tryptophan has been researched along with cellulase in 25 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 3 (12.00) | 18.7374 |
1990's | 9 (36.00) | 18.2507 |
2000's | 6 (24.00) | 29.6817 |
2010's | 4 (16.00) | 24.3611 |
2020's | 3 (12.00) | 2.80 |
Authors | Studies |
---|---|
Hurst, PL; Shepherd, MG; Sullivan, PA | 1 |
Porath, J; Vijayalakshmi, MA | 1 |
Bennich, H; Engström, A; Lindeberg, G | 1 |
Clarke, AJ | 1 |
Claeyssens, M; Henrissat, B; Macarrón, R | 1 |
Arata, Y; Hayashi, Y; Ito, S; Kawaminami, S; Ozaki, K; Shimada, I; Sumitomo, N | 1 |
Burtnick, LD; Din, N; Forsythe, IJ; Gilkes, NR; Kilburn, DG; Miller, RC; Warren, RA | 1 |
Arunachalam, U; Kellis, JT | 1 |
Gao, P; Sun, YQ; Yan, BX | 1 |
Drakenberg, T; Harjunpää, V; Jones, TA; Kinnari, T; Koivula, A; Rouvinen, J; Ruohonen, L; Teeri, TT; Teleman, A | 1 |
Linder, M; Nevanen, T; Teeri, TT | 1 |
Arata, Y; Ito, S; Kawaminami, S; Shimada, I; Takahashi, H | 1 |
Barras, F; Brun, E; Chapon, V; Morelli, X; Simpson, HD | 1 |
Boraston, AB; Chiu, P; Freelove, AC; Kilburn, DG; Notenboom, V; Rose, DR | 1 |
Bailey, M; Collén, A; Fagerström, R; Hyytiä, T; Kula, MR; Nakari-Setlä, T; Penttilä, M; Persson, J; Selber, K; Stålbrand, H; Tjerneld, F | 1 |
Larsen, S; Lo Leggio, L | 1 |
Bakalova, NG; Kolev, DN; Petrova, SD | 1 |
Catalá, C; Irwin, D; Ripoll, DR; Rose, JK; Urbanowicz, BR; Wilson, DB | 1 |
Barnes, CA; Bose, S; Petrich, JW | 1 |
Barger, GR; Bosnyák, E; Chugani, DC; Jeong, JW; Juhász, C; Kamson, DO; Kupsky, WJ; Mittal, S; Robinette, NL | 1 |
Han, SO; Hyeon, JE; Kim, SH; Kim, SJ; Shin, SK | 1 |
Borne, R; Fierobe, HP; Franche, N; Pagès, S; Ravachol, J; Tardif, C; Vita, N | 1 |
Badino, SF; Borch, K; Cavaleiro, AM; Kari, J; Morth, JP; Røjel, N; Schaller, K; Sørensen, TH; Westh, P | 1 |
Hao, N; Jie, C; Li, J; Liu, Z; Wu, B | 1 |
Huang, KF; Ko, TP; Wu, SH; Ye, TJ | 1 |
25 other study(ies) available for tryptophan and cellulase
Article | Year |
---|---|
Chemical modification of cellulase from Aspergillus niger.
Topics: Aspergillus niger; Azo Compounds; Benzyl Compounds; Bromosuccinimide; Carbodiimides; Cellulase; Diethyl Pyrocarbonate; Hydrogen-Ion Concentration; Ions; Kinetics; Structure-Activity Relationship; Tryptophan | 1977 |
Charge-transfer and water-mediated adsorption. III. Adsorption on tryptophan-substituted Sephadex and Sepharose.
Topics: Amino Acids; Cellulase; Chromatography, Affinity; Chromatography, Gel; Sepharose; Tryptophan; Tyrosine | 1979 |
Purification of synthetic peptides. Immobilized metal ion affinity chromatography (IMAC).
Topics: Amino Acid Sequence; Amino Acids; Antigens, Differentiation, B-Lymphocyte; Antimicrobial Cationic Peptides; Cellulase; Chelating Agents; Chromatography, Affinity; Cysteine; Histidine; Insect Hormones; Ion Exchange Resins; Metals; Molecular Sequence Data; Peptides; Receptors, Fc; Receptors, IgE; Ribonucleotide Reductases; Tryptophan | 1991 |
Essential tryptophan residues in the function of cellulase from Schizophyllum commune.
