(Q28182784)

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A kinase anchoring protein (AKAP) interaction and dimerization of the RIalpha and RIbeta regulatory subunits of protein kinase a in vivo by the yeast two hybrid system

scientific article (publication date: 28 March 2003)

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scholarly article

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A kinase anchoring protein (AKAP) interaction and dimerization of the RIalpha and RIbeta regulatory subunits of protein kinase a in vivo by the yeast two hybrid system (English)

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3

object named as

Kjetil Taskén

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author name string

Cathrine R Carlson

1

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Anja Ruppelt

2

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language of work or name

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publication date

28 March 2003

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Journal of Molecular Biology

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327

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3

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609-18

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16 Structure, function, and regulation of human cAMP-dependent protein kinases

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Unconventional myosin VIIA is a novel A-kinase-anchoring protein

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Isoform-specific differences between the type Ialpha and IIalpha cyclic AMP-dependent protein kinase anchoring domains revealed by solution NMR.

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Dimerization/docking domain of the type Ialpha regulatory subunit of cAMP-dependent protein kinase. Requirements for dimerization and docking are distinct but overlapping

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A stable alpha-helical domain at the N terminus of the RIalpha subunits of cAMP-dependent protein kinase is a novel dimerization/docking motif

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Molecular cloning, cDNA structure and tissue-specific expression of the human regulatory subunit RI beta of cAMP-dependent protein kinases

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Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding

1 reference

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Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95

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AKAP mediated signal transduction

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10.1016/S0022-2836(03)00093-7

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