Mdm2 and MdmX partner to regulate p53. (Q38016717)

27 August 2017

title

Mdm2 and MdmX partner to regulate p53. (English)

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27 August 2017

Xinjiang Wang

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27 August 2017

Xuejun Jiang

series ordinal

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27 August 2017

language of work or name

English

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publication date

8 March 2012

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27 August 2017

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27 August 2017

volume

586

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27 August 2017

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27 August 2017

page(s)

1390-1396

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Blinded by the Light: The Growing Complexity of p53

27 August 2017

cites work

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The first 30 years of p53: growing ever more complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The p53 tumor suppressor protein is a critical regulator of hematopoietic stem cell behavior

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Signaling to p53: ribosomal proteins find their way.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Regulation of the p53 tumor suppressor protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The p53 orchestra: Mdm2 and Mdmx set the tone

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Posttranslational modification of p53: cooperative integrators of function

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Regulating the p53 pathway: in vitro hypotheses, in vivo veritas

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Ubiquitin, E6-AP, and their role in p53 inactivation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

p53 ubiquitination: Mdm2 and beyond

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Mdm2-mediated ubiquitylation: p53 and beyond.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

p53 regulation by ubiquitin

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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.2012.02.049

Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Mdm2 promotes the rapid degradation of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Regulation of p53 stability by Mdm2

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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.2012.02.049

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.2012.02.049

Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Making sense of ubiquitin ligases that regulate p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Mdm2 regulates p53 mRNA translation through inhibitory interactions with ribosomal protein L26

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Targeted inactivation of Mdm2 RING finger E3 ubiquitin ligase activity in the mouse reveals mechanistic insights into p53 regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Unlocking the Mdm2-p53 loop: ubiquitin is the key.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Synergistic roles of Mdm2 and Mdm4 for p53 inhibition in central nervous system development

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Mdmx as an essential regulator of p53 activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

MDM2 interacts with MDMX through their RING finger domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

MdmX Protein Is Essential for Mdm2 Protein-mediated p53 Polyubiquitination

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Mutual dependence of MDM2 and MDMX in their functional inactivation of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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.2012.02.049

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Heterodimerization of Mdm2 and Mdm4 is critical for regulating p53 activity during embryogenesis but dispensable for p53 and Mdm2 stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

MdmX protects p53 from Mdm2-mediated degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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.2012.02.049

Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

E3 ligases determine ubiquitination site and conjugate type by enforcing specificity on E2 enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Crystal Structures of Human MdmX (HdmX) in Complex with p53 Peptide Analogues Reveal Surprising Conformational Changes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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.2012.02.049

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.2012.02.049

MDM2 promotes ubiquitination and degradation of MDMX

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

DNA damage-induced MDMX degradation is mediated by MDM2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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.2012.02.049

Phosphorylation of Hdmx mediates its Hdm2- and ATM-dependent degradation in response to DNA damage

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Quantitative analyses reveal the importance of regulated Hdmx degradation for p53 activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

c-Abl phosphorylation of Mdm2 facilitates Mdm2-Mdmx complex formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Increased radioresistance and accelerated B cell lymphomas in mice with Mdmx mutations that prevent modifications by DNA-damage-activated kinases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

ATM activates p53 by regulating MDM2 oligomerization and E3 processivity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Divorcing ARF and p53: an unsettled case

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

MDMX regulation of p53 response to ribosomal stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Regulation of the MDM2-P53 pathway and tumor growth by PICT1 via nucleolar RPL11

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

A Critical Role for Noncoding 5S rRNA in Regulating Mdmx Stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

HDMX-L is expressed from a functional p53-responsive promoter in the first intron of the HDMX gene and participates in an autoregulatory feedback loop to control p53 activity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

p53 inactivation by MDM2 and MDMX negative feedback loops in testicular germ cell tumors

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Tumour suppression: disruption of HAUSP gene stabilizes p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Inactivation of HAUSP in vivo modulates p53 function

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The p53--Mdm2--HAUSP complex is involved in p53 stabilization by HAUSP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

MdmX is a substrate for the deubiquitinating enzyme USP2a

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

USP10 regulates p53 localization and stability by deubiquitinating p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Regulation of p53 stability and function by the deubiquitinating enzyme USP42

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Role of Pirh2 in mediating the regulation of p53 and c-Myc

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

The ubiquitin ligase COP1 is a critical negative regulator of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Inactivation of arf-bp1 induces p53 activation and diabetic phenotypes in mice

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

JFK, a Kelch domain-containing F-box protein, links the SCF complex to p53 regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

CRL4s: the CUL4-RING E3 ubiquitin ligases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Deletion of DDB1 in mouse brain and lens leads to p53-dependent elimination of proliferating cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

UBE4B promotes Hdm2-mediated degradation of the tumor suppressor p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

U box proteins as a new family of ubiquitin-protein ligases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Polyubiquitination of p53 by a ubiquitin ligase activity of p300.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Acetylation of p53 inhibits its ubiquitination by Mdm2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

Acetylation is indispensable for p53 activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2012.02.049

10.1016/J.FEBSLET.2012.02.049

21 January 2018

Identifiers

DOI

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27 August 2017

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