Work

Prolyl isomerase PIN1 regulates the stability, transcriptional activity and oncogenic potential of BRD4

Year: 2017

Type: article

Source: Oncogene

DOI: 10.1038/onc.2017.137

Authors: X Hu, S-H Dong, J Chen, X Z Zhou, R Chen, S Nair, K P Lu, L-F Chen

Institutions: University of Illinois Urbana-Champaign, Beth Israel Deaconess Medical Center, Harvard University, Xiamen University, Fujian Medical University

Language: English

Topic: Signaling Pathways in Disease

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Natural Science Foundation of China, National Institutes of Health, University of Illinois at Urbana-Champaign, National Cancer Institute, National Institute of Allergy and Infectious Diseases, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: Function and Regulation of the Phosphorylation-Specific Prolyl Isomerase Pin1, G5537519703, Antimicrobial activity of pH-activated polypeptides toward H. pylori, NF-kB Signaling and H. Pylori-induced Gastric Disease, Transcriptional regulation of H. pylori-mediated gastric inflammation and cancer, G9000291756, G9000294327

OpenAlex ID: W2612805392

FWCI: 1.9

Cites: 57

Cited by: 42

Related to: 10