β1,6 GlcNAc branches-modified protein tyrosine phosphatase alpha enhances its stability and promotes focal adhesion formation in MCF-7 cells-Reference-Cited by-同舟云学术

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β1,6 GlcNAc branches-modified protein tyrosine phosphatase alpha enhances its stability and promotes focal adhesion formation in MCF-7 cells

Published:2017-01 Issue:4 Volume:482 Page:1455-1461
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Xiao Jin,Gao Yan,Yang Fuming,Wang Can,Xu Yaolin,Chang Ruiqi,Zha Xiliang,Wang Liying

Funder

National Natural Science Foundation of China

National Key Research and Development Program of China

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference24 articles.

1. Targeting protein tyrosine phosphatases for anticancer drug discovery;Scott;Curr. Pharm. Des.,2010

2. Expression of protein tyrosine phosphatase alpha (RPTPalpha) in human breast cancer correlates with low tumor grade, and inhibits tumor cell growth in vitro and in vivo;Ardini;Oncogene,2000

3. Tyrosine phosphatase PTPα contributes to HER2-evoked breast tumor initiation and maintenance;Meyer;Oncogene,2014

4. Protein-tyrosine phosphatase a regulates Src family kinases and alters cell-substratum adhesion;Harder;J. Biol. Chem.,1999

5. Protein tyrosine phosphatase alpha (PTPalpha): a Src family kinase activator and mediator of multiple biological effects;Pallen;Curr. Top. Med. Chem.,2003

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4. PTPRA facilitates cancer growth and migration via the TNF‑α‑mediated PTPRA‑NF‑κB pathway in MCF‑7 breast cancer cells;Oncology Letters;2020-08-20

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