n-glycylalanine has been researched along with glycyl-l-phenylalanine in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (20.00) | 18.2507 |
2000's | 4 (80.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Collantes, ER; Dunn, WJ | 1 |
Faria, TN; Quan, Y; Smith, RL; Stouch, TR; Timoszyk, JK; Vig, BS; Wall, DA | 1 |
Bonini, BM; Thevelein, JM; Van Zeebroeck, G; Versele, M | 1 |
Kumar, I; Pratt, RF | 2 |
5 other study(ies) available for n-glycylalanine and glycyl-l-phenylalanine
Article | Year |
---|---|
Amino acid side chain descriptors for quantitative structure-activity relationship studies of peptide analogues.
Topics: Amino Acid Sequence; Amino Acids; Bradykinin; Electrochemistry; Molecular Sequence Data; Peptides; Structure-Activity Relationship; Taste | 1995 |
Human PEPT1 pharmacophore distinguishes between dipeptide transport and binding.
Topics: Animals; Binding Sites; Biological Transport; Cell Line; Dipeptides; Dogs; Electricity; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Peptide Transporter 1; Proline; Protein Binding; Protein Conformation; Structure-Activity Relationship; Symporters | 2006 |
Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor.
Topics: Amino Acid Transport Systems; Amino Acids; Biological Transport; Catalytic Domain; Dipeptides; Gene Expression Regulation, Fungal; Mutagenesis; Protein Conformation; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Signal Transduction | 2009 |
Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 DD-peptidase: the structural basis of acyl acceptor specificity.
Topics: Catalysis; Dipeptides; Kinetics; Models, Chemical; Models, Molecular; Oligopeptides; Peptidyl Transferases; Serine-Type D-Ala-D-Ala Carboxypeptidase; Streptomyces; Structure-Activity Relationship; Substrate Specificity | 2005 |
Transpeptidation reactions of a specific substrate catalyzed by the streptomyces R61 DD-peptidase: characterization of a chromogenic substrate and acyl acceptor design.
Topics: Binding Sites; Catalysis; Chromogenic Compounds; Dipeptides; Esters; Molecular Mimicry; Oligopeptides; Peptidyl Transferases; Serine-Type D-Ala-D-Ala Carboxypeptidase; Streptomyces; Substrate Specificity; Sulfhydryl Compounds | 2005 |