phenylalanine and guanosine monophosphate

phenylalanine has been researched along with guanosine monophosphate 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
Fersht, AR; Frisch, C; Schreiber, G	1
Munagala, NR; Wang, CC	1

Other Studies

2 other study(ies) available for phenylalanine and guanosine monophosphate

Article	Year
The role of Glu73 of barnase in catalysis and the binding of barstar. Journal of molecular biology, 1997, Jul-04, Volume: 270, Issue:1 Topics: Bacterial Proteins; Binding Sites; Enzyme Stability; Glutamic Acid; Guanosine Monophosphate; Models, Molecular; Mutation; Phenylalanine; Protein Conformation; Ribonucleases; RNA; Structure-Activity Relationship; Tryptophan	1997
Altering the purine specificity of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus by structure-based point mutations in the enzyme protein. Biochemistry, 1998, Nov-24, Volume: 37, Issue:47 Topics: Adenine Phosphoribosyltransferase; Amino Acid Substitution; Animals; Arginine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Enzyme Activation; Glutamic Acid; Guanine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Isoleucine; Lysine; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Purines; Ribonucleotides; Serine; Structure-Activity Relationship; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine	1998

Article

Year

The role of Glu73 of barnase in catalysis and the binding of barstar.

Journal of molecular biology, 1997, Jul-04, Volume: 270, Issue:1

Topics: Bacterial Proteins; Binding Sites; Enzyme Stability; Glutamic Acid; Guanosine Monophosphate; Models, Molecular; Mutation; Phenylalanine; Protein Conformation; Ribonucleases; RNA; Structure-Activity Relationship; Tryptophan

1997

Altering the purine specificity of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus by structure-based point mutations in the enzyme protein.

Biochemistry, 1998, Nov-24, Volume: 37, Issue:47

Topics: Adenine Phosphoribosyltransferase; Amino Acid Substitution; Animals; Arginine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Enzyme Activation; Glutamic Acid; Guanine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Isoleucine; Lysine; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Purines; Ribonucleotides; Serine; Structure-Activity Relationship; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine

1998