phosphoribosyl pyrophosphate and serine

phosphoribosyl pyrophosphate has been researched along with serine 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
Basus, VJ; Munagala, N; Wang, CC	1
Davidson, JN; Haubner, A; Ream, A; Simmons, AJ; Simmons, CQ	1

Other Studies

2 other study(ies) available for phosphoribosyl pyrophosphate and serine

Article	Year
Role of the flexible loop of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus in enzyme catalysis. Biochemistry, 2001, Apr-10, Volume: 40, Issue:14 Topics: Amino Acid Sequence; Animals; Binding Sites; Catalysis; Magnesium; Molecular Sequence Data; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Pentosyltransferases; Phosphoribosyl Pyrophosphate; Protein Structure, Secondary; Serine; Spectrometry, Fluorescence; Substrate Specificity; Thermodynamics; Tritrichomonas foetus; Tryptophan; Tyrosine	2001
Substitutions in hamster CAD carbamoyl-phosphate synthetase alter allosteric response to 5-phosphoribosyl-alpha-pyrophosphate (PRPP) and UTP. The Biochemical journal, 2004, Mar-15, Volume: 378, Issue:Pt 3 Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Animals; Aspartate Carbamoyltransferase; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Cricetinae; Dihydroorotase; Escherichia coli; Lysine; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Phosphoribosyl Pyrophosphate; Sequence Homology, Amino Acid; Serine; Tryptophan; Uridine Triphosphate	2004

Article

Year

Role of the flexible loop of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus in enzyme catalysis.

Biochemistry, 2001, Apr-10, Volume: 40, Issue:14

Topics: Amino Acid Sequence; Animals; Binding Sites; Catalysis; Magnesium; Molecular Sequence Data; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Pentosyltransferases; Phosphoribosyl Pyrophosphate; Protein Structure, Secondary; Serine; Spectrometry, Fluorescence; Substrate Specificity; Thermodynamics; Tritrichomonas foetus; Tryptophan; Tyrosine

2001

Substitutions in hamster CAD carbamoyl-phosphate synthetase alter allosteric response to 5-phosphoribosyl-alpha-pyrophosphate (PRPP) and UTP.

The Biochemical journal, 2004, Mar-15, Volume: 378, Issue:Pt 3

Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Animals; Aspartate Carbamoyltransferase; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Cricetinae; Dihydroorotase; Escherichia coli; Lysine; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Phosphoribosyl Pyrophosphate; Sequence Homology, Amino Acid; Serine; Tryptophan; Uridine Triphosphate

2004