J Biol Chem. 1962 Nov;237:3476-85.

Metabolism of gamma-hydroxyglutamic acid. I. Conversion to alpha-hydroxy-gamma-ketoglutarate by purified glutamic-aspartic transaminase to rat liver.

GOLDSTONE A, ADAMS E.

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PURIFICATION OF RAT-LIVER GAMMA-HYDROXYGLUTAMATE TRANSAMINASE AND ITS PROBABLE IDENTITY WITH GLUTAMATE-ASPARTATE TRANSAMINASE. [Biochim Biophys Acta. 1964]
PURIFICATION OF RAT-LIVER GAMMA-HYDROXYGLUTAMATE TRANSAMINASE AND ITS PROBABLE IDENTITY WITH GLUTAMATE-ASPARTATE TRANSAMINASE.
MAITRA U, DEEKKER E. Biochim Biophys Acta. 1964 Mar 9; 81:517-32.
[DISTRIBUTION OF GLUTAMIC ACID DECARBOXYLASE, GAMMA-AMINOBUTYRATE-ALPHA-KETOGLUTARATE TRANSAMINASE AND GAMMA-AMINOBUTYRIC ACID AND THEIR RELATIONSHIPS IN THE RAT BRAIN]. [Sheng Li Xue Bao. 1963]
[DISTRIBUTION OF GLUTAMIC ACID DECARBOXYLASE, GAMMA-AMINOBUTYRATE-ALPHA-KETOGLUTARATE TRANSAMINASE AND GAMMA-AMINOBUTYRIC ACID AND THEIR RELATIONSHIPS IN THE RAT BRAIN].
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THE METABOLISM OF GAMMA-HYDROXYGLUTAMATE IN RAT LIVER. II. A TRANSAMINASE CONCERNED IN GAMMA-HYDROXYGLUTAMATE METABOLISM. [Biochim Biophys Acta. 1963]
THE METABOLISM OF GAMMA-HYDROXYGLUTAMATE IN RAT LIVER. II. A TRANSAMINASE CONCERNED IN GAMMA-HYDROXYGLUTAMATE METABOLISM.
KURATOMI K, FUKUNAGA K, KOBAYASHI Y. Biochim Biophys Acta. 1963 Dec 13; 78:629-36.
Review The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants. [Neurochem Int. 2004]
Review The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants.
Cooper AJ. Neurochem Int. 2004 Jun; 44(8):557-77.

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Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.
Riedel TJ, Johnson LC, Knight J, Hantgan RR, Holmes RP, Lowther WT. PLoS One. 2011; 6(10):e26021. Epub 2011 Oct 6.
Hydroxyprolinaemia with normal development. [Arch Dis Child. 1980]
Hydroxyprolinaemia with normal development.
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Control of the citric acid cycle by glyoxylate. Mechanism of the inhibition by oxalomalate and gamma-hydroxy-alpha-oxoglutarate. [Biochem J. 1967]
Control of the citric acid cycle by glyoxylate. Mechanism of the inhibition by oxalomalate and gamma-hydroxy-alpha-oxoglutarate.
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Metabolism of gamma-hydroxyglutamic acid. I. Conversion to alpha-hydroxy-gamma-ketoglutarate by purified glutamic-aspartic transaminase to rat liver.

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