protoporphyrin ix has been researched along with histidine in 12 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (25.00) | 18.2507 |
2000's | 5 (41.67) | 29.6817 |
2010's | 4 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cocco, MJ; Lecomte, JT | 1 |
Johjima, T; Tanaka, H; Wariishi, H | 1 |
Chu, GC; Ikeda-Saito, M; Sönnichsen, FD; Tomita, T; Yoshida, T | 1 |
Delepierre, M; Deniau, C; Kumar, V; Lecroisey, A; Létoffé, S; Simenel, C; Stojiljkovic, I; Wandersman, C; Wolff, N | 1 |
Schmidt, P; Schramm, M; Schröder, H; Stasch, JP | 1 |
Berezhna, S; Cao, W; Champion, PM; Demidov, AA; Georgiev, GY; Sage, JT; Sjodin, T; Wang, W; Ye, X | 1 |
Austin, CJ; Jamie, JF; Kosim-Satyaputra, P; Matin, A; Mizdrak, J; Parker, MW; Polekhina, G; Roberts, TH; Sirijovski, N; Truscott, RJ; Willows, RD | 1 |
Al-Karadaghi, S; Hansson, M; Hansson, MD; Karlberg, T; Rahardja, MA | 1 |
Chung, CW; Jeong, YI; Johnson, RP; Kang, DH; Kim, I; Suh, H | 1 |
Shen, Y; Wang, Y | 1 |
Bielecki, M; Olczak, M; Olczak, T; Smalley, JW; Wojaczyński, J; Wójtowicz, H | 1 |
Curnow, A; Dodd, NJF; Dogra, Y; Ferguson, DCJ; Smerdon, GR; Winyard, PG | 1 |
12 other study(ies) available for protoporphyrin ix and histidine
Article | Year |
---|---|
Structural features of the protoporphyrin-apomyoglobin complex: a proton NMR spectroscopy study.
Topics: Amino Acid Sequence; Animals; Apoproteins; Binding Sites; Histidine; Horses; Hydrogen; Iron; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Myoglobin; Protein Binding; Protein Conformation; Protons; Protoporphyrins; Whales; X-Ray Diffraction | 1990 |
The effect of ligand field strength on nonresonance Raman characteristics of hemoproteins.
Topics: Animals; Binding Sites; Cattle; Cytochrome c Group; Hemeproteins; Histidine; Horseradish Peroxidase; Horses; Iron; Ligands; Methemoglobin; Metmyoglobin; Myocardium; Protoporphyrins; Spectrophotometry, Infrared; Spectrum Analysis, Raman | 1996 |
The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site.
Topics: Bacterial Proteins; Binding Sites; Cobalt; Corynebacterium diphtheriae; Electron Spin Resonance Spectroscopy; Heme Oxygenase (Decyclizing); Hemin; Histidine; Hydrogen-Ion Concentration; Iron; Magnetic Resonance Spectroscopy; Multienzyme Complexes; Protoporphyrins; Spectrophotometry; Spectrum Analysis, Raman | 1999 |
Histidine pK(a) shifts and changes of tautomeric states induced by the binding of gallium-protoporphyrin IX in the hemophore HasA(SM).
Topics: Bacterial Proteins; Binding Sites; Carrier Proteins; Crystallography, X-Ray; Escherichia coli; Gallium; Heme; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Membrane Proteins; Models, Molecular; Protein Binding; Protein Conformation; Protoporphyrins | 2002 |
Preparation of heme-free soluble guanylate cyclase.
Topics: Benzoates; Chromatography, Ion Exchange; Cyclic GMP; Enzyme Activation; Enzyme Activators; Guanosine Triphosphate; Guanylate Cyclase; Heme; Hemeproteins; Histidine; Indazoles; Nitroprusside; Polysorbates; Proteins; Protoporphyrins; Spectrophotometry; Zinc | 2003 |
Proximal and distal influences on ligand binding kinetics in microperoxidase and heme model compounds.
Topics: Animals; Carbon Monoxide; Heart; Heme; Histidine; Horses; Imidazoles; Kinetics; Ligands; Models, Molecular; Myoglobin; Peroxidases; Photolysis; Protein Binding; Protein Conformation; Protoporphyrins; Spectrum Analysis, Raman; Time Factors | 2004 |
Optimised expression and purification of recombinant human indoleamine 2,3-dioxygenase.
Topics: Aminolevulinic Acid; Biochemistry; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Heme; Histidine; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Iron; Isopropyl Thiogalactoside; Kynurenine; Plasmids; Protoporphyrins; Recombinant Proteins; Temperature; Time Factors; Tryptophan; Tryptophan Oxygenase | 2004 |
Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX.
Topics: Bacillus subtilis; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Ferrochelatase; Glutamic Acid; Histidine; Iron; Models, Molecular; Mutagenesis, Site-Directed; Protoporphyrins; Water | 2007 |
Poly(L-histidine)-tagged 5-aminolevulinic acid prodrugs: new photosensitizing precursors of protoporphyrin IX for photodynamic colon cancer therapy.
Topics: Aminolevulinic Acid; Apoptosis; Cell Survival; Colonic Neoplasms; Flow Cytometry; HCT116 Cells; HEK293 Cells; Histidine; Humans; Hydrogen-Ion Concentration; Models, Molecular; Photochemotherapy; Photosensitizing Agents; Prodrugs; Protoporphyrins | 2012 |
Is it possible for Fe2+ to approach protoporphyrin IX from the side of Tyr-13 in Bacillus subtilis ferrochelatase? An answer from QM/MM study.
Topics: Bacillus subtilis; Bacterial Proteins; Cations, Divalent; Ferrochelatase; Histidine; Humans; Iron; Kinetics; Molecular Dynamics Simulation; Protons; Protoporphyrins; Quantum Theory; Thermodynamics; Tyrosine; Water | 2013 |
The Porphyromonas gingivalis HmuY haemophore binds gallium(iii), zinc(ii), cobalt(iii), manganese(iii), nickel(ii), and copper(ii) protoporphyrin IX but in a manner different to iron(iii) protoporphyrin IX.
Topics: Absorption; Bacterial Proteins; Circular Dichroism; Cobalt; Copper; Gallium; Heme; Hemeproteins; Histidine; Ligands; Magnetic Resonance Spectroscopy; Manganese; Metals; Mutant Proteins; Nickel; Porphyromonas gingivalis; Protein Binding; Protoporphyrins; Spectrophotometry, Ultraviolet; Zinc | 2013 |
The hydroxypyridinone iron chelator CP94 increases methyl-aminolevulinate-based photodynamic cell killing by increasing the generation of reactive oxygen species.
Topics: Aminolevulinic Acid; Cell Line, Tumor; Cell Survival; Histidine; Humans; Iron Chelating Agents; Metalloporphyrins; Photochemotherapy; Photosensitizing Agents; Protoporphyrins; Pyridones; Reactive Oxygen Species | 2016 |