Product cited in:
Kanaani, Lissin, Kash et al.: "The hydrophilic isoform of glutamate decarboxylase, GAD67, is targeted to membranes and nerve terminals independent of dimerization with the hydrophobic membrane-anchored isoform, GAD65." in: The Journal of biological chemistry, Vol. 274, Issue 52, pp. 37200-9, 2000 (PubMed).
Hsu, Thomas, Chen et al.: "Role of synaptic vesicle proton gradient and protein phosphorylation on ATP-mediated activation of membrane-associated brain glutamate decarboxylase." in: The Journal of biological chemistry, Vol. 274, Issue 34, pp. 24366-71, 1999 (PubMed).
Kim, Richter, Aanstoot et al.: "Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets." in: Diabetes, Vol. 42, Issue 12, pp. 1799-808, 1993 (PubMed).
Esclapez, Tillakaratne, Kaufman et al.: "Comparative localization of two forms of glutamic acid decarboxylase and their mRNAs in rat brain supports the concept of functional differences between the forms." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 14, Issue 3 Pt 2, pp. 1834-55, 1994 (PubMed).
Chang, Gottlieb: "Characterization of the proteins purified with monoclonal antibodies to glutamic acid decarboxylase." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 8, Issue 6, pp. 2123-30, 1988 (PubMed).
Kaufman, McGinnis, Krieger et al.: "Brain glutamate decarboxylase cloned in lambda gt-11: fusion protein produces gamma-aminobutyric acid." in: Science (New York, N.Y.), Vol. 232, Issue 4754, pp. 1138-40, 1986 (PubMed).
Bu, Erlander, Hitz et al.: "Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 6, pp. 2115-9, 1992 (PubMed).