Biologically Active Small Molecules

An irreversible inhibitor of ornithine decarboxylase that suppresses polyamine biosynthesis displays antiangiogenic, cytostatic, and antiparasitic effects.

An irreversible inhibitor of ornithine decarboxylase that suppresses polyamine biosynthesis displays antiangiogenic, cytostatic, and antiparasitic effects.

DL-&alpha-lipoic acid is a cyclic disulfide antioxidant that interconverts with its reduced dithiol form. It is an essential cofactor for decarboxylation reactions of the citric acid cycle, and acts as a general antioxidant.

DL-&alpha-lipoic acid is a cyclic disulfide antioxidant that interconverts with its reduced dithiol form. It is an essential cofactor for decarboxylation reactions of the citric acid cycle, and acts as a general antioxidant.

DL-&alpha-lipoic acid is a cyclic disulfide antioxidant that interconverts with its reduced dithiol form. It is an essential cofactor for decarboxylation reactions of the citric acid cycle, and acts as a general antioxidant.

DL-&alpha-lipoic acid is a cyclic disulfide antioxidant that interconverts with its reduced dithiol form. It is an essential cofactor for decarboxylation reactions of the citric acid cycle, and acts as a general antioxidant.

A competitive mGluR1 antagonist (Ki = 298 &muM IC₅₀ = 1 mM for rat mGluR1&alpha when challenged with glutamate) at concentrations from 10-300 &muM, used to characterize the role of mGluR in LTP in the hippocampus in a model of

A competitive mGluR1 antagonist (Ki = 298 &muM IC₅₀ = 1 mM for rat mGluR1&alpha when challenged with glutamate) at concentrations from 10-300 &muM, used to characterize the role of mGluR in LTP in the hippocampus in a model of

The racemic version of the selective NMDA receptor antagonist, D-AP5 that competitively inhibits the glutamate binding site of NMDA receptors (Kd = 1.4 &muM) D-AP5 is the active (&minus)-stereoisomer, while L-AP5, the(+)-isomer, demonstrates

The racemic version of the selective NMDA receptor antagonist, D-AP5 that competitively inhibits the glutamate binding site of NMDA receptors (Kd = 1.4 &muM) D-AP5 is the active (&minus)-stereoisomer, while L-AP5, the(+)-isomer, demonstrates

The racemic version of the selective NMDA receptor antagonist, D-AP5 that competitively inhibits the glutamate binding site of NMDA receptors (Kd = 1.4 &muM) D-AP5 is the active (&minus)-stereoisomer, while L-AP5, the(+)-isomer, demonstrates

The racemic version of the selective NMDA receptor antagonist, D-AP5 that competitively inhibits the glutamate binding site of NMDA receptors (Kd = 1.4 &muM) D-AP5 is the active (&minus)-stereoisomer, while L-AP5, the(+)-isomer, demonstrates