(Q27629129)

5

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author name string

T A Graham

1

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F Mao

3

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D Kimelman

Single amino acid substitutions in proteins of the armadillo gene family abolish their binding to alpha-catenin

4

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language of work or name

English

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publication date

8 December 2000

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published in

Cell

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volume

103

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page(s)

885-96

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issue

6

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cites work

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Interaction among GSK-3, GBP, axin, and APC in Xenopus axis specification

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Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3 beta

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Functional characterization of multiple transactivating elements in beta-catenin, some of which interact with the TATA-binding protein in vitro

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The p300/CBP acetyltransferases function as transcriptional coactivators of beta-catenin in vertebrates

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Xenopus axin interacts with glycogen synthase kinase-3 beta and is expressed in the anterior midbrain.

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Three-dimensional structure of the armadillo repeat region of beta-catenin

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E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton

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Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin

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An in vivo structure-function study of armadillo, the beta-catenin homologue, reveals both separate and overlapping regions of the protein required for cell adhesion and for wingless signaling

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Drosophila alpha-catenin and E-cadherin bind to distinct regions of Drosophila Armadillo.

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Structure of the Dimerization and β-Catenin- Binding Region of α-Catenin

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The transcriptional coactivator CBP interacts with beta-catenin to activate gene expression

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Armadillo coactivates transcription driven by the product of the Drosophila segment polarity gene dTCF

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

3671325

3671325

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference