methane has been researched along with alpha-chymotrypsin in 21 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 7 (33.33) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 4 (19.05) | 29.6817 |
| 2010's | 9 (42.86) | 24.3611 |
| 2020's | 1 (4.76) | 2.80 |
| Authors | Studies |
|---|---|
| Chen, SN; Hoffman, MZ | 1 |
| Gentry, L; Hass, GM | 1 |
| Muszynska, G; Riordan, JF | 1 |
| Schoellmann, G | 1 |
| Steiner, RF | 1 |
| Scherrer, P; Stoeckenius, W | 1 |
| Dronova, LA; Mosolov, VV; Shul'mina, AI | 1 |
| Ermler, U; Goubeaud, M; Grabarse, W; Kahnt, J; Selmer, T; Shima, S; Thauer, RK | 1 |
| Dordick, JS; Kane, RS; Karajanagi, SS; Vertegel, AA | 1 |
| Cousins, BG; Das, AK; Hillier, IH; Kinloch, IA; Li, Y; McNamara, JP; Sharma, R; Ulijn, RV | 1 |
| Li, Z; Mu, Q; Xing, Y; Yan, B; Zhang, B; Zhou, H | 1 |
| Yan, B; Zhang, Q; Zhou, H | 1 |
| Chen, GN; Lin, ZA; Liu, B; Liu, W; Yang, HH; Zhang, XL; Zheng, C | 1 |
| Chen, ZF; Hu, K; Huang, Y; Li, M; Liang, H; Lv, Q; Zhao, S | 1 |
| Jiang, GF; Le, ZG; Sun, DZ; Xie, ZB | 1 |
| Guo, Y; Li, M; Pu, X; Xiao, X; Yuan, Y; Zhang, L | 1 |
| Chen, SZ; Esposito, EX; Hopfinger, AJ; Shao, CY; Su, BH; Tseng, YJ | 1 |
| Hao, F; Jiang, G; Liu, W; Lu, D; Zhao, X; Zhou, Q | 1 |
| Zhao, D; Zhou, J | 1 |
| Chen, J; Wang, Y; Wei, X; Xu, P; Zhou, Y | 1 |
| Calvaresi, M; Cantelli, A; Di Giosia, M; Marforio, TD; Su, Q; Valle, F; Wang, H; Zerbetto, F | 1 |
21 other study(ies) available for methane and alpha-chymotrypsin
| Article | Year |
|---|---|
Effect of pH on the reactivity of the carbonate radical in aqueous solution.
Topics: Carbonates; Chymotrypsin; Cysteine; Histidine; Hydrogen-Ion Concentration; Methane; Methionine; Muramidase; Penicillamine; Photochemistry; Propionates; Ribonucleases; Solutions; Tyrosine; Water | 1975 |
Nitration of polypeptides using ethanol in reaction buffers minimizes crosslinking.
Topics: Buffers; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Chymotrypsin; Cross-Linking Reagents; Ethanol; Indicators and Reagents; Insulin; Methane; Plant Proteins; Protease Inhibitors; Tetranitromethane | 1979 |
Chemical modification of carboxypeptidase A crystals. Nitration of tyrosine-248.
Topics: Amino Acids; Animals; Binding Sites; Carboxypeptidases; Cattle; Chymotrypsin; Methane; Peptide Fragments; Protein Binding; Tetranitromethane | 1976 |
[Specific fluorescent derivatives of macromolecules. Synthesis and characterization of N-alpha-dansyl-L-phenylalanyl-chymotrypsino (His-57)-methane and N-alpha-dansyl-L-lysyl-trypsino (His-46)-methane].
Topics: Alkylation; Chemical Phenomena; Chemistry; Chymotrypsin; Fluorescence; Lysine; Macromolecular Substances; Methane; Phenylalanine; Structure-Activity Relationship; Trypsin Inhibitors | 1972 |
The interaction of the Bowman-Birk inhibitor with trypsin and chymotrypsin.
Topics: Binding Sites; Chymotrypsin; Hydrogen-Ion Concentration; Kinetics; Methane; Nitro Compounds; Protein Binding; Spectrometry, Fluorescence; Spectrophotometry; Trypsin; Trypsin Inhibitors; Tyrosine | 1972 |
Selective nitration of tyrosines-26 and -64 in bacteriorhodopsin with tetranitromethane.
Topics: Bacteriorhodopsins; Carotenoids; Chemical Phenomena; Chemistry; Chymotrypsin; Halobacterium; Hydrogen-Ion Concentration; Methane; Photochemistry; Spectrophotometry; Structure-Activity Relationship; Tetranitromethane; Tyrosine | 1984 |
[Modification of tyrosine residues in the protein inhibitor of potato proteinases].
Topics: Chymotrypsin; Kinetics; Methane; Peptide Hydrolases; Plants; Protease Inhibitors; Protein Binding; Protein Conformation; Tetranitromethane; Trypsin Inhibitors; Tyrosine | 1980 |
The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase.
Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Chromatography, High Pressure Liquid; Chymotrypsin; Glutamine; Mass Spectrometry; Metalloporphyrins; Methane; Methanobacterium; Methionine; Methylation; Molecular Sequence Data; Molecular Structure; Oxidoreductases; Peptide Fragments; Protein Processing, Post-Translational; S-Adenosylmethionine; Sequence Analysis | 2000 |
Structure and function of enzymes adsorbed onto single-walled carbon nanotubes.
