tryptophan has been researched along with 1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone in 16 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (6.25) | 18.2507 |
| 2000's | 14 (87.50) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 1 (6.25) | 2.80 |
| Authors | Studies |
|---|---|
| Sasaki, N; Shimada, T; Sutoh, K | 1 |
| Bagshaw, CR; Málnási-Csizmadia, A; Woolley, RJ | 1 |
| Bagshaw, CR; Botchway, SW; Kovacs, M; Malnasi-Csizmadia, A; Woolley, RJ | 1 |
| Bagshaw, CR; Geeves, MA; Kovács, M; Málnási-Csizmadia, A; Pearson, DS; Woolley, RJ | 1 |
| Bagshaw, CR; Kovacs, M; Malnasi-Csizmadia, A; Woolley, RJ | 1 |
| Ito, K; Sutoh, K; Suzuki, Y; Uyeda, TQ; Yamamoto, K | 1 |
| Bagshaw, CR; Conibear, PB; Floyd, DN; Kovács, M; Málnási-Csizmadia, A; Wakelin, S; Woolley, RJ | 1 |
| Bódis, E; Gonnelli, M; Málnási-Csizmadia, A; Somogyi, B; Strambini, GB | 1 |
| Bagshaw, CR; Conibear, PB; Málnási-Csizmadia, A | 1 |
| Bagshaw, CR; Conibear, PB; Cowie, RA; Dickens, JL; Málnási-Csizmadia, A; Wakelin, S; Zeng, W | 1 |
| Berger, CL; Chrin, LR; Gaffney, DP; Robertson, CI | 1 |
| Bagshaw, CR; Geeves, MA; Gyimesi, M; Kintses, B; Málnási-Csizmadia, A; Pearson, DS; Zeng, W | 1 |
| Bagshaw, CR; Geeves, MA; Hetényi, C; Kovács, M; Málnási-Csizmadia, A; Nyitray, L; Pearson, DS; Tóth, J | 1 |
| Jahn, W | 1 |
| Kintses, B; Málnási-Csizmadia, A; Yang, Z | 1 |
| Fischer, M; Görlich, D; Huyton, T; Jaiswal, M; Taxer, W | 1 |
2 review(s) available for tryptophan and 1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone
| Article | Year |
|---|---|
Engineering Dictyostelium discoideum myosin II for the introduction of site-specific fluorescence probes.
Topics: Adenosine Diphosphate; Animals; Dictyostelium; Fluorescent Dyes; Genes, Reporter; Green Fluorescent Proteins; Kinetics; Luminescent Proteins; Myosin Type II; Protein Engineering; Protozoan Proteins; Tryptophan | 2002 |
Dynamics of actomyosin interactions in relation to the cross-bridge cycle.
Topics: Actins; Animals; Binding Sites; Biomechanical Phenomena; Dictyostelium; Kinetics; Models, Molecular; Molecular Motor Proteins; Muscle Contraction; Muscles; Mutation; Myosins; Protein Conformation; Tryptophan | 2004 |
14 other study(ies) available for tryptophan and 1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone
| Article | Year |
|---|---|
Mutational analysis of the switch II loop of Dictyostelium myosin II.
Topics: Actins; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Cell Division; Dictyostelium; Fluorescence; Models, Molecular; Mutagenesis; Myosins; Protein Structure, Tertiary; Recombinant Proteins; Transformation, Genetic; Tryptophan | 1998 |
Resolution of conformational states of Dictyostelium myosin II motor domain using tryptophan (W501) mutants: implications for the open-closed transition identified by crystallography.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Aluminum Compounds; Animals; Binding Sites; Crystallography, X-Ray; Dictyostelium; Fluorides; Hydrolysis; Kinetics; Molecular Motor Proteins; Mutagenesis, Site-Directed; Myosins; Protein Conformation; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan | 2000 |
The dynamics of the relay loop tryptophan residue in the Dictyostelium myosin motor domain and the origin of spectroscopic signals.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Anisotropy; Cloning, Molecular; Dictyostelium; Kinetics; Models, Chemical; Myosins; Phenylalanine; Protein Structure, Tertiary; Spectrometry, Fluorescence; Spectrophotometry; Time Factors; Tryptophan | 2001 |
Kinetic resolution of a conformational transition and the ATP hydrolysis step using relaxation methods with a Dictyostelium myosin II mutant containing a single tryptophan residue.
