Identification of a surface on the beta-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5 (Q28214056)

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scientific article (publication date: July 2001)

Language	Label	Description	Also known as
English	Identification of a surface on the beta-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5	scientific article (publication date: July 2001)

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scholarly article

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Identification of a surface on the beta-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5 (English)

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author name string

M R Steele

1

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A McCahill

2

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D S Thompson

3

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C MacKenzie

4

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N W Isaacs

5

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M D Houslay

6

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G B Bolger

7

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language of work or name

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publication date

July 2001

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Cellular Signalling

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13

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7

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507-13

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Signaling through scaffold, anchoring, and adaptor proteins

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Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins

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An autoregulatory region in protein kinase C: the pseudoanchoring site

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Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit

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RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells

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Association of RACK1 and PKCbeta with the common beta-chain of the IL-5/IL-3/GM-CSF receptor.

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RACK1, a protein kinase C anchoring protein, coordinates the binding of activated protein kinase C and select pleckstrin homology domains in vitro

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The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform

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The ancient regulatory-protein family of WD-repeat proteins

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Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry

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10.1016/S0898-6568(01)00167-X

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Consolidated OpenCitations Corpus – April 2017

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