4-hydroxyphenylpyruvic acid and glutamine

4-hydroxyphenylpyruvic acid has been researched along with glutamine in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Thompson, JR; Wu, GY	1
Chang, CW; Chang, NY; Chang, TC; Lee, HJ; Lin, JF; Sheih, YL; Shen, CP	1

Other Studies

2 other study(ies) available for 4-hydroxyphenylpyruvic acid and glutamine

Article	Year
The effect of glutamine on protein turnover in chick skeletal muscle in vitro. The Biochemical journal, 1990, Jan-15, Volume: 265, Issue:2 Topics: Amino Acids; Animals; Chickens; Glutamine; Kinetics; Muscles; Phenylalanine; Phenylpyruvic Acids; Protein Biosynthesis; Proteins	1990
The interactions in the carboxyl terminus of human 4-hydroxyphenylpyruvate dioxygenase are critical to mediate the conformation of the final helix and the tail to shield the active site for catalysis. PloS one, 2013, Volume: 8, Issue:8 Topics: 4-Hydroxyphenylpyruvate Dioxygenase; Amino Acid Sequence; Amino Acid Substitution; Biocatalysis; Catalytic Domain; Escherichia coli; Glutamine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Phenylpyruvic Acids; Protein Structure, Secondary; Recombinant Proteins; Sequence Alignment; Substrate Specificity	2013

Article

Year

The effect of glutamine on protein turnover in chick skeletal muscle in vitro.

The Biochemical journal, 1990, Jan-15, Volume: 265, Issue:2

Topics: Amino Acids; Animals; Chickens; Glutamine; Kinetics; Muscles; Phenylalanine; Phenylpyruvic Acids; Protein Biosynthesis; Proteins

1990

The interactions in the carboxyl terminus of human 4-hydroxyphenylpyruvate dioxygenase are critical to mediate the conformation of the final helix and the tail to shield the active site for catalysis.

PloS one, 2013, Volume: 8, Issue:8

Topics: 4-Hydroxyphenylpyruvate Dioxygenase; Amino Acid Sequence; Amino Acid Substitution; Biocatalysis; Catalytic Domain; Escherichia coli; Glutamine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Phenylpyruvic Acids; Protein Structure, Secondary; Recombinant Proteins; Sequence Alignment; Substrate Specificity

2013