heme has been researched along with asparagine in 31 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (12.90) | 18.7374 |
| 1990's | 11 (35.48) | 18.2507 |
| 2000's | 10 (32.26) | 29.6817 |
| 2010's | 6 (19.35) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Erman, JE; Kraut, J; Mauro, JM; Miller, MA; Vitello, LB | 1 |
| Brayer, GD; Funk, WD; Lo, TP; MacGillivray, RT; Mauk, AG; Mauk, MR | 1 |
| Erman, JE; Kraut, J; Mauro, JM; Satterlee, JD | 1 |
| Boxer, SG; Gray, HB; Varadarajan, R; Zewert, TE | 1 |
| Baldassare, JJ; Bunn, HF; Ho, C; Lindstrom, TR | 1 |
| Tanaka, Y | 1 |
| Dus, K; Erbes, DL; Gunsalus, IC; Katagiri, M; Yu, CA | 1 |
| Morishima, I; Nagano, S; Tanaka, M; Watanabe, Y | 1 |
| Dalbøge, H; Tams, JW; Veitch, NC; Vind, J; Welinder, KG | 1 |
| Koshy, TI; Luntz, TL; Margoliash, E; Sanishvili, R; Schejter, A; Vig, I | 1 |
| Marzocchi, MP; Neri, F; Smulevich, G; Welinder, KG | 1 |
| Galactéros, F; Groff, P; Kalmes, G; Kiger, L; Kister, J; Promé, D; Wajcman, H | 1 |
| Bogumil, R; Brayer, GD; Luo, Y; Mauk, AG; Maurus, R; Overall, CM; Smith, M | 1 |
| Brandt, U; Meunier, B; Ortwein, C; Rich, PR | 1 |
| Hendrich, MP; Ho, C; Ho, NT; Jeong, ST | 1 |
| Bravo, J; Carpena, X; Fita, I; Loewen, PC; Maté, MJ; Melik-Adamyan, W; Switala, J | 1 |
| Antholine, W; Ferguson-Miller, S; Kang, UG; Schmidt, B; Zhen, Y | 1 |
| Banerjee, R; Blom, H; Boers, GH; Evande, R | 1 |
| Ciaccio, C; Coletta, M; De Sanctis, G; Feis, A; Neri, F; Santoni, E; Smulevich, G; Welinder, KG | 1 |
| Brzezinski, P; Ferguson-Miller, S; Gennis, RB; Mills, D; Morgan, J; Namslauer, A; Pawate, AS | 1 |
| Brunori, M; D'Itri, E; Forte, E; Giuffrè, A; Ludwig, B; Richter, OM; Sarti, P; Scandurra, FM | 1 |
| Ambrogelly, A; Feng, L; Namgoong, S; Polycarpo, C; Randau, L; Sheppard, K; Söll, D; Tumbula-Hansen, D | 1 |
| Gurel, E; Mandaci, S; Ozturk, M; Watmough, NJ | 1 |
| Boeglin, WE; Brash, AR; Gao, B | 1 |
| Banerjee, S; Calisto, BM; Carpena, X; Fita, I; Furtmüller, PG; Obinger, C; Rovira, C; Schroettner, K; Soudi, M; Stampler, J; Vidossich, P | 1 |
| Gunner, MR; Zhang, J | 1 |
| Battistuzzi, G; Bellei, M; Furtmüller, PG; Gruber, C; Obinger, C; Soudi, M; Stampler, J | 1 |
| Hisabori, T; Sugano, Y; Tsuge, H; Yoshida, T | 1 |
| Hargis, JC; Vankayala, SL; Woodcock, HL | 1 |
| Chauhan, VS; Kumari, P; Sahal, D | 1 |
| Fan, CZ; Li, YT; Pan, ZF; Tang, WY; Wang, W | 1 |
1 review(s) available for heme and asparagine
| Article | Year |
|---|---|
Aminoacyl-tRNA synthesis by pre-translational amino acid modification.
