Page last updated: 2024-08-26

glycylsarcosine and glycyltyrosine

glycylsarcosine has been researched along with glycyltyrosine in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Faria, TN; Quan, Y; Smith, RL; Stouch, TR; Timoszyk, JK; Vig, BS; Wall, DA	1
Frølund, S; Holm, R; Kall, MA; Langthaler, L; Nielsen, CU	1

Other Studies

2 other study(ies) available for glycylsarcosine and glycyltyrosine

Article	Year
Human PEPT1 pharmacophore distinguishes between dipeptide transport and binding. Journal of medicinal chemistry, 2006, Jun-15, Volume: 49, Issue:12 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
Intestinal drug transport via the proton-coupled amino acid transporter PAT1 (SLC36A1) is inhibited by Gly-X(aa) dipeptides. Molecular pharmaceutics, 2012, Sep-04, Volume: 9, Issue:9 Topics: Administration, Oral; Amino Acid Transport Systems; Animals; Biological Transport; Caco-2 Cells; Cell Membrane Permeability; Dipeptides; Glycine; Humans; Intestinal Absorption; Intestinal Mucosa; Intestines; Isoxazoles; Male; Oocytes; Protons; Rats; Rats, Sprague-Dawley; Symporters; Xenopus laevis	2012

Article

Year

Human PEPT1 pharmacophore distinguishes between dipeptide transport and binding.

Journal of medicinal chemistry, 2006, Jun-15, Volume: 49, Issue:12

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

Intestinal drug transport via the proton-coupled amino acid transporter PAT1 (SLC36A1) is inhibited by Gly-X(aa) dipeptides.

Molecular pharmaceutics, 2012, Sep-04, Volume: 9, Issue:9

Topics: Administration, Oral; Amino Acid Transport Systems; Animals; Biological Transport; Caco-2 Cells; Cell Membrane Permeability; Dipeptides; Glycine; Humans; Intestinal Absorption; Intestinal Mucosa; Intestines; Isoxazoles; Male; Oocytes; Protons; Rats; Rats, Sprague-Dawley; Symporters; Xenopus laevis

2012