(Q24290417)

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The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation

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The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation (English)

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phosphorylation

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Casein kinase 2 alpha 1

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GOA release 2020-03-11

protein serine/threonine kinase activity

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GOA release 2020-03-11

author name string

J Torres

1

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R Pulido

2

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language of work or name

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publication date

12 January 2001

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Journal of Biological Chemistry

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276

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2

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993-8

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Asymmetric expression of protein kinase CK2 subunits in human kidney tumors

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The ubiquitin-proteasome proteolytic pathway

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Casein kinase 2: an 'eminence grise' in cellular regulation?

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Phosphorylation of transcriptional factors and cell-cycle-dependent proteins by casein kinase II.

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Differential nuclear and cytoplasmic expression of PTEN in normal thyroid tissue, and benign and malignant epithelial thyroid tumors

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The multiple roles of PTEN in tumor suppression

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Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association

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Heterogeneous lack of expression of the tumour suppressor PTEN protein in human neoplastic tissues

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Proteasome inhibitors: valuable new tools for cell biologists

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PTEN: a tumour suppressor that functions as a phospholipid phosphatase

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Analysis of the cellular functions of PTEN using catalytic domain and C-terminal mutations: differential effects of C-terminal deletion on signalling pathways downstream of phosphoinositide 3-kinase

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The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

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Identifiers

10.1074/JBC.M009134200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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