carbon monoxide has been researched along with threonine in 9 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (11.11) | 18.7374 |
1990's | 3 (33.33) | 18.2507 |
2000's | 4 (44.44) | 29.6817 |
2010's | 1 (11.11) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Charache, S; Winslow, RM | 1 |
Hirose, T; Ishimura, Y; Kimata, Y; Shimada, H | 1 |
Alben, JO; Gennis, RB; Lemieux, LJ; Thomas, JW | 1 |
Brunori, M; Cavalli, V; Vallone, B; Vecchini, P | 1 |
Lukat-Rodgers, GS; Rodgers, KR; Rusnak, F; Wengenack, NL | 1 |
Ascenzi, P; Bolognesi, M; Deng, P; Dewilde, S; Geuens, E; Hale, A; Moens, L; Nardini, M; Nienhaus, GU; Nienhaus, K; Olson, JS; Pesce, A; Riggs, AF | 1 |
Ishimori, K; Morishima, I; Nagano, S; Poulos, TL; Tosha, T | 1 |
Chapman, SK; Clark, JP; Daff, SN; Miles, CS; Mowat, CG; Reid, GA; Walkinshaw, MD | 1 |
Adelroth, P; Brzezinski, P; Chang, HY; Fee, JA; Gennis, RB; Reimann, J; Smirnova, I; von Ballmoos, C | 1 |
9 other study(ies) available for carbon monoxide and threonine
Article | Year |
---|---|
Hemoglobin Richmond. Subunit dissociation and oxygen equilibrium properties.
Topics: Amino Acid Sequence; Asparagine; Binding Sites; Carbon Monoxide; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kansas; Kinetics; Lysine; Macromolecular Substances; Oxygen; Threonine; Virginia | 1975 |
Role of Thr-252 in cytochrome P450cam: a study with unnatural amino acid mutagenesis.
Topics: Alanine; Amino Acid Sequence; Base Sequence; Binding Sites; Camphor 5-Monooxygenase; Carbon Monoxide; Cytochrome P-450 Enzyme System; DNA Primers; Mixed Function Oxygenases; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; NADH, NADPH Oxidoreductases; Point Mutation; Polymerase Chain Reaction; Pseudomonas putida; Recombinant Proteins; RNA, Transfer, Amino Acyl; Spectrophotometry; Threonine; Valine | 1995 |
Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center.
Topics: Amino Acid Sequence; Binding Sites; Carbon Monoxide; Cell Membrane; Copper; Electron Transport Complex IV; Escherichia coli; Iron; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Protons; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Threonine | 1993 |
Site-directed mutagenesis in hemoglobin. Effect of some mutations at protein interfaces.
Topics: Allosteric Regulation; Arginine; Carbon Monoxide; Hemoglobin A; Histidine; Humans; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Oxygen; Protein Conformation; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Threonine; Tryptophan; Valine | 1993 |
Carbon monoxide adducts of KatG and KatG(S315T) as probes of the heme site and isoniazid binding.
Topics: Amino Acid Substitution; Antitubercular Agents; Bacterial Proteins; Binding Sites; Carbon Monoxide; Electron Spin Resonance Spectroscopy; Ferric Compounds; Heme; Isoniazid; Mycobacterium tuberculosis; Peroxidases; Serine; Spectrum Analysis, Raman; Threonine | 2001 |
Thr-E11 regulates O2 affinity in Cerebratulus lacteus mini-hemoglobin.
Topics: Animals; Carbon Monoxide; Crystallization; Hemoglobins; Hydrogen Bonding; Hydrogen-Ion Concentration; Invertebrates; Kinetics; Models, Molecular; Molecular Structure; Mutagenesis; Oxygen; Photolysis; Spectroscopy, Fourier Transform Infrared; Static Electricity; Structure-Activity Relationship; Thermodynamics; Threonine; Valine | 2004 |
Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.
Topics: Aspartic Acid; Binding Sites; Camphor; Camphor 5-Monooxygenase; Carbon Monoxide; Crystallography, X-Ray; Cysteine; Cystine; Electrons; Escherichia coli; Ferredoxins; Leucine; Magnetic Resonance Spectroscopy; Models, Molecular; Mutation; Protein Binding; Protein Conformation; Temperature; Threonine | 2004 |
The role of Thr268 and Phe393 in cytochrome P450 BM3.
Topics: Base Sequence; Carbon Monoxide; Crystallography; Cytochrome P-450 Enzyme System; DNA Primers; Escherichia coli; Hydrogen Bonding; Kinetics; Models, Molecular; Oxidation-Reduction; Phenylalanine; Spectrometry, Mass, Electrospray Ionization; Threonine | 2006 |
Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus.
Topics: Carbon Monoxide; Electron Transport Complex IV; Models, Molecular; Oxidation-Reduction; Oxygen; Point Mutation; Protons; Thermus thermophilus; Threonine | 2010 |