Post-translational modifications of PML: Consequences and implications

N/ACitations
Citations of this article
68Readers
Mendeley users who have this article in their library.

Abstract

The tumor suppressor promyelocytic leukemia protein (PML) predominantly resides in a structurally distinct sub-nuclear domain called PML nuclear bodies. Emerging evidences indicated that PML actively participates in many aspects of cellular processes, but the molecular mechanisms underlying PML regulation in response to stress and environmental cues are not complete. Post-translational modifications, such as SUMOylation, phosphorylation, acetylation, and ubiquitination of PML add a complex layer of regulation to the physiological function of PML. In this review, we discuss the fast-moving horizon of post-translational modifications targeting PML.© 2013 Cheng and Kao.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Cite

CITATION STYLE

APA

Cheng, X., & Kao, H. Y. (2013). Post-translational modifications of PML: Consequences and implications. Frontiers in Oncology. https://doi.org/10.3389/fonc.2012.00210

Readers' Seniority

Tooltip

PhD / Post grad / Masters / Doc 30

70%

Researcher 8

19%

Professor / Associate Prof. 3

7%

Lecturer / Post doc 2

5%

Readers' Discipline

Tooltip

Agricultural and Biological Sciences 22

48%

Biochemistry, Genetics and Molecular Bi... 19

41%

Medicine and Dentistry 3

7%

Chemistry 2

4%

Save time finding and organizing research with Mendeley

Sign up for free