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glycyl-l-phenylalanine and taurine

glycyl-l-phenylalanine has been researched along with taurine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Bonini, BM; Thevelein, JM; Van Zeebroeck, G; Versele, M	1
BENNETT, WE; DANNENBERG, AM	1

Other Studies

2 other study(ies) available for glycyl-l-phenylalanine and taurine

Article	Year
Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor. Nature chemical biology, 2009, Volume: 5, Issue:1 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
HYDROLYTIC ENZYMES OF RABBIT MONONUCLEAR EXUDATE CELLS. I. QUANTITATIVE ASSAY AND PROPERTIES OF CERTAIN PROTEASES, NON-SPECIFIC ESTERASES, AND LIPASES OF MONONUCLEAR AND POLYMORPHONUCLEAR CELLS AND ERYTHROCYTES. The Journal of cell biology, 1964, Volume: 21 Topics: Animals; Azoles; Benzoates; Calcium; Carboxylesterase; Dipeptides; Edetic Acid; Endopeptidases; Enzyme Inhibitors; Erythrocytes; Esterases; Exudates and Transudates; Hemoglobins; Hydrogen-Ion Concentration; Hydrolysis; Leukocytes; Lipase; Lymphocytes; Macrophages; Naphthalenes; Naphthols; Peptide Hydrolases; Phenylalanine; Protamines; Rabbits; Research; Sodium Chloride; Taurine; Tyrosine	1964

Article

Year

Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor.

Nature chemical biology, 2009, Volume: 5, Issue:1

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

HYDROLYTIC ENZYMES OF RABBIT MONONUCLEAR EXUDATE CELLS. I. QUANTITATIVE ASSAY AND PROPERTIES OF CERTAIN PROTEASES, NON-SPECIFIC ESTERASES, AND LIPASES OF MONONUCLEAR AND POLYMORPHONUCLEAR CELLS AND ERYTHROCYTES.

The Journal of cell biology, 1964, Volume: 21

Topics: Animals; Azoles; Benzoates; Calcium; Carboxylesterase; Dipeptides; Edetic Acid; Endopeptidases; Enzyme Inhibitors; Erythrocytes; Esterases; Exudates and Transudates; Hemoglobins; Hydrogen-Ion Concentration; Hydrolysis; Leukocytes; Lipase; Lymphocytes; Macrophages; Naphthalenes; Naphthols; Peptide Hydrolases; Phenylalanine; Protamines; Rabbits; Research; Sodium Chloride; Taurine; Tyrosine

1964