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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Archives of Insect B...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Archives of Insect Biochemistry and Physiology
Article . 2002 . Peer-reviewed
License: Wiley Online Library User Agreement
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Ras target protein canoe is a substrate for Cdc2 and Cdk5 kinases

Authors: Kuniaki, Takahashi; Noriko, Hamada; Daisuke, Yamamoto;

Ras target protein canoe is a substrate for Cdc2 and Cdk5 kinases

Abstract

AbstractMutations in the canoe locus of Drosophila lead to failure in the dorsal closure of the embryonic epidermis and pattern formation defects in imaginal eyes and wings. In the wing, the canoe mutants develop extra veins when they are heterozygous for shaggy, a mutation in the locus encoding the glycogen synthase kinase 3β (Gsk3β), which has been known to phosphorylate the Armadillo protein. Although Canoe has a putative target sequence for phosphorylation by Gsk3β similar to that found in Armadillo, in vitro experiments indicate that Canoe is not phosphorylated by Gsk3β. Instead, Canoe is demonstrated to be a good substrate of Cdc2 and Cdk5 kinases. Thus, Cdc2 and Cdk5 kinases are the potential regulators of the function of Canoe in morphogenesis. Arch. Insect Biochem. Physiol. 49:102–107, 2002. © 2002 Wiley‐Liss, Inc.

Keywords

Armadillo Domain Proteins, Binding Sites, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Molecular Sequence Data, Glycogen Synthase Kinases, Cyclin-Dependent Kinase 5, Protein Serine-Threonine Kinases, Cyclin-Dependent Kinases, Substrate Specificity, Glycogen Synthase Kinase 3, Drosophila melanogaster, CDC2 Protein Kinase, Calcium-Calmodulin-Dependent Protein Kinases, Animals, Drosophila Proteins, Insect Proteins, Cattle, Amino Acid Sequence, Phosphorylation

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
3
Average
Average
Average
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