Topics: Basidiomycota; Binding Sites; Bromosuccinimide; Cellulase; Cellulose; Chemical Phenomena; Chemistry; Fluorescence; Oligosaccharides; Oxidation-Reduction; Schizophyllum; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Tryptophan | 1987 |
Family A cellulases: two essential tryptophan residues in endoglucanase III from Trichoderma reesei.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Bromosuccinimide; Catalysis; Cellulase; Cellulose; Hydrolysis; Kinetics; Molecular Sequence Data; Oxidation-Reduction; Structure-Activity Relationship; Trichoderma; Tryptophan | 1995 |
A stable isotope-aided NMR study of the active site of an endoglucanase from a strain of Bacillus.
Topics: Amino Acid Sequence; Bacillus subtilis; Binding Sites; Carbon Isotopes; Cellulase; Kinetics; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Alignment; Trisaccharides; Tryptophan | 1994 |
The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: evidence for the involvement of tryptophan residues in binding.
Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Binding Sites; Cellulase; Cellulose; Gram-Positive Rods; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Alignment; Sequence Homology, Amino Acid; Tryptophan | 1994 |
Folding and stability of endoglucanase III, a single-domain cellulase from Trichoderma reesei.
Topics: Bacterial Proteins; Cellulase; Circular Dichroism; Disulfides; Dithiothreitol; Enzyme Stability; Hydrogen-Ion Concentration; Kinetics; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence; Temperature; Thermodynamics; Trichoderma; Tryptophan; Urea | 1996 |
Intrinsic fluorescence in endoglucanase and cellobiohydrolase from Trichoderma pseudokiningii S-38: effects of pH, quenching agents, and ligand binding.
Topics: Acrylamide; Acrylamides; Cellulase; Cellulose 1,4-beta-Cellobiosidase; Fluorescence; Hydrogen-Ion Concentration; Kinetics; Ligands; Potassium Iodide; Spectrometry, Fluorescence; Substrate Specificity; Trichoderma; Tryptophan | 1997 |
Tryptophan 272: an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A.
Topics: Binding Sites; Cellulase; Cellulose; Cellulose 1,4-beta-Cellobiosidase; Hydrolysis; Models, Molecular; Mutagenesis, Site-Directed; Oligosaccharides; Trichoderma; Tryptophan | 1998 |
Design of a pH-dependent cellulose-binding domain.
Topics: Amino Acid Sequence; Binding Sites; Cellulase; Cellulose; Cellulose 1,4-beta-Cellobiosidase; Histidine; Hydrogen-Ion Concentration; Models, Molecular; Molecular Sequence Data; Protein Engineering; Titrimetry; Tryptophan | 1999 |
A multinuclear NMR study of the active site of an endoglucanase from a strain of Bacillus. Use of Trp residues as structural probes.
Topics: Amino Acid Sequence; Aspartic Acid; Bacillus; Binding Sites; Cellulase; Clostridium; Deuterium; Glutamic Acid; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Protein Structure, Tertiary; Sequence Alignment; Tryptophan | 1999 |
Alteration of a single tryptophan residue of the cellulose-binding domain blocks secretion of the Erwinia chrysanthemi Cel5 cellulase (ex-EGZ) via the type II system.
Topics: Amino Acid Substitution; Binding Sites; Cellulase; Cellulose; Dickeya chrysanthemi; Models, Molecular; Mutation; Periplasm; Protein Binding; Protein Sorting Signals; Protein Structure, Tertiary; Sequence Deletion; Tryptophan | 2000 |
Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study.
Topics: Alanine; Binding Sites; Calorimetry; Cellulase; Cellulose; Clostridium; Crystallography, X-Ray; Hydrogen Bonding; Ligands; Models, Molecular; Mutation; Oligosaccharides; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Static Electricity; Substrate Specificity; Tetroses; Thermodynamics; Titrimetry; Trioses; Tryptophan | 2001 |
Primary recovery of a genetically engineered Trichoderma reesei endoglucanase I (Cel 7B) fusion protein in cloud point extraction systems.