Topics: Amino Acids; Amino Acyl-tRNA Synthetases; Archaea; Asparagine; Bacillus subtilis; Chlorophyll; Escherichia coli; Glutamine; Heme; Models, Biological; Phylogeny; Porphyrins; Protein Modification, Translational; RNA, Transfer, Amino Acyl; Species Specificity | 2004 |
30 other study(ies) available for heme and asparagine
| Article | Year |
|---|---|
Effect of Asp-235-->Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase.
Topics: Asparagine; Aspartic Acid; Buffers; Cytochrome-c Peroxidase; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; Nitrates; Phosphates; Spectrum Analysis | 1992 |
Mutagenic, electrochemical, and crystallographic investigation of the cytochrome b5 oxidation-reduction equilibrium: involvement of asparagine-57, serine-64, and heme propionate-7.
Topics: Amino Acid Sequence; Animals; Asparagine; Base Sequence; Cattle; Cytochromes b5; DNA; Electrochemistry; Escherichia coli; Heme; Molecular Sequence Data; Mutation; Oxidation-Reduction; Protein Conformation; Serine; X-Ray Diffraction | 1990 |
Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Topics: Asparagine; Aspartic Acid; Cytochrome-c Peroxidase; Escherichia coli; Fungal Proteins; Heme; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Fusion Proteins; Saccharomyces cerevisiae | 1990 |
Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin.
Topics: Asparagine; Aspartic Acid; Glutamates; Glutamic Acid; Heme; Humans; Mutation; Myoglobin; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Thermodynamics; Valine | 1989 |
Nuclear magnetic resonance and spin-label studies of hemoglobin Kempsey.
Topics: Asparagine; Aspartic Acid; Australia; Carboxyhemoglobin; Cyclic N-Oxides; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Inositol; Iodoacetates; Ligands; Magnetic Resonance Spectroscopy; Mutation; Organophosphorus Compounds; Piperidines; Protein Conformation; Spin Labels | 1973 |
The N-terminal structure of adult hemoglobin from Japanese monkey (Macaca fuscata fuscata) and the N-terminal amino acids of all the tryptic peptides from its alpha and beta polypeptide chains.
Topics: Amino Acids; Animals; Asparagine; Chromatography, Paper; Countercurrent Distribution; Globins; Haplorhini; Heme; Hemoglobins; Humans; Peptides; Serine; Spectrophotometry; Time Factors; Trypsin | 1969 |
Chemical characterization of cytochrome P-450cam.
Topics: Amino Acid Sequence; Amino Acids; Asparagine; Aspartic Acid; Autoanalysis; Camphor; Carbohydrates; Carboxypeptidases; Chemical Phenomena; Chemistry; Cytochromes; Formates; Heme; Hydrazines; Hydrogen-Ion Concentration; Isoelectric Focusing; Isoflurophate; Molecular Weight; Nitrobenzenes; Peptides; Porphyrins; Pseudomonas; Valine | 1970 |
Putative hydrogen bond network in the heme distal site of horseradish peroxidase.
Topics: Amino Acid Sequence; Asparagine; Cloning, Molecular; Electron Transport Complex IV; Escherichia coli; Heme; Horseradish Peroxidase; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Spectrophotometry; Valine | 1995 |
NMR studies of recombinant Coprinus peroxidase and three site-directed mutants. Implications for peroxidase substrate binding.
Topics: Amino Acid Sequence; Asparagine; Binding Sites; Coprinus; Glutamine; Heme; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Peroxidase; Phenylalanine; Recombinant Proteins; Substrate Specificity | 1994 |
Effects of mutating Asn-52 to isoleucine on the haem-linked properties of cytochrome c.
Topics: Animals; Asparagine; Cyanides; Cytochrome c Group; Heme; Hydrogen-Ion Concentration; Ions; Isoleucine; Mutagenesis, Site-Directed; Oxidation-Reduction; Rats; Saccharomyces cerevisiae | 1994 |
Versatility of heme coordination demonstrated in a fungal peroxidase. Absorption and resonance Raman studies of Coprinus cinereus peroxidase and the Asp245-->Asn mutant at various pH values.
