(Q38360337)

2 September 2017

title

Nuclear phosphatases and the proteasome in suppression of STAT1 activity in hepatocytes (English)

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2 September 2017

Dongxu Liu

1

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2 September 2017

Jennifer Scafidi

2

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2 September 2017

Anne E Prada

3

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2 September 2017

Kamyar Zahedi

4

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2 September 2017

Alvin E Davis

5

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2 September 2017

language of work or name

English

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publication date

1 December 2002

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Biochemical and Biophysical Research Communications

2 September 2017

published in

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2 September 2017

volume

299

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2 September 2017

issue

4

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2 September 2017

page(s)

574-580

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Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins

2 September 2017

cites work

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The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals

7 January 2021

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Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis

7 January 2021

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The nuclear ubiquitin-proteasome system degrades MyoD.

7 January 2021

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A nuclear tyrosine phosphatase downregulates interferon-induced gene expression

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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The ubiquitin-activating enzyme E1 is phosphorylated and localized to the nucleus in a cell cycle-dependent manner

7 January 2021

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Substrate targeting in the ubiquitin system

7 January 2021

1 reference

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Involvement of proteasomes in regulating Jak-STAT pathways upon interleukin-2 stimulation.

7 January 2021

1 reference

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10.1016/S0006-291X(02)02694-3

7 January 2021

Identifiers

DOI

1 reference

2 September 2017

1 reference