glutamate-1-semialdehyde has been researched along with heme in 3 studies
Studies (glutamate-1-semialdehyde) | Trials (glutamate-1-semialdehyde) | Recent Studies (post-2010) (glutamate-1-semialdehyde) | Studies (heme) | Trials (heme) | Recent Studies (post-2010) (heme) |
---|---|---|---|---|---|
14 | 0 | 3 | 19,086 | 115 | 4,781 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 2 (66.67) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Kannangara, CG; von Wettstein, D; Vothknecht, UC | 1 |
CaJacob, CA; Loida, PJ; Thompson, RL; Walker, DM | 1 |
Chen, X; Dong, W; Fang, Y; Gong, W; Lin, Y; Liu, L; Zhao, A; Zhao, S | 1 |
3 other study(ies) available for glutamate-1-semialdehyde and heme
Article | Year |
---|---|
Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase.
Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Aminolevulinic Acid; Base Sequence; Cytochromes; Escherichia coli; Glutamates; Glutamic Acid; Glutathione Transferase; Heme; Hemin; Hordeum; Molecular Sequence Data; Oxidation-Reduction; Recombinant Fusion Proteins; Spectrophotometry | 1996 |
Novel inhibitors of glutamyl-tRNA(Glu) reductase identified through cell-based screening of the heme/chlorophyll biosynthetic pathway.
Topics: Aldehyde Oxidoreductases; Aminolevulinic Acid; Arabidopsis; Chlorophyll; Cyclohexanecarboxylic Acids; Drug Evaluation, Preclinical; Enzyme Inhibitors; Escherichia coli; Glutamates; Heme; Hordeum; Inhibitory Concentration 50; Intramolecular Transferases; Kinetics; Mutation; Recombinant Fusion Proteins; Reproducibility of Results; RNA, Transfer, Gln; Sequence Homology, Amino Acid; Spinacia oleracea; Substrate Specificity | 1999 |
Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein.
Topics: Aldehyde Oxidoreductases; Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Binding Sites; Crystallography, X-Ray; Glutamates; Glutamic Acid; Heme; Models, Molecular; Molecular Sequence Data; Multiprotein Complexes; NADP; Protein Interaction Domains and Motifs; Recombinant Proteins; RNA-Binding Proteins; Sequence Homology, Amino Acid; Static Electricity | 2014 |