Pharmaceutical Sciences Faculty Publications

Document Type

Article

Publication Date

11-25-2015

Journal Title

J Mol Biochem

ISSN

2241-0090

Volume

4

First Page

95

Last Page

103

PubMed ID

27099843

PubMed CentralĀ® ID

PMC4834723

Abstract

Nucleophosmin (NPM) is a ubiquitously expressed phosphoprotein involved in many cellular processes. Phosphorylation is considered the major regulatory mechanism of the NPM protein, associated with diverse cellular events. In this study, we characterized the phosphorylation status of several physiological phosphorylation sites of NPM, especially the newly confirmed

Keywords

Cell cycle-dependent phosphorylation, nucleophosmin, peptidyl-prolyl cis/trans isomerase

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