Topics: Adenosine Triphosphate; Animals; Cold Temperature; Dictyostelium; Hot Temperature; Hydrolysis; Kinetics; Molecular Motor Proteins; Mutagenesis, Site-Directed; Myosin Type II; Pressure; Protein Conformation; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan | 2001 |
Analysis of nucleotide binding to Dictyostelium myosin II motor domains containing a single tryptophan near the active site.
Topics: Adenine; Adenosine Triphosphatases; Animals; Anisotropy; Binding Sites; Dictyostelium; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Kinetics; Models, Chemical; Models, Molecular; Myosin Type II; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectrometry, Fluorescence; Time Factors; Tryptophan | 2002 |
Requirement of domain-domain interaction for conformational change and functional ATP hydrolysis in myosin.
Topics: Actins; Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Cell Division; Cell Movement; Dictyostelium; Fluorescence; Fluorescence Resonance Energy Transfer; Hydrolysis; Mutagenesis, Site-Directed; Myosins; Phenotype; Protein Structure, Tertiary; Tryptophan | 2003 |
Characterization of f-actin tryptophan phosphorescence in the presence and absence of tryptophan-free myosin motor domain.
Topics: Actins; Amino Acid Substitution; Animals; Binding Sites; Dictyostelium; Luminescent Measurements; Macromolecular Substances; Molecular Motor Proteins; Mutagenesis, Site-Directed; Myosin Subfragments; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rabbits; Recombinant Proteins; Structure-Activity Relationship; Tropomyosin; Tryptophan | 2004 |
The effect of F-actin on the relay helix position of myosin II, as revealed by tryptophan fluorescence, and its implications for mechanochemical coupling.
Topics: Actins; Actomyosin; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Dictyostelium; Molecular Motor Proteins; Myosin Type II; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Protozoan Proteins; Rabbits; Signal Transduction; Spectrometry, Fluorescence; Tryptophan | 2004 |
Structural rearrangements in the active site of smooth-muscle myosin.
Topics: Acrylamide; Actins; Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Binding Sites; Cell Line; Chickens; Crystallography, X-Ray; Dictyostelium; DNA, Complementary; Dose-Response Relationship, Drug; Fluorescence Resonance Energy Transfer; Hydrolysis; Insecta; Kinetics; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Myosin Type II; Myosins; Nucleotides; Protein Conformation; Protein Structure, Tertiary; Temperature; Time Factors; Tryptophan | 2005 |
Reversible movement of switch 1 loop of myosin determines actin interaction.
Topics: Actins; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Cryoelectron Microscopy; Crystallography, X-Ray; Dictyostelium; Magnesium; Models, Chemical; Models, Molecular; Myosins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Tryptophan | 2007 |
Selective perturbation of the myosin recovery stroke by point mutations at the base of the lever arm affects ATP hydrolysis and phosphate release.
Topics: Adenosine Triphosphate; Animals; Dictyostelium; Models, Molecular; Myosins; Phosphates; Point Mutation; Protein Structure, Tertiary; Tryptophan | 2007 |
The association of actin and myosin in the presence of gamma-amido-ATP proceeds mainly via a complex with myosin in the closed conformation.
Topics: Actins; Adenosine Diphosphate; Adenylyl Imidodiphosphate; Animals; Dictyostelium; Fluorescence; Myosins; ortho-Aminobenzoates; Protein Conformation; Spectrometry, Fluorescence; Tryptophan | 2007 |
Experimental investigation of the seesaw mechanism of the relay region that moves the myosin lever arm.
Topics: Actins; Adenosine Triphosphate; Animals; Binding Sites; Dictyostelium; Hydrolysis; Kinetics; Mutation; Myosin Type II; Nucleotides; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Thermodynamics; Tryptophan | 2008 |
Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins.
Topics: Amino Acid Sequence; Asparagine; Dictyostelium; Histidine; Isoleucine; Leucine; Leucine-Rich Repeat Proteins; Phenylalanine; Tryptophan; Tyrosine | 2022 |