PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53
出版年份 2012 全文链接
标题
PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53
作者
关键词
-
出版物
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 19, Issue 9, Pages 916-924
出版商
Springer Nature
发表日期
2012-08-06
DOI
10.1038/nsmb.2353
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Identification of Akt Interaction Protein PHF20/TZP That Transcriptionally Regulates p53
- (2012) Sungman Park et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Loss of the Methyl Lysine Effector Protein PHF20 Impacts the Expression of Genes Regulated by the Lysine Acetyltransferase MOF
- (2011) Aimee I. Badeaux et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Combinatorial Readout of Dual Histone Modifications by Paired Chromatin-associated Modules
- (2011) Zhanxin Wang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins
- (2011) Konstantinos Tripsianes et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Regulation of p53 function by lysine methylation
- (2011) Lisandra E West et al. Epigenomics
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Cellular structural biology
- (2010) Yutaka Ito et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain
- (2010) Siddhartha Roy et al. JOURNAL OF MOLECULAR BIOLOGY
- Simultaneous Detection of Protein Phosphorylation and Acetylation by High-Resolution NMR Spectroscopy
- (2010) Stamatios Liokatis et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- The C terminus of p53 binds the N-terminal domain of MDM2
- (2010) Masha V Poyurovsky et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2
- (2010) Melanie A. Adams-Cioaba et al. PLoS One
- Transcriptional Regulation by P53
- (2010) R. Beckerman et al. Cold Spring Harbor Perspectives in Biology
- Preparation of Recombinant Peptides with Site- and Degree-Specific Lysine13C-Methylation
- (2009) Gaofeng Cui et al. BIOCHEMISTRY
- Blinded by the Light: The Growing Complexity of p53
- (2009) Karen H. Vousden et al. CELL
- Subunit Composition and Substrate Specificity of a MOF-containing Histone Acetyltransferase Distinct from the Male-specific Lethal (MSL) Complex
- (2009) Yong Cai et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Two Mammalian MOF Complexes Regulate Transcription Activation by Distinct Mechanisms
- (2009) Xiangzhi Li et al. MOLECULAR CELL
- Protein structure prediction on the Web: a case study using the Phyre server
- (2009) Lawrence A Kelley et al. Nature Protocols
- Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
- (2009) John R Horton et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Posttranslational Modification of p53: Cooperative Integrators of Function
- (2009) D. W. Meek et al. Cold Spring Harbor Perspectives in Biology
- Role for 53BP1 Tudor Domain Recognition of p53 Dimethylated at Lysine 382 in DNA Damage Signaling
- (2008) Ioulia Kachirskaia et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- In situ observation of protein phosphorylation by high-resolution NMR spectroscopy
- (2008) Philipp Selenko et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Increased Seroreactivity to Glioma-Expressed Antigen 2 in Brain Tumor Patients under Radiation
- (2008) Sabrina M. Heisel et al. PLoS One
- Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S
- (2008) Chao Xu et al. STRUCTURE
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started