Enhancement of recombinant alpha 1 beta 1 gamma 2L gamma-aminobutyric acidA receptor whole-cell currents by protein kinase C is mediated through phosphorylation of both beta 1 and gamma 2L subunits.

Y F Lin; T P Angelotti; E M Dudek; M D Browning; R L Macdonald

Abstract

Enhancement of recombinant alpha 1 beta 1 gamma 2L gamma-aminobutyric acidA receptor whole-cell currents by protein kinase C is mediated through phosphorylation of both beta 1 and gamma 2L subunits.

Y F Lin, T P Angelotti, E M Dudek, M D Browning and R L Macdonald

Molecular Pharmacology July 1996, 50 (1) 185-195;

Y F Lin

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T P Angelotti

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E M Dudek

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M D Browning

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R L Macdonald

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Molecular Pharmacology

Vol. 50, Issue 1

1 Jul 1996

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Abstract

Enhancement of recombinant alpha 1 beta 1 gamma 2L gamma-aminobutyric acidA receptor whole-cell currents by protein kinase C is mediated through phosphorylation of both beta 1 and gamma 2L subunits.

Y F Lin, T P Angelotti, E M Dudek, M D Browning and R L Macdonald

Molecular Pharmacology July 1, 1996, 50 (1) 185-195;

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Abstract

Enhancement of recombinant alpha 1 beta 1 gamma 2L gamma-aminobutyric acidA receptor whole-cell currents by protein kinase C is mediated through phosphorylation of both beta 1 and gamma 2L subunits.

Y F Lin, T P Angelotti, E M Dudek, M D Browning and R L Macdonald

Molecular Pharmacology July 1, 1996, 50 (1) 185-195;

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Enhancement of recombinant alpha 1 beta 1 gamma 2L gamma-aminobutyric acidA receptor whole-cell currents by protein kinase C is mediated through phosphorylation of both beta 1 and gamma 2L subunits.

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Enhancement of recombinant alpha 1 beta 1 gamma 2L gamma-aminobutyric acidA receptor whole-cell currents by protein kinase C is mediated through phosphorylation of both beta 1 and gamma 2L subunits.

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