aspartic acid has been researched along with pepstatin in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (11.11) | 18.7374 |
| 1990's | 5 (55.56) | 18.2507 |
| 2000's | 3 (33.33) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Berman, J; Nichols, JS; Wiseman, JS; Wypij, DM | 1 |
| Kay, J | 1 |
| Brereton, IM; Chai, RY; Kent, SB; Smith, R | 1 |
| Muegge, I; Tao, H; Warshel, A | 1 |
| Ito, M; Narutaki, S; Oda, K; Uchida, K | 1 |
| Abe, S; Oda, K; Oyama, H; Takahashi, S; Ushiyama, S | 1 |
| Carloni, P; Parrinello, M; Piana, S; Sebastiani, D | 1 |
| Backman, D; Danielson, UH | 1 |
| Eapen, A; Sharma, A; Subbarao, SK | 1 |
9 other study(ies) available for aspartic acid and pepstatin
| Article | Year |
|---|---|
Evidence against a role for aspartyl proteases in intracellular processing of big endothelin.
Topics: Ammonium Chloride; Aspartic Acid; Aspartic Acid Endopeptidases; Cells, Cultured; Chloroquine; Chromatography, High Pressure Liquid; Endothelin-1; Endothelins; Endothelium; Hydrogen-Ion Concentration; Indicators and Reagents; Kinetics; Monensin; Pepstatins; Protein Precursors | 1991 |
Aspartic proteinases and their inhibitors.
Topics: Animals; Aspartic Acid; Aspartic Acid Endopeptidases; Binding Sites; Endopeptidases; Humans; Pepstatins; Protease Inhibitors; Protein Conformation; Structure-Activity Relationship | 1985 |
Ionization states of the catalytic residues in HIV-1 protease.
Topics: Aspartic Acid; Catalysis; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Hydrogen-Ion Concentration; Ions; Magnetic Resonance Spectroscopy; Pepstatins | 1996 |
A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding.
Topics: Aspartic Acid; Aspartic Acid Endopeptidases; Binding Sites; Chemical Phenomena; Chemistry, Physical; Crystallization; Electrochemistry; Models, Molecular; Mutation; Pepstatins; Structure-Activity Relationship; Thermodynamics | 1997 |
Identification of carboxyl residues in pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. 101 that participate in catalysis and substrate binding.
Topics: Amino Acid Sequence; Aspartic Acid; Aspartic Acid Endopeptidases; Bacterial Proteins; Binding Sites; Catalytic Domain; Dicyclohexylcarbodiimide; Enzyme Activation; Glutamic Acid; Hydrogen-Ion Concentration; Methanol; Molecular Sequence Data; Oligopeptides; Pepstatins; Peptides; Protease Inhibitors; Pseudomonas; Serine Endopeptidases; Substrate Specificity | 1999 |
Identification of catalytic residues of pepstatin-insensitive carboxyl proteinases from prokaryotes by site-directed mutagenesis.
Topics: Amino Acid Sequence; Aspartic Acid; Aspartic Acid Endopeptidases; Base Sequence; Catalytic Domain; Circular Dichroism; Cloning, Molecular; Conserved Sequence; Escherichia coli; Glutamic Acid; Molecular Sequence Data; Mutagenesis, Site-Directed; Pepstatins; Polymerase Chain Reaction; Protein Conformation; Pseudomonas; Recombinant Proteins; Restriction Mapping; Sequence Alignment; Sequence Homology, Amino Acid; Xanthomonas | 1999 |
Ab initio molecular dynamics-based assignment of the protonation state of pepstatin A/HIV-1 protease cleavage site.
Topics: Aspartic Acid; Catalysis; Formates; HIV Protease; Hydrogen Bonding; Isotopes; Macromolecular Substances; Magnetic Resonance Spectroscopy; Models, Chemical; Pepstatins; Protease Inhibitors; Protein Binding; Protons | 2001 |
Kinetic and mechanistic analysis of the association and dissociation of inhibitors interacting with secreted aspartic acid proteases 1 and 2 from Candida albicans.
Topics: Amino Acid Sequence; Aspartic Acid; Aspartic Acid Endopeptidases; Binding Sites; Candida albicans; Fungal Proteins; Hydrogen-Ion Concentration; Isoenzymes; Molecular Sequence Data; Pepstatins; Protease Inhibitors; Sequence Alignment; Surface Plasmon Resonance; Thermodynamics | 2003 |
Parasite killing in Plasmodium vivax malaria by nitric oxide: implication of aspartic protease inhibition.
Topics: Animals; Aspartic Acid; Aspartic Acid Endopeptidases; Catalase; Catalytic Domain; Chromatography, High Pressure Liquid; Cysteine; Dithiothreitol; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Erythrocytes; Gelatin; Glutamate Dehydrogenase (NADP+); Glutathione; Hydrogen-Ion Concentration; Inhibitory Concentration 50; Malaria, Vivax; Molsidomine; Nitric Oxide; Nitric Oxide Donors; Nitroprusside; Pepsin A; Pepstatins; Plasmodium; Plasmodium vivax; Protease Inhibitors; Reactive Nitrogen Species; S-Nitrosoglutathione; Time Factors; Up-Regulation | 2004 |