Topics: Asparagine; Aspartic Acid; Catalysis; Coprinus; Ferrous Compounds; Heme; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Peroxidases; Spectrum Analysis, Raman | 1996 |
Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme.
Topics: Adult; Alanine; Asparagine; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrolysis; Male; Mutation; Oxygen | 1996 |
A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket.
Topics: Animals; Asparagine; Binding Sites; Circular Dichroism; Electron Spin Resonance Spectroscopy; Escherichia coli; Heme; Horses; Leucine; Molecular Sequence Data; Mutation; Myocardium; Myoglobin; Nucleic Acid Conformation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Spectrophotometry | 1997 |
Effects of mutation of residue I67 on redox-linked protonation processes in yeast cytochrome c oxidase.
Topics: Asparagine; Electron Transport Complex IV; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Isoleucine; Kinetics; Macromolecular Substances; Models, Molecular; Oxidation-Reduction; Point Mutation; Potentiometry; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae | 1998 |
Recombinant hemoglobin(alpha 29leucine --> phenylalanine, alpha 96valine --> tryptophan, beta 108asparagine --> lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation.
Topics: Amino Acid Substitution; Asparagine; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Heme; Hemoglobins; Humans; Kinetics; Leucine; Lysine; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxygen; Oxyhemoglobins; Phenylalanine; Protein Binding; Recombinant Proteins; Tryptophan; Valine | 1999 |
Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli.
Topics: Alleles; Asparagine; Binding Sites; Catalase; Catalysis; Crystallization; Escherichia coli; Heme; Histamine; Hydrogen Peroxide; Models, Molecular; Mutation; Oxidation-Reduction; Solvents | 2001 |
Mutants of the CuA site in cytochrome c oxidase of Rhodobacter sphaeroides: I. Spectral and functional properties.
Topics: Amino Acid Substitution; Asparagine; Cell Membrane; Copper; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Glycine; Heme; Histidine; Iron; Kinetics; Leucine; Manganese; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Secondary; Proton Pumps; Rhodobacter sphaeroides; Spectrometry, Fluorescence; Spectrophotometry; Spectroscopy, Fourier Transform Infrared | 2002 |
Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase.
Topics: Allosteric Regulation; Amino Acid Substitution; Asparagine; Aspartic Acid; Carbon Monoxide; Cell Line; Cystathionine beta-Synthase; Enzyme Activation; Ferrous Compounds; Fibroblasts; Heme; Humans; Kinetics; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Recombinant Proteins; RNA, Messenger; S-Adenosylmethionine | 2002 |
Fine-tuning of the binding and dissociation of CO by the amino acids of the heme pocket of Coprinus cinereus peroxidase.
Topics: Amino Acid Substitution; Amino Acids; Anions; Arginine; Asparagine; Aspartic Acid; Carbon Monoxide; Coprinus; Cytochrome-c Peroxidase; Ferrous Compounds; Heme; Kinetics; Ligands; Mutation; Peroxidase; Phenylalanine; Protein Binding; Spectrophotometry, Infrared; Spectrum Analysis, Raman | 2002 |
A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping.
Topics: Amino Acid Substitution; Asparagine; Aspartic Acid; Cold Temperature; Electron Transport Complex IV; Enzyme Activation; Heme; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Photolysis; Proton Pumps; Rhodobacter sphaeroides; Spectrophotometry, Ultraviolet | 2002 |
Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants.
Topics: Amino Acid Substitution; Anaerobiosis; Asparagine; Aspartic Acid; Calibration; Electron Transport Complex IV; Heme; Lysine; Methionine; Oxidation-Reduction; Paracoccus denitrificans; Phenolsulfonphthalein; Protein Subunits; Protons; Spectrophotometry | 2004 |
Site-directed mutagenesis of five conserved residues of subunit i of the cytochrome cbb3 oxidase in Rhodobacter capsulatus.
