Breast cancer-specific mutations in CK1epsilon inhibit Wnt/beta-catenin and activate the Wnt/Rac1/JNK and NFAT pathways to decrease cell adhesion and promote cell migration. (Q34048070)

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English	Breast cancer-specific mutations in CK1epsilon inhibit Wnt/beta-catenin and activate the Wnt/Rac1/JNK and NFAT pathways to decrease cell adhesion and promote cell migration.	scientific article

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3 February 2020

Breast cancer-specific mutations in CK1epsilon inhibit Wnt/beta-catenin and activate the Wnt/Rac1/JNK and NFAT pathways to decrease cell adhesion and promote cell migration (English)

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Silvie Foldynová-Trantírková

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Wulf Blankenfeldt

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Lukáš Trantírek

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Vítězslav Bryja

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Alois Kozubík

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3 February 2020

author name string

Petra Sekyrová

2

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Katerina Tmejová

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Eva Brumovská

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Ondrej Bernatík

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publication date

27 May 2010

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3 February 2020

Breast Cancer Research

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3 February 2020

12

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3

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R30

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3 February 2020

describes a project that uses

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RTCA

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CZ Software Mentions: A large dataset of software mentions in the biomedical literature

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Quantitative in situ analysis of beta-catenin expression in breast cancer shows decreased expression is associated with poor outcome

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The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation

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NFAT induces breast cancer cell invasion by promoting the induction of cyclooxygenase-2.

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A formylated hexapeptide ligand mimics the ability of Wnt-5a to impair migration of human breast epithelial cells

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Wnt proteins induce dishevelled phosphorylation via an LRP5/6- independent mechanism, irrespective of their ability to stabilize beta-catenin

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A conserved docking motif for CK1 binding controls the nuclear localization of NFAT1.

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Casein kinase Iepsilon modulates the signaling specificities of dishevelled

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