aspartic acid and iodoacetamide
aspartic acid has been researched along with iodoacetamide in 5 studies
Research
Studies (5)
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (20.00) | 18.7374 |
1990's | 3 (60.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors
Authors | Studies |
---|---|
Bellows, DS; Clarke, ID; Diamandis, P; Dirks, PB; Graham, J; Jamieson, LG; Ling, EK; Sacher, AG; Tyers, M; Ward, RJ; Wildenhain, J | 1 |
Alexiev, U; Greenhalgh, DA; Heyn, MP; Khorana, HG; Otto, H; Subramaniam, S | 1 |
Jordan, F; Polgár, L | 1 |
Meister, A; Smith, TK | 1 |
Jung, H; Quick, M | 1 |
Other Studies
5 other study(ies) available for aspartic acid and iodoacetamide
Article | Year |
---|---|
Chemical genetics reveals a complex functional ground state of neural stem cells.
Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells | 2007 |
Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin.
Topics: Amino Acid Sequence; Aspartic Acid; Bacteriorhodopsins; Cysteine; Glutamates; Glutamic Acid; Halobacterium salinarum; Iodoacetamide; Iodoacetates; Iodoacetic Acid; Kinetics; Mutagenesis, Site-Directed; Protons; Recombinant Proteins | 1992 |
Proton nuclear magnetic resonance evidence for the absence of a stable hydrogen bond between the active site aspartate and histidine residues of native subtilisins and for its presence in thiolsubtilisins.
Topics: Aspartic Acid; Binding Sites; Dithionitrobenzoic Acid; Histidine; Hydrogen Bonding; Iodoacetamide; Magnetic Resonance Spectroscopy; Subtilisins | 1981 |
Chemical modification of active site residues in gamma-glutamyl transpeptidase. Aspartate 422 and cysteine 453.
Topics: Acetylation; Amino Acid Sequence; Animals; Aspartic Acid; Binding Sites; Catalysis; Enzyme Stability; gamma-Glutamyltransferase; Hydroxylamine; Hydroxylamines; Imidazoles; Iodoacetamide; Models, Chemical; Molecular Sequence Data; Protein Denaturation; Rats | 1995 |
A conserved aspartate residue, Asp187, is important for Na+-dependent proline binding and transport by the Na+/proline transporter of Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Amino Acid Transport Systems, Neutral; Aspartic Acid; Biological Transport, Active; Blotting, Western; Conserved Sequence; Cysteine; Iodoacetamide; Iodoacetic Acid; Kinetics; Ligands; Membrane Transport Proteins; Molecular Sequence Data; Proline; Protein Binding; Sequence Homology, Amino Acid; Sodium | 1998 |