C-terminal truncation of GSK-3β enhances its dephosphorylation by PP2A-Reference-Cited by-同舟云学术

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C-terminal truncation of GSK-3β enhances its dephosphorylation by PP2A

Published:2017-03-23 Issue:7 Volume:591 Page:1053-1063
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Jin Nana¹,Wu Yue¹,Xu Wen¹²,Gong Cheng-Xin¹²,Iqbal Khalid²,Liu Fei¹²

Affiliation:

1. Key laboratory of neuroregeneration of Jiangsu and Ministry of Education; Co-innovation Center of Regeneration; Nantong University; China

2. Department of Neurochemistry; New York State Institute for Basic Research in Developmental Disabilities; Staten Island NY USA

Funder

Nantong University

New York State Office of People with Developmental Disabilities (OPWDD)

Alzheimer's Association

National Natural Science Foundation of China

Natural Science Research Program of Nantong University

Priority Academic Program Development of Jiangsu Higher Education institutions

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/1873-3468.12617/fullpdf

Reference45 articles.

1. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments;Grundke-Iqbal;J Biol Chem,1986

2. A68: a major subunit of paired helical filaments and derivatized forms of normal tau;Lee;Science,1991

3. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology;Grundke-Iqbal;Proc Natl Acad Sci USA,1986

4. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules;Alonso;Nat Med,1996

5. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease;Alonso;Proc Natl Acad Sci USA,1994

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