tryptophan and t0901317

tryptophan has been researched along with t0901317 in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Bledsoe, RK; Boggs, S; Collins, JL; Lambert, MH; McKee, DD; Miller, AB; Moore, J; Moore, L; Nichols, J; Parks, D; Watson, M; Williams, S; Willson, TM; Wisely, B	1
Banerjee, M; Chai, SC; Chen, T; Robbins, D; Wu, J	1

Other Studies

2 other study(ies) available for tryptophan and t0901317

Article	Year
X-ray crystal structure of the liver X receptor beta ligand binding domain: regulation by a histidine-tryptophan switch. The Journal of biological chemistry, 2003, Jul-18, Volume: 278, Issue:29 Topics: Anticholesteremic Agents; Binding Sites; Cholesterol; Crystallography, X-Ray; DNA-Binding Proteins; Histidine; Humans; Hydrocarbons, Fluorinated; Hydrogen Bonding; In Vitro Techniques; Ligands; Liver; Liver X Receptors; Models, Molecular; Mutagenesis, Site-Directed; Orphan Nuclear Receptors; Protein Conformation; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear; Recombinant Proteins; Sulfonamides; Tryptophan	2003
Tryptophan 299 is a conserved residue of human pregnane X receptor critical for the functional consequence of ligand binding. Biochemical pharmacology, 2016, Mar-15, Volume: 104 Topics: Alanine; Amino Acid Substitution; Binding Sites; Computational Biology; Crystallography, X-Ray; Cytochrome P-450 CYP3A; Diphosphonates; Epithelial Cells; Hep G2 Cells; Humans; Hydrocarbons, Fluorinated; Ligands; Luciferases; Mutation; Pregnane X Receptor; Protein Binding; Protein Conformation; Receptors, Steroid; Sulfonamides; Transfection; Tryptophan; Two-Hybrid System Techniques	2016

Article

Year

X-ray crystal structure of the liver X receptor beta ligand binding domain: regulation by a histidine-tryptophan switch.

The Journal of biological chemistry, 2003, Jul-18, Volume: 278, Issue:29

Topics: Anticholesteremic Agents; Binding Sites; Cholesterol; Crystallography, X-Ray; DNA-Binding Proteins; Histidine; Humans; Hydrocarbons, Fluorinated; Hydrogen Bonding; In Vitro Techniques; Ligands; Liver; Liver X Receptors; Models, Molecular; Mutagenesis, Site-Directed; Orphan Nuclear Receptors; Protein Conformation; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear; Recombinant Proteins; Sulfonamides; Tryptophan

2003

Tryptophan 299 is a conserved residue of human pregnane X receptor critical for the functional consequence of ligand binding.

Biochemical pharmacology, 2016, Mar-15, Volume: 104

Topics: Alanine; Amino Acid Substitution; Binding Sites; Computational Biology; Crystallography, X-Ray; Cytochrome P-450 CYP3A; Diphosphonates; Epithelial Cells; Hep G2 Cells; Humans; Hydrocarbons, Fluorinated; Ligands; Luciferases; Mutation; Pregnane X Receptor; Protein Binding; Protein Conformation; Receptors, Steroid; Sulfonamides; Transfection; Tryptophan; Two-Hybrid System Techniques

2016