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1
Solution structure of the C4 zinc finger domain of HDM2.
Protein Sci. 2006 Feb;15(2):384-9. doi: 10.1110/ps.051927306. Epub 2005 Dec 29.
2
Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53.
J Mol Biol. 2006 Oct 20;363(2):433-50. doi: 10.1016/j.jmb.2006.08.027. Epub 2006 Aug 14.
3
Metal and RNA binding properties of the hdm2 RING finger domain.
Biochemistry. 1998 Dec 1;37(48):7005-15. doi: 10.1021/bi980596r.
4
The central region of HDM2 provides a second binding site for p53.
Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1227-32. doi: 10.1073/pnas.0510343103. Epub 2006 Jan 23.
5
Identification of a Catalytic Active but Non-Aggregating MDM2 RING Domain Variant.
J Mol Biol. 2021 Mar 5;433(5):166807. doi: 10.1016/j.jmb.2021.166807. Epub 2021 Jan 13.
6
Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold.
J Mol Biol. 2007 May 25;369(1):1-10. doi: 10.1016/j.jmb.2007.03.017. Epub 2007 Mar 15.
7
Interferon-inducible protein IFIXalpha1 functions as a negative regulator of HDM2.
Mol Cell Biol. 2006 Mar;26(5):1979-96. doi: 10.1128/MCB.26.5.1979-1996.2006.
9
Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans.
Cell Death Differ. 2008 May;15(5):841-8. doi: 10.1038/sj.cdd.4402309. Epub 2008 Jan 25.
10
Intrinsically unstructured domains of Arf and Hdm2 form bimolecular oligomeric structures in vitro and in vivo.
J Mol Biol. 2008 Dec 5;384(1):240-54. doi: 10.1016/j.jmb.2008.09.019. Epub 2008 Sep 16.

引用本文的文献

1
Redox properties of CysHis and Cys zinc fingers determined by electrospray ionization mass spectrometry.
FEBS Open Bio. 2018 Apr 25;8(6):923-931. doi: 10.1002/2211-5463.12422. eCollection 2018 Jun.
3
Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activation.
Genes Dev. 2015 Jul 15;29(14):1524-34. doi: 10.1101/gad.261792.115.
4
Autoactivation of the MDM2 E3 ligase by intramolecular interaction.
Mol Cell Biol. 2014 Aug;34(15):2800-10. doi: 10.1128/MCB.00246-14. Epub 2014 May 19.
5
MDMX contains an autoinhibitory sequence element.
Proc Natl Acad Sci U S A. 2013 Oct 29;110(44):17814-9. doi: 10.1073/pnas.1317398110. Epub 2013 Oct 14.
6
In vitro selection of mutant HDM2 resistant to Nutlin inhibition.
PLoS One. 2013 Apr 30;8(4):e62564. doi: 10.1371/journal.pone.0062564. Print 2013.
7
Splicing up mdm2 for cancer proteome diversity.
Genes Cancer. 2012 Mar;3(3-4):311-9. doi: 10.1177/1947601912455323.
8
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The general definition of the p97/valosin-containing protein (VCP)-interacting motif (VIM) delineates a new family of p97 cofactors.
J Biol Chem. 2011 Nov 4;286(44):38670-38678. doi: 10.1074/jbc.M111.274472. Epub 2011 Sep 6.
10
The evolution of MDM2 family genes.
Gene. 2011 Oct 15;486(1-2):23-30. doi: 10.1016/j.gene.2011.06.030. Epub 2011 Jul 4.

本文引用的文献

1
MDM2 is a central node in the p53 pathway: 12 years and counting.
Curr Cancer Drug Targets. 2005 Feb;5(1):3-8. doi: 10.2174/1568009053332627.
2
Ubiquitin interactions of NZF zinc fingers.
EMBO J. 2004 Apr 7;23(7):1411-21. doi: 10.1038/sj.emboj.7600114. Epub 2004 Mar 18.
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p53-independent functions of MDM2.
Mol Cancer Res. 2003 Dec;1(14):1027-35.
4
In vivo activation of the p53 pathway by small-molecule antagonists of MDM2.
Science. 2004 Feb 6;303(5659):844-8. doi: 10.1126/science.1092472. Epub 2004 Jan 2.
5
Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4.
J Biol Chem. 2003 May 30;278(22):20225-34. doi: 10.1074/jbc.M300459200. Epub 2003 Mar 18.
6
Structural classification of zinc fingers: survey and summary.
Nucleic Acids Res. 2003 Jan 15;31(2):532-50. doi: 10.1093/nar/gkg161.
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The PROSITE database, its status in 2002.
Nucleic Acids Res. 2002 Jan 1;30(1):235-8. doi: 10.1093/nar/30.1.235.
10

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