|
Effects of domain-specific erythrocyte membrane modulators on acetylcholinesterase and NADH:cytochrome b5 reductase activities.
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.
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.
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.
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.
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.
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.
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.
Topics: Heme; Oxidoreductases Acting on CH-NH Group Donors; Polyamine Oxidase; Pseudomonas aeruginosa; Spermidine; Spermine | 2022 |