The Structure and Interactions of the Proline-rich Domain of ASPP2-Reference-Cited by-同舟云学术

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The Structure and Interactions of the Proline-rich Domain of ASPP2

Published:2008-07 Issue:27 Volume:283 Page:18990-18999
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Rotem Shahar,Katz Chen,Benyamini Hadar,Lebendiker Mario,Veprintsev Dmitry,Rüdiger Stefan,Danieli Tsafi,Friedler Assaf

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference58 articles.

1. ASPP Proteins Specifically Stimulate the Apoptotic Function of p53

2. Two cellular proteins that bind to wild-type but not mutant p53.

3. The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M

4. Solution Structure of ASPP2 N-terminal Domain (N-ASPP2) Reveals a Ubiquitin-like Fold

5. Structure of the p53 Tumor Suppressor Bound to the Ankyrin and SH3 Domains of 53BP2

Cited by 40 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Arabidopsis thaliana ubiquitin-associated protein 2 (AtUAP2) functions as an E4 ubiquitin factor and negatively modulates dehydration stress response;Plant Molecular Biology;2024-02

2. ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection;Journal of General Virology;2023-09-26

3. Biophysical characterization of the DNA binding motif of human phospholipid scramblase 1;European Biophysics Journal;2022-10-19

4. TP53BP2: Roles in suppressing tumorigenesis and therapeutic opportunities;Genes & Diseases;2022-09

5. RDIVpSGP motif of ASPP2 binds to 14-3-3 and enhances ASPP2/k18/14-3-3 ternary complex formulation to promote BRAF/MEK/ERK signal inhibited cell proliferation in hepatocellular carcinoma;Cancer Gene Therapy;2022-05-03

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