tryptophan and methanethiosulfonate

tryptophan has been researched along with methanethiosulfonate 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	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Lamb, RA; Pinto, LH; Tang, Y; Zaitseva, F	1
Torres, VI; Weiss, DS	1

Other Studies

2 other study(ies) available for tryptophan and methanethiosulfonate

Article	Year
The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. The Journal of biological chemistry, 2002, Oct-18, Volume: 277, Issue:42 Topics: Animals; Cell Membrane; Cysteine; DNA, Complementary; Histidine; Hydrogen-Ion Concentration; Ions; Kinetics; Membrane Potentials; Mesylates; Mutation; Oocytes; Protein Binding; Protein Structure, Tertiary; Time Factors; Tryptophan; Viral Matrix Proteins; Xenopus laevis	2002
Identification of a tyrosine in the agonist binding site of the homomeric rho1 gamma-aminobutyric acid (GABA) receptor that, when mutated, produces spontaneous opening. The Journal of biological chemistry, 2002, Nov-15, Volume: 277, Issue:46 Topics: Amino Acid Sequence; Animals; Binding Sites; Binding, Competitive; Crotonates; Dimerization; Dose-Response Relationship, Drug; Electrophysiology; Ethyl Methanesulfonate; GABA Antagonists; Glycine; Humans; Imidazoles; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Organophosphorus Compounds; Picrotoxin; Protein Binding; Receptors, GABA-B; RNA, Complementary; Serine; Transcription, Genetic; Tryptophan; Tyrosine; Xenopus laevis	2002

Article

Year

The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue.

The Journal of biological chemistry, 2002, Oct-18, Volume: 277, Issue:42

Topics: Animals; Cell Membrane; Cysteine; DNA, Complementary; Histidine; Hydrogen-Ion Concentration; Ions; Kinetics; Membrane Potentials; Mesylates; Mutation; Oocytes; Protein Binding; Protein Structure, Tertiary; Time Factors; Tryptophan; Viral Matrix Proteins; Xenopus laevis

2002

Identification of a tyrosine in the agonist binding site of the homomeric rho1 gamma-aminobutyric acid (GABA) receptor that, when mutated, produces spontaneous opening.

The Journal of biological chemistry, 2002, Nov-15, Volume: 277, Issue:46

Topics: Amino Acid Sequence; Animals; Binding Sites; Binding, Competitive; Crotonates; Dimerization; Dose-Response Relationship, Drug; Electrophysiology; Ethyl Methanesulfonate; GABA Antagonists; Glycine; Humans; Imidazoles; Mesylates; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oocytes; Organophosphorus Compounds; Picrotoxin; Protein Binding; Receptors, GABA-B; RNA, Complementary; Serine; Transcription, Genetic; Tryptophan; Tyrosine; Xenopus laevis

2002