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A novel Aurora-A-mediated phosphorylation of p53 inhibits its interaction with MDM2
Kai Wei Hsueh,
Shu Ling Fu
, Chirn Bin Chang, Yu Ling Chang,
Chao Hsiung Lin
*
*
此作品的通信作者
傳統醫藥研究所
生命科學系暨基因體科學研究所
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引文 斯高帕斯(Scopus)
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Keyphrases
Phosphorylation
100%
Aurora A
100%
Murine Double Minute 2 (MDM2)
100%
Co-immunoprecipitation (co-IP)
18%
Phosphorylation Sites
18%
Phosphopeptides
18%
Functional Consequences
18%
Protein Stability
9%
Mass Spectrometry
9%
Human Cancer
9%
Michael Addition
9%
Protein-protein Interaction
9%
Interacting Proteins
9%
Transactivation
9%
Reporter Assay
9%
Phosphorylated Protein
9%
Trypsin
9%
Phosphate
9%
Cancer Biology
9%
Western Blot Assay
9%
Whole Genome Amplification
9%
Phos-tag SDS-PAGE
9%
In Vitro Phosphorylation
9%
P53 Phosphorylation
9%
Alanine mutation
9%
Immobilized Metal Affinity Chromatography
9%
Biochemistry, Genetics and Molecular Biology
P53
100%
Immunoprecipitation
15%
Protein-Protein Interaction
15%
Phosphopeptide
15%
Genetics
7%
Protein Stability
7%
Mass Spectrometry
7%
Polyacrylamide Gel Electrophoresis
7%
Western Blot
7%
Transactivation
7%
Phosphoprotein
7%
Aurora A Kinase
7%
Michael Addition
7%
Serine
7%
Alanine
7%
Affinity Chromatography
7%
Pharmacology, Toxicology and Pharmaceutical Science
Protein P53
100%
Immunoprecipitation
15%
Phosphopeptide
15%
Malignant Neoplasm
7%
Western Blot
7%
Polyacrylamide Gel Electrophoresis
7%
Serine
7%
Elimination
7%
Alanine
7%
Phosphoprotein
7%
Aurora A Kinase
7%