Work

Acetylation-regulated interaction between p53 and SET reveals a widespread regulatory mode

Year: 2016

Type: article

Source: Nature

DOI: 10.1038/nature19759

Authors: Donglai Wang, Ning Kon, Gorka Lasso, Le Jiang, Wenchuan Leng, Wei-Guo Zhu, Jun Qin, Barry Honig, Wei Gu

Institutions: Herbert Irving Comprehensive Cancer Center, Columbia University, Howard Hughes Medical Institute, State Key Laboratory of Proteomics, Shenzhen University, Baylor College of Medicine, Alkek Center for Molecular Discovery

Language: English

Topic: Cancer-related Molecular Pathways

Subfield: Oncology

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences

Awards: National Center: Multiscale Analysis of Genomic and Cellular Networks (MAGNet), G1370126020, Regulation of SLC7A11 by p53 in cancer metabolism, Storage System for High Performance Computing, High-performance compute cluster for biomedical computing, Computer Studies of Protein Structure and Function, COMPUTER STUDIES OF PROTEIN STRUCTURE AND FUNCTION, HAUSP inhibitors in p53-wild type and p53-mutant tumors, Regulation of p53 acetylation and deacetylation in tumorigenesis., p53 - Regulators and Effectors

OpenAlex ID: W2518890317

FWCI: 8.979

Cites: 30

Cited by: 195

Related to: 10