(Q28579703)

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HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized

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31 January 2017

HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized (English)

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31 January 2017

5

Kwang-Hyun Baek

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31 January 2017

4

Yu-Kyoung Oh

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31 January 2017

Hye-Jin Lee

1

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31 January 2017

Myung-Sun Kim

series ordinal

2

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31 January 2017

Yu-Kyung Kim

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3

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31 January 2017

language of work or name

English

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publication date

29 August 2005

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579

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31 January 2017

4867–4872

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21

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The ubiquitin-proteasome pathway: on protein death and cell life

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reference URL

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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Mechanisms underlying ubiquitination

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reference URL

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Regulation of p53 stability by Mdm2

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Human mdm2 mediates multiple mono-ubiquitination of p53 by a mechanism requiring enzyme isomerization

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Polyubiquitination of p53 by a ubiquitin ligase activity of p300.

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization

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21 January 2018

A dynamic role of HAUSP in the p53-Mdm2 pathway

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USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

DUB-1A, a novel deubiquitinating enzyme subfamily member, is polyubiquitinated and cytokine-inducible in B-lymphocytes

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Deubiquitinating enzyme USP36 contains the PEST motif and is polyubiquitinated

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.

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SUMO-1 modification activates the transcriptional response of p53

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity

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reference URL

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.07.048

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21 January 2018

Identifiers

DOI

10.1016/J.FEBSLET.2005.07.048

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31 January 2017

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31 January 2017

ResearchGate publication ID

7648418

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(Q28579703)

HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized

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