A cell-permeant glutamic acid derivative that enhances insulin release in response to glucose in isolated islets and in animal models of diabetes also potentiates the insulinotropic potential of glyburide and GLP-1.
A cell-permeant glutamic acid derivative that enhances insulin release in response to glucose in isolated islets and in animal models of diabetes also potentiates the insulinotropic potential of glyburide and GLP-1.
Leelamine is a diterpene molecule whose name derives from the Sanskrit word leela which means "play". It has weak affinity for the human CB1 and CB2 receptors, exhibiting 20% displacement of [3H]-CP55940 at a concentration of 10 µM.
Leelamine is a diterpene molecule whose name derives from the Sanskrit word leela which means "play". It has weak affinity for the human CB1 and CB2 receptors, exhibiting 20% displacement of [3H]-CP55940 at a concentration of 10 µM.
The active metabolite of ramipril, an ACE inhibitor (pKi = 9.08 in human heart) that suppresses the conversion of angiotensin I to angiotensin II and the degradation of bradykinin, thereby preventing vasoconstriction interferes with the targeting
The active metabolite of ramipril, an ACE inhibitor (pKi = 9.08 in human heart) that suppresses the conversion of angiotensin I to angiotensin II and the degradation of bradykinin, thereby preventing vasoconstriction interferes with the targeting
A cell-permeant glutamic acid derivative that enhances insulin release in response to glucose in isolated islets and in animal models of diabetes also potentiates the insulinotropic potential of glyburide and GLP-1.
A cell-permeant glutamic acid derivative that enhances insulin release in response to glucose in isolated islets and in animal models of diabetes also potentiates the insulinotropic potential of glyburide and GLP-1.
A second generation antiepileptic compound used to prevent convulsions in a variety of settings binds the synaptic vesicle protein SV2A (pIC<sub>50</sub> = 5.7), presumably altering vesicle exocytosis alters the metabolism and turnover of GABA.
A second generation antiepileptic compound used to prevent convulsions in a variety of settings binds the synaptic vesicle protein SV2A (pIC<sub>50</sub> = 5.7), presumably altering vesicle exocytosis alters the metabolism and turnover of GABA.
A cell-permeant glutamic acid derivative that enhances insulin release in response to glucose in isolated islets and in animal models of diabetes also potentiates the insulinotropic potential of glyburide and GLP-1.
A cell-permeant glutamic acid derivative that enhances insulin release in response to glucose in isolated islets and in animal models of diabetes also potentiates the insulinotropic potential of glyburide and GLP-1.
A polysaccharide made of &alpha-D-glucose units that constitutes about 20% of starch acts as an indicator, turning blue in the presence of iodine, and has also been coupled to magnetic beads for the isolation and purification of maltose-binding
A polysaccharide made of &alpha-D-glucose units that constitutes about 20% of starch acts as an indicator, turning blue in the presence of iodine, and has also been coupled to magnetic beads for the isolation and purification of maltose-binding
A second generation antiepileptic compound used to prevent convulsions in a variety of settings binds the synaptic vesicle protein SV2A (pIC<sub>50</sub> = 5.7), presumably altering vesicle exocytosis alters the metabolism and turnover of GABA.
A second generation antiepileptic compound used to prevent convulsions in a variety of settings binds the synaptic vesicle protein SV2A (pIC<sub>50</sub> = 5.7), presumably altering vesicle exocytosis alters the metabolism and turnover of GABA.
The active metabolite of ramipril, an ACE inhibitor (pKi = 9.08 in human heart) that suppresses the conversion of angiotensin I to angiotensin II and the degradation of bradykinin, thereby preventing vasoconstriction interferes with the targeting
The active metabolite of ramipril, an ACE inhibitor (pKi = 9.08 in human heart) that suppresses the conversion of angiotensin I to angiotensin II and the degradation of bradykinin, thereby preventing vasoconstriction interferes with the targeting