Topics: Amino Acid Sequence; Amino Acids; Asparagine; Bacterial Proteins; Catalysis; Cytochromes c; Electron Transport Complex IV; Electrophoresis, Polyacrylamide Gel; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Subunits; Rhodobacter capsulatus; Sequence Homology, Amino Acid; Serine; Structure-Activity Relationship; Threonine | 2007 |
Role of the conserved distal heme asparagine of coral allene oxide synthase (Asn137) and human catalase (Asn148): mutations affect the rate but not the essential chemistry of the enzymatic transformations.
Topics: Amino Acid Sequence; Animals; Anthozoa; Asparagine; Catalase; Conserved Sequence; Enzyme Activation; Enzyme Stability; Heme; Humans; Intramolecular Oxidoreductases; Kinetics; Molecular Sequence Data; Mutation; Species Specificity; Structure-Activity Relationship | 2008 |
Essential role of proximal histidine-asparagine interaction in mammalian peroxidases.
Topics: Asparagine; Cell Line; Chlorides; Crystallography, X-Ray; Glycosylation; Heme; Histidine; Humans; Hypochlorous Acid; Lactoperoxidase; Leukocytes; Mutation, Missense; Oxidation-Reduction; Peroxidase; Protein Processing, Post-Translational; Protein Structure, Tertiary | 2009 |
Multiconformation continuum electrostatics analysis of the effects of a buried Asp introduced near heme a in Rhodobacter sphaeroides cytochrome c oxidase.
Topics: Asparagine; Electron Transport; Electron Transport Complex IV; Heme; Hydrogen Bonding; Oxidation-Reduction; Protons; Rhodobacter sphaeroides; Static Electricity; Thermodynamics; Water | 2010 |
Manipulating the proximal triad His-Asn-Arg in human myeloperoxidase.
Topics: Amino Acid Substitution; Arginine; Asparagine; Binding Sites; Cell Line; Cloning, Molecular; Ferric Compounds; Ferrous Compounds; Heme; Histidine; Humans; Models, Molecular; Mutant Proteins; Oxidation-Reduction; Peroxidase | 2011 |
Crystal structures of dye-decolorizing peroxidase with ascorbic acid and 2,6-dimethoxyphenol.
Topics: Arginine; Ascorbic Acid; Asparagine; Binding Sites; Coloring Agents; Crystallography, X-Ray; Heme; Hemeproteins; Hydrogen Bonding; Peroxidase; Protein Structure, Tertiary; Pyrogallol; Substrate Specificity; Water | 2012 |
How does catalase release nitric oxide? A computational structure-activity relationship study.
Topics: Asparagine; Catalase; Catalytic Domain; Glycine; Heme; Histidine; Humans; Hydrogen Bonding; Hydroxyurea; Isoenzymes; Kinetics; Molecular Docking Simulation; Molecular Dynamics Simulation; Nitric Oxide; Structure-Activity Relationship; Thermodynamics | 2013 |
Dendrimeric template of Plasmodium falciparum histidine rich protein II repeat motifs bearing Asp→Asn mutation exhibits heme binding and β-hematin formation.
Topics: Amino Acid Motifs; Amino Acid Sequence; Antigens, Protozoan; Asparagine; Aspartic Acid; Bicarbonates; Binding Sites; Chromatography, High Pressure Liquid; Chromatography, Reverse-Phase; Dendrimers; Heme; Hemeproteins; Kinetics; Mass Spectrometry; Molecular Sequence Data; Mutation; Plasmodium falciparum; Protein Binding; Protein Stability; Protozoan Proteins; Repetitive Sequences, Amino Acid; Spectrum Analysis; Structure-Activity Relationship; Titrimetry | 2014 |
[Research on Early Diagnosis of Gastric Cancer by the Surface Enhanced Raman Spectroscopy of Human Hemoglobin].
Topics: Asparagine; Early Detection of Cancer; Heme; Hemoglobins; Humans; Methemoglobin; Multivariate Analysis; Oxyhemoglobins; Phenylalanine; Principal Component Analysis; Spectrum Analysis, Raman; Stomach Neoplasms; Tyrosine | 2015 |