tryptophan and cytidine monophosphate

tryptophan has been researched along with cytidine monophosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	0 (0.00)	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
Doi, M; Inoue, M; Ishida, T; Segawa, K; Ueda, H	1
Gea-Mallorqui, E; Goring, ME; Hanic-Joyce, PJ; Joyce, PB; Karls, S; Leibovitch, M; Richard, F	1

Other Studies

2 other study(ies) available for tryptophan and cytidine monophosphate

Article	Year
Stacking interactions between protonated nucleic acid bases and aromatic amino acids: spectroscopic and structural analyses of m3CMP-tryptophan derivative complex. Nucleic acids symposium series, 1989, Issue:21 Topics: Cytidine Monophosphate; Cytosine Nucleotides; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; Tryptophan; X-Ray Diffraction	1989
The ability of an arginine to tryptophan substitution in Saccharomyces cerevisiae tRNA nucleotidyltransferase to alleviate a temperature-sensitive phenotype suggests a role for motif C in active site organization. Biochimica et biophysica acta, 2013, Volume: 1834, Issue:10 Topics: Adenosine Monophosphate; Amino Acid Motifs; Amino Acid Substitution; Arginine; Aspartic Acid; Catalytic Domain; Cytidine Monophosphate; Hot Temperature; Molecular Dynamics Simulation; Molecular Sequence Data; Phenotype; Protein Structure, Secondary; RNA Nucleotidyltransferases; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Tryptophan	2013

Article

Year

Stacking interactions between protonated nucleic acid bases and aromatic amino acids: spectroscopic and structural analyses of m3CMP-tryptophan derivative complex.

Nucleic acids symposium series, 1989, Issue:21

Topics: Cytidine Monophosphate; Cytosine Nucleotides; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; Tryptophan; X-Ray Diffraction

1989

The ability of an arginine to tryptophan substitution in Saccharomyces cerevisiae tRNA nucleotidyltransferase to alleviate a temperature-sensitive phenotype suggests a role for motif C in active site organization.

Biochimica et biophysica acta, 2013, Volume: 1834, Issue:10

Topics: Adenosine Monophosphate; Amino Acid Motifs; Amino Acid Substitution; Arginine; Aspartic Acid; Catalytic Domain; Cytidine Monophosphate; Hot Temperature; Molecular Dynamics Simulation; Molecular Sequence Data; Phenotype; Protein Structure, Secondary; RNA Nucleotidyltransferases; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Tryptophan

2013