Page last updated: 2024-08-17

aspartic acid and mocimycin

aspartic acid has been researched along with mocimycin 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
Clark, BF; Knudsen, CR	1
Krab, IM; Parmeggiani, A	1

Other Studies

2 other study(ies) available for aspartic acid and mocimycin

Article	Year
Site-directed mutagenesis of Arg58 and Asp86 of elongation factor Tu from Escherichia coli: effects on the GTPase reaction and aminoacyl-tRNA binding. Protein engineering, 1995, Volume: 8, Issue:12 Topics: Anti-Bacterial Agents; Arginine; Aspartic Acid; Base Sequence; DNA Primers; Escherichia coli; GTP Phosphohydrolase-Linked Elongation Factors; Guanosine Diphosphate; Guanosine Triphosphate; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Peptide Elongation Factor Tu; Protein Binding; Pyridones; Recombinant Proteins; Ribosomes; RNA, Transfer; RNA, Transfer, Phe	1995
Mutagenesis of three residues, isoleucine-60, threonine-61, and aspartic acid-80, implicated in the GTPase activity of Escherichia coli elongation factor Tu. Biochemistry, 1999, Oct-05, Volume: 38, Issue:40 Topics: Aspartic Acid; Binding Sites; Escherichia coli; Esters; GTP Phosphohydrolases; Guanosine Diphosphate; Guanosine Triphosphate; Isoleucine; Magnesium; Models, Molecular; Mutagenesis, Site-Directed; Peptide Elongation Factor Tu; Peptides; Pyridones; Recombinant Proteins; Ribosomes; RNA, Transfer, Phe; Threonine	1999

Article

Year

Site-directed mutagenesis of Arg58 and Asp86 of elongation factor Tu from Escherichia coli: effects on the GTPase reaction and aminoacyl-tRNA binding.

Protein engineering, 1995, Volume: 8, Issue:12

Topics: Anti-Bacterial Agents; Arginine; Aspartic Acid; Base Sequence; DNA Primers; Escherichia coli; GTP Phosphohydrolase-Linked Elongation Factors; Guanosine Diphosphate; Guanosine Triphosphate; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Peptide Elongation Factor Tu; Protein Binding; Pyridones; Recombinant Proteins; Ribosomes; RNA, Transfer; RNA, Transfer, Phe

1995

Mutagenesis of three residues, isoleucine-60, threonine-61, and aspartic acid-80, implicated in the GTPase activity of Escherichia coli elongation factor Tu.

Biochemistry, 1999, Oct-05, Volume: 38, Issue:40

Topics: Aspartic Acid; Binding Sites; Escherichia coli; Esters; GTP Phosphohydrolases; Guanosine Diphosphate; Guanosine Triphosphate; Isoleucine; Magnesium; Models, Molecular; Mutagenesis, Site-Directed; Peptide Elongation Factor Tu; Peptides; Pyridones; Recombinant Proteins; Ribosomes; RNA, Transfer, Phe; Threonine

1999