Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase (Q24316238)

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Transcriptional regulation by p53: one protein, many possibilities

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

The P53 pathway: what questions remain to be explored?

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Decision making by p53: life, death and cancer

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

21 January 2018

p53: puzzle and paradigm

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

21 January 2018

Surfing the p53 network

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

What have animal models taught us about the p53 pathway?

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Live or let die: the cell's response to p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

The IARC TP53 database: new online mutation analysis and recommendations to users

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Keeping p53 in check: essential and synergistic functions of Mdm2 and Mdm4.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

The p53-Mdm2 module and the ubiquitin system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

MDM2 inhibits p300-mediated p53 acetylation and activation by forming a ternary complex with the two proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

RING finger proteins: mediators of ubiquitin ligase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

MDM2 interacts with MDMX through their RING finger domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

An essential function of the extreme C-terminus of MDM2 can be provided by MDMX

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

C-terminal modifications regulate MDM2 dissociation and nuclear export of p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

DNA damage-induced phosphorylation of MdmX at serine 367 activates p53 by targeting MdmX for Mdm2-dependent degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Hdmx protein stability is regulated by the ubiquitin ligase activity of Mdm2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Mono- versus polyubiquitination: differential control of p53 fate by Mdm2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Cytoplasmic tethering is involved in synergistic inhibition of p53 by Mdmx and Mdm2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Identification of p53 sequence elements that are required for MDM2-mediated nuclear export

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

C-terminal ubiquitination of p53 contributes to nuclear export

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Regulation of p53 by Mdm2: fate is in the numbers

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

A mouse p53 mutant lacking the proline-rich domain rescues Mdm4 deficiency and provides insight into the Mdm2-Mdm4-p53 regulatory network

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

RING domain-mediated interaction is a requirement for MDM2's E3 ligase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021

Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2009.07.021