Page last updated: 2024-08-17

uridine diphosphate and asparagine

uridine diphosphate has been researched along with asparagine 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
Larivière, L; Moréra, S	1
Assairi, L; Barzu, O; Briozzo, P; Evrin, C; Gilles, AM; Joly, N; Meyer, P	1

Other Studies

2 other study(ies) available for uridine diphosphate and asparagine

Article	Year
Structural evidence of a passive base-flipping mechanism for beta-glucosyltransferase. The Journal of biological chemistry, 2004, Aug-13, Volume: 279, Issue:33 Topics: 5-Methylcytosine; Adenine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Crystallography, X-Ray; Cytosine; DNA; Glucosyltransferases; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Oligonucleotides; Plasmids; Protein Binding; Protein Conformation; Uridine Diphosphate	2004
Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation. The Journal of biological chemistry, 2005, Jul-08, Volume: 280, Issue:27 Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Asparagine; Binding Sites; Crystallography; Enzyme Activation; Escherichia coli; Guanosine Triphosphate; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleoside-Phosphate Kinase; Phosphates; Protein Folding; Protein Structure, Quaternary; Threonine; Uridine Diphosphate; Uridine Monophosphate; Uridine Triphosphate	2005

Article

Year

Structural evidence of a passive base-flipping mechanism for beta-glucosyltransferase.

The Journal of biological chemistry, 2004, Aug-13, Volume: 279, Issue:33

Topics: 5-Methylcytosine; Adenine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Crystallography, X-Ray; Cytosine; DNA; Glucosyltransferases; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Oligonucleotides; Plasmids; Protein Binding; Protein Conformation; Uridine Diphosphate

2004

Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation.

The Journal of biological chemistry, 2005, Jul-08, Volume: 280, Issue:27

Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Asparagine; Binding Sites; Crystallography; Enzyme Activation; Escherichia coli; Guanosine Triphosphate; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleoside-Phosphate Kinase; Phosphates; Protein Folding; Protein Structure, Quaternary; Threonine; Uridine Diphosphate; Uridine Monophosphate; Uridine Triphosphate

2005