protoporphyrin ix has been researched along with arginine in 7 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 2 (28.57) | 18.2507 |
2000's | 4 (57.14) | 29.6817 |
2010's | 1 (14.29) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Belushkina, NN; Severina, IS | 1 |
Curtis, MA; Harper, F; U, S | 1 |
Andreoletti, P; Gagnon, J; Jaquinod, M; Jouve, HM; Sainz, G | 1 |
Brown, KA; Moody, PC; Raven, EL; Sharp, KH | 1 |
Shimizu, T; Tanaka, A | 1 |
Graczyk, A; Kasprzycka-Guttman, T; Misiewicz-Krzemińska, I; Skupińska, K | 1 |
Aljabri, MD; Bhosale, SV; Gosavi, NM; Jones, LA; La, DD; Morajkar, PP | 1 |
7 other study(ies) available for protoporphyrin ix and arginine
Article | Year |
---|---|
Increase in activating ability of human platelet guanylate cyclase during aggregation.
Topics: Adenosine Diphosphate; Arachidonic Acid; Arginine; Blood Platelets; Cyclic GMP; Enzyme Activation; Guanylate Cyclase; Humans; Nitroprusside; Platelet Aggregation; Protoporphyrins | 1992 |
Haemin inhibits the trypsin-like enzyme activity of Porphyromonas gingivalis W83.
Topics: Arginine; Bacteroides; Chlorophyll; Electrophoresis, Polyacrylamide Gel; Hemin; Humans; Immunoglobulin G; Porphyrins; Protoporphyrins; Trypsin Inhibitors | 1990 |
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron.
Topics: Acetates; Anions; Arginine; Binding Sites; Catalase; Catalysis; Crystallography, X-Ray; Heme; Hydrogen Bonding; Iron; Models, Molecular; NADP; Protein Conformation; Proteus mirabilis; Protoporphyrins; Recombinant Proteins; Spectrum Analysis; Sulfates | 2003 |
Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex.
Topics: Arginine; Ascorbate Peroxidases; Binding Sites; Crystallography, X-Ray; Glycine max; Heme; Iron; Models, Molecular; Molecular Structure; Peroxidases; Protein Structure, Tertiary; Protons; Protoporphyrins; Salicylamides; Spectrophotometry | 2004 |
Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand
Topics: Animals; Arginine; Catalysis; Cattle; Cyclic GMP; Escherichia coli Proteins; Ferric Compounds; Heme; Ligands; Methionine; Mutagenesis, Site-Directed; Phenylalanine; Phosphoric Diester Hydrolases; Protein Binding; Protein Structure, Tertiary; Protoporphyrins | 2008 |
Influence of protoporphyrin IX amino acid substituents on affinity to human breast adenocarcinoma MCF-7 cells.
Topics: Amino Acids, Diamino; Arginine; Breast Neoplasms; Cell Line, Tumor; Cell Survival; Female; Histocytochemistry; Humans; Microscopy, Fluorescence; Protoporphyrins | 2009 |
Arginine-Induced Self-Assembly of Protoporphyrin to Obtain Effective Photocatalysts in Aqueous Media Under Visible Light.
Topics: Arginine; Catalysis; Light; Nanoparticles; Protoporphyrins; Water | 2019 |