norvaline and cycloserine

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

Authors

Authors	Studies
Brandsch, M; Gebauer, S; Laug, L; Schäfer, S; Thondorf, I; Voigt, V; Zebisch, K	1
Anufrieva, NV; Demidkina, TV; Faleev, NG; Fedorova, OS; Kuznetsov, NA; Kuznetsova, AA; Morozova, EA; Nikulin, AD; Revtovich, SV	1

Other Studies

2 other study(ies) available for norvaline and cycloserine

Article	Year
Three-dimensional quantitative structure-activity relationship analyses of substrates of the human proton-coupled amino acid transporter 1 (hPAT1). Bioorganic & medicinal chemistry, 2011, Nov-01, Volume: 19, Issue:21 Topics: Amino Acid Transport Systems; Caco-2 Cells; Endocytosis; Humans; Kinetics; Models, Chemical; Models, Molecular; Molecular Conformation; Quantitative Structure-Activity Relationship; Substrate Specificity; Symporters	2011
Pre-steady-state kinetic and structural analysis of interaction of methionine γ-lyase from Citrobacter freundii with inhibitors. The Journal of biological chemistry, 2015, Jan-02, Volume: 290, Issue:1 Topics: Alanine; Bacterial Proteins; Carbon-Sulfur Lyases; Catalytic Domain; Citrobacter freundii; Crystallography, X-Ray; Cycloserine; Cysteine; Enzyme Inhibitors; Escherichia coli; Gene Expression; Glycine; Imines; Kinetics; Models, Chemical; Pyridoxal Phosphate; Recombinant Proteins; Thermodynamics; Valine	2015

Article

Year

Three-dimensional quantitative structure-activity relationship analyses of substrates of the human proton-coupled amino acid transporter 1 (hPAT1).

Bioorganic & medicinal chemistry, 2011, Nov-01, Volume: 19, Issue:21

Topics: Amino Acid Transport Systems; Caco-2 Cells; Endocytosis; Humans; Kinetics; Models, Chemical; Models, Molecular; Molecular Conformation; Quantitative Structure-Activity Relationship; Substrate Specificity; Symporters

2011

Pre-steady-state kinetic and structural analysis of interaction of methionine γ-lyase from Citrobacter freundii with inhibitors.

The Journal of biological chemistry, 2015, Jan-02, Volume: 290, Issue:1

Topics: Alanine; Bacterial Proteins; Carbon-Sulfur Lyases; Catalytic Domain; Citrobacter freundii; Crystallography, X-Ray; Cycloserine; Cysteine; Enzyme Inhibitors; Escherichia coli; Gene Expression; Glycine; Imines; Kinetics; Models, Chemical; Pyridoxal Phosphate; Recombinant Proteins; Thermodynamics; Valine

2015