alanine and 1,5-i-aedans

alanine has been researched along with 1,5-i-aedans 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
Honma, M; Kawai, J; Yamada, M	1
Flint, DH	1

Other Studies

2 other study(ies) available for alanine and 1,5-i-aedans

Article	Year
Identification of the reactive sulfhydryl group of 1-aminocyclopropane-1-carboxylate deaminase. Bioscience, biotechnology, and biochemistry, 1993, Volume: 57, Issue:12 Topics: Alanine; Amino Acid Sequence; Amino Acids; Amino Acids, Cyclic; Carbon-Carbon Lyases; Cysteine; Iodoacetamide; Lyases; Molecular Sequence Data; Naphthalenesulfonates; Protein Conformation; Pseudomonas; Spectrophotometry, Ultraviolet; Temperature	1993
Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. The Journal of biological chemistry, 1996, Jul-05, Volume: 271, Issue:27 Topics: Alanine; Amino Acid Sequence; Azotobacter vinelandii; Bacterial Proteins; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Disulfides; Escherichia coli; Genes, Bacterial; Haemophilus influenzae; Hydro-Lyases; Iron-Sulfur Proteins; Kinetics; Macromolecular Substances; Molecular Sequence Data; Naphthalenesulfonates; Pantetheine; Peptide Fragments; Pyridoxal Phosphate; Sequence Homology, Amino Acid; Sulfhydryl Reagents	1996

Article

Year

Identification of the reactive sulfhydryl group of 1-aminocyclopropane-1-carboxylate deaminase.

Bioscience, biotechnology, and biochemistry, 1993, Volume: 57, Issue:12

Topics: Alanine; Amino Acid Sequence; Amino Acids; Amino Acids, Cyclic; Carbon-Carbon Lyases; Cysteine; Iodoacetamide; Lyases; Molecular Sequence Data; Naphthalenesulfonates; Protein Conformation; Pseudomonas; Spectrophotometry, Ultraviolet; Temperature

1993

Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase.

The Journal of biological chemistry, 1996, Jul-05, Volume: 271, Issue:27

Topics: Alanine; Amino Acid Sequence; Azotobacter vinelandii; Bacterial Proteins; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Disulfides; Escherichia coli; Genes, Bacterial; Haemophilus influenzae; Hydro-Lyases; Iron-Sulfur Proteins; Kinetics; Macromolecular Substances; Molecular Sequence Data; Naphthalenesulfonates; Pantetheine; Peptide Fragments; Pyridoxal Phosphate; Sequence Homology, Amino Acid; Sulfhydryl Reagents

1996