valine and mocimycin

valine 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	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hughes, D; Tubulekas, I	1
Arcari, P; Cantiello, P; De Paola, B; Fiengo, A; Masullo, M; Vitagliano, L; Zagari, A	1

Other Studies

2 other study(ies) available for valine and mocimycin

Article	Year
A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome. Journal of bacteriology, 1993, Volume: 175, Issue:1 Topics: Anti-Bacterial Agents; Glycine; Guanosine Triphosphate; Hydrolysis; Kinetics; Macromolecular Substances; Models, Molecular; Peptide Elongation Factor Tu; Phenotype; Protein Biosynthesis; Protein Conformation; Pyridones; Ribosomes; RNA, Transfer, Amino Acyl; RNA, Transfer, Phe; Salmonella typhimurium; Valine	1993
Valine 114 replacements in archaeal elongation factor 1 alpha enhanced its ability to interact with aminoacyl-tRNA and kirromycin. Biochemistry, 2002, Dec-10, Volume: 41, Issue:49 Topics: Alanine; Amino Acid Substitution; Archaeal Proteins; Glutamic Acid; GTP Phosphohydrolases; Hot Temperature; Lysine; Mutagenesis, Site-Directed; Peptide Elongation Factor 1; Protein Denaturation; Pyridones; RNA, Transfer, Amino Acid-Specific; Structure-Activity Relationship; Sulfolobus; Valine	2002

Article

Year

A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome.

Journal of bacteriology, 1993, Volume: 175, Issue:1

Topics: Anti-Bacterial Agents; Glycine; Guanosine Triphosphate; Hydrolysis; Kinetics; Macromolecular Substances; Models, Molecular; Peptide Elongation Factor Tu; Phenotype; Protein Biosynthesis; Protein Conformation; Pyridones; Ribosomes; RNA, Transfer, Amino Acyl; RNA, Transfer, Phe; Salmonella typhimurium; Valine

1993

Valine 114 replacements in archaeal elongation factor 1 alpha enhanced its ability to interact with aminoacyl-tRNA and kirromycin.

Biochemistry, 2002, Dec-10, Volume: 41, Issue:49

Topics: Alanine; Amino Acid Substitution; Archaeal Proteins; Glutamic Acid; GTP Phosphohydrolases; Hot Temperature; Lysine; Mutagenesis, Site-Directed; Peptide Elongation Factor 1; Protein Denaturation; Pyridones; RNA, Transfer, Amino Acid-Specific; Structure-Activity Relationship; Sulfolobus; Valine

2002