Topics: Animals; Binding Sites; Cattle; Chymotrypsin; Enzymes, Immobilized; Glycine max; Hydrophobic and Hydrophilic Interactions; Microscopy, Atomic Force; Models, Molecular; Nanotubes, Carbon; Peroxidase; Protein Structure, Secondary; Protein Structure, Tertiary; Spectroscopy, Fourier Transform Infrared | 2004 |
Enzyme-activated surfactants for dispersion of carbon nanotubes.
Topics: Chymotrypsin; Colloids; Computer Simulation; Enzyme Activation; Macromolecular Substances; Materials Testing; Models, Chemical; Models, Molecular; Molecular Conformation; Nanotechnology; Nanotubes, Carbon; Particle Size; Surface Properties; Surface-Active Agents; Thermolysin | 2009 |
Functionalized carbon nanotubes specifically bind to alpha-chymotrypsin's catalytic site and regulate its enzymatic function.
Topics: Catalytic Domain; Chymotrypsin; Combinatorial Chemistry Techniques; Drug Delivery Systems; Fluorescence; Hydrophobic and Hydrophilic Interactions; Nanotubes, Carbon | 2009 |
Reducing nanotube cytotoxicity using a nano-combinatorial library approach.
Topics: Animals; Biocompatible Materials; Carbonic Anhydrases; Cattle; Cell Proliferation; Cell Survival; Cells, Cultured; Chymotrypsin; Combinatorial Chemistry Techniques; Hemoglobins; Humans; Materials Testing; Nanotubes, Carbon; Serum Albumin, Bovine; Surface Properties | 2010 |
A selective artificial enzyme inhibitor based on nanoparticle-enzyme interactions and molecular imprinting.
Topics: Chymotrypsin; Drug Design; Models, Molecular; Molecular Conformation; Molecular Imprinting; Nanoparticles; Nanotubes, Carbon; Polymers; Protease Inhibitors | 2013 |
Carbon nanotube-enhanced polarization of fluorescent peptides: a novel amplification strategy for homogeneous detection of proteases.
Topics: Chymotrypsin; Fluorescence Polarization; Fluorescent Dyes; Nanotubes, Carbon; Peptides; Thrombin | 2014 |
Facile synthesis of bis(indolyl)methanes catalyzed by α-chymotrypsin.
Topics: Animals; Biocatalysis; Cattle; Chemistry, Organic; Chymotrypsin; Ethanol; Indoles; Methane; Sus scrofa; Temperature | 2014 |
Probing immobilization mechanism of alpha-chymotrypsin onto carbon nanotube in organic media by molecular dynamics simulation.
Topics: Adsorption; Catalysis; Catalytic Domain; Chymotrypsin; Enzymes, Immobilized; Hydrogen Bonding; Models, Molecular; Molecular Dynamics Simulation; Nanotubes, Carbon; Protein Binding; Protein Conformation; Protein Structure, Secondary | 2015 |
Exploring possible mechanisms of action for the nanotoxicity and protein binding of decorated nanotubes: interpretation of physicochemical properties from optimal QSAR models.
Topics: Carbonic Anhydrases; Cell Survival; Chymotrypsin; Hemoglobins; Macrophages; Molecular Structure; Nanotubes, Carbon; Nitric Oxide; Protein Binding; Quantitative Structure-Activity Relationship; Risk Assessment; Serum Albumin, Bovine; Surface Properties | 2015 |
Influence of the Surface Functional Group Density on the Carbon-Nanotube-Induced α-Chymotrypsin Structure and Activity Alterations.
Topics: Biocatalysis; Chymotrypsin; Circular Dichroism; Hydrogen-Ion Concentration; Kinetics; Microscopy, Atomic Force; Nanotubes, Carbon; Osmolar Concentration; Protein Structure, Secondary; Protein Structure, Tertiary; Spectroscopy, Fourier Transform Infrared | 2015 |
Electrostatics-mediated α-chymotrypsin inhibition by functionalized single-walled carbon nanotubes.
Topics: Chymotrypsin; Enzyme Activation; Enzyme Inhibitors; Hydrophobic and Hydrophilic Interactions; Molecular Dynamics Simulation; Nanotubes, Carbon; Static Electricity | 2017 |
Preparation of ionic liquid modified magnetic metal-organic frameworks composites for the solid-phase extraction of α-chymotrypsin.
Topics: Animals; Cattle; Chymotrypsin; Complex Mixtures; Enzyme Assays; Equipment Reuse; Ferrosoferric Oxide; Hemoglobins; Ionic Liquids; Magnetite Nanoparticles; Metal-Organic Frameworks; Nanotubes, Carbon; Osmolar Concentration; Ovalbumin; Pancreas; Sensitivity and Specificity; Serum Albumin, Bovine; Solid Phase Extraction; Swine; Zeolites | 2018 |
Inhibition of α-chymotrypsin by pristine single-wall carbon nanotubes: Clogging up the active site.
Topics: Binding Sites; Chymotrypsin; Fullerenes; Molecular Dynamics Simulation; Nanotubes, Carbon; Particle Size; Serine Proteinase Inhibitors; Surface Properties | 2020 |