Topics: Bioreactors; Blotting, Western; Cellulase; Cellulose 1,4-beta-Cellobiosidase; Chemistry Techniques, Analytical; Detergents; Fermentation; Hydrophobic and Hydrophilic Interactions; Pilot Projects; Polyethylenes; Polypropylenes; Protein Engineering; Recombinant Fusion Proteins; Sensitivity and Specificity; Surface-Active Agents; Temperature; Trichoderma; Tryptophan | 2002 |
The 1.62 A structure of Thermoascus aurantiacus endoglucanase: completing the structural picture of subfamilies in glycoside hydrolase family 5.
Topics: Ascomycota; Binding Sites; Cellulase; Crystallization; Crystallography, X-Ray; Glycoside Hydrolases; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; Substrate Specificity; Tryptophan | 2002 |
Catalytically important amino acid residues in endoglucanases from a mutant strain Trichoderma sp. M7.
Topics: Bacterial Proteins; Bromosuccinimide; Catalysis; Cellulase; Trichoderma; Tryptophan | 2006 |
A tomato endo-beta-1,4-glucanase, SlCel9C1, represents a distinct subclass with a new family of carbohydrate binding modules (CBM49).
Topics: Amino Acid Sequence; Carbohydrates; Catalytic Domain; Cell Wall; Cellulase; Cellulose; Glutathione Transferase; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Solanum lycopersicum; Tryptophan | 2007 |
Enhanced stability and activity of cellulase in an ionic liquid and the effect of pretreatment on cellulose hydrolysis.
Topics: Aspergillus niger; Biofuels; Cellulase; Cellulose; Enzyme Stability; Hydrogen-Ion Concentration; Hydrolysis; Imidazoles; Ionic Liquids; Quaternary Ammonium Compounds; Solubility; Spectrometry, Fluorescence; Sulfuric Acid Esters; Temperature; Tryptophan; Viscosity | 2012 |
Multi-modal imaging of tumor cellularity and Tryptophan metabolism in human Gliomas.
Topics: Adolescent; Adult; Aged; Brain Neoplasms; Cellulase; Diffusion Tensor Imaging; Female; Glioma; Humans; Immunohistochemistry; Male; Positron-Emission Tomography; ROC Curve; Tryptophan | 2015 |
Mutation of a conserved tryptophan residue in the CBM3c of a GH9 endoglucanase inhibits activity.
Topics: Amino Acid Substitution; Bacterial Proteins; Cellulase; Clostridium cellulovorans; Enzyme Stability; Mutation, Missense; Protein Structure, Secondary; Tryptophan | 2016 |
Restoration of cellulase activity in the inactive cellulosomal protein Cel9V from Ruminiclostridium cellulolyticum.
Topics: Bacterial Proteins; Catalytic Domain; Cellulase; Clostridium cellulolyticum; Enzyme Activation; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid; Tryptophan | 2018 |
Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues.
Topics: Catalytic Domain; Cellulase; Cellulose; Enzyme Activation; Fungal Proteins; Kinetics; Models, Molecular; Protein Binding; Substrate Specificity; Thermodynamics; Trichoderma; Tryptophan | 2020 |
A multifunctional α-amylase BSGH13 from Bacillus subtilis BS-5 possessing endoglucanase and xylanase activities.
Topics: alpha-Amylases; Amino Acid Substitution; Bacillus subtilis; Bacterial Proteins; Catalytic Domain; Cellulase; Cellulose; Cloning, Molecular; Endo-1,4-beta Xylanases; Escherichia coli; Gene Expression; Genetic Vectors; Kinetics; Maltose; Models, Molecular; Mutation; Phenylalanine; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Recombinant Proteins; Structural Homology, Protein; Structure-Activity Relationship; Substrate Specificity; Tetroses; Tryptophan; Xylans | 2021 |
Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.
Topics: Catalytic Domain; Cellulase; Glycoside Hydrolases; Polysaccharides; Substrate Specificity; Tryptophan | 2022 |