tryptophan and atractyloside

tryptophan has been researched along with atractyloside in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Brandolin, G; Dianoux, AC; Fiore, C; Lauquin, GJ; Le Saux, A; Roux, P; Schwimmer, C; Trézéguet, V; Vignais, PV	2

Other Studies

2 other study(ies) available for tryptophan and atractyloside

Article	Year
Conformational changes of the yeast mitochondrial adenosine diphosphate/adenosine triphosphate carrier studied through its intrinsic fluorescence. 1. Tryptophanyl residues of the carrier can be mutated without impairing protein activity. Biochemistry, 1996, Dec-17, Volume: 35, Issue:50 Topics: Atractyloside; Base Sequence; Binding Sites; DNA Primers; Escherichia coli; Kinetics; Mitochondria; Mitochondrial ADP, ATP Translocases; Models, Structural; Mutagenesis, Site-Directed; Plasmids; Point Mutation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan	1996
Conformational changes of the yeast mitochondrial adenosine diphosphate/adenosine triphosphate carrier studied through its intrinsic fluorescence. 2. Assignment of tryptophanyl residues of the carrier to the responses to specific ligands. Biochemistry, 1996, Dec-17, Volume: 35, Issue:50 Topics: Adenosine Diphosphate; Atractyloside; Binding Sites; Bongkrekic Acid; Kinetics; Mitochondria; Mitochondrial ADP, ATP Translocases; Models, Structural; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Tryptophan	1996

Article

Year

Conformational changes of the yeast mitochondrial adenosine diphosphate/adenosine triphosphate carrier studied through its intrinsic fluorescence. 1. Tryptophanyl residues of the carrier can be mutated without impairing protein activity.

Biochemistry, 1996, Dec-17, Volume: 35, Issue:50

Topics: Atractyloside; Base Sequence; Binding Sites; DNA Primers; Escherichia coli; Kinetics; Mitochondria; Mitochondrial ADP, ATP Translocases; Models, Structural; Mutagenesis, Site-Directed; Plasmids; Point Mutation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan

1996

Conformational changes of the yeast mitochondrial adenosine diphosphate/adenosine triphosphate carrier studied through its intrinsic fluorescence. 2. Assignment of tryptophanyl residues of the carrier to the responses to specific ligands.

Biochemistry, 1996, Dec-17, Volume: 35, Issue:50

Topics: Adenosine Diphosphate; Atractyloside; Binding Sites; Bongkrekic Acid; Kinetics; Mitochondria; Mitochondrial ADP, ATP Translocases; Models, Structural; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Tryptophan

1996