Dysregulation of protein phosphatase 2A in parkinson disease and dementia with lewy bodies-Reference-Cited by-同舟云学术

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Dysregulation of protein phosphatase 2A in parkinson disease and dementia with lewy bodies

Published:2016-09-07 Issue:10 Volume:3 Page:769-780
ISSN:2328-9503
Container-title:Annals of Clinical and Translational Neurology
language:en
Short-container-title:Ann Clin Transl Neurol

Author:

Park Hye‐Jin¹,Lee Kang‐Woo¹,Park Eun S.¹,Oh Stephanie¹,Yan Run¹,Zhang Jie¹,Beach Thomas G.²,Adler Charles H.³,Voronkov Michael⁴,Braithwaite Steven P.⁴,Stock Jeffry B.⁴⁵,Mouradian M. Maral¹

Affiliation:

1. Center for Neurodegenerative and Neuroimmunologic Diseases Department of Neurology Rutgers – Robert Wood Johnson Medical School Piscataway New Jersey 08854

2. Banner Sun Health Research Institute Sun City Arizona 85372

3. Mayo Clinic Scottsdale Arizona 85259

4. Signum Biosciences 133 Wall Street Princeton New Jersey 08540

5. Department of Molecular Biology Princeton University Princeton New Jersey 08544

Funder

Michael J. Fox Foundation for Parkinson's Research

American Parkinson Disease Association

National Institutes of Health

National Institute of Neurological Disorders and Stroke

National Institute on Aging

Arizona Department of Health Services

Arizona Biomedical Research Commission

Publisher

Wiley

Subject

Neurology (clinical),General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/acn3.337

Reference64 articles.

1. Protein serine/threonine phosphatase 1 and 2A associate with and dephosphorylate neurofilaments

2. Brain protein phosphatase 2A: Developmental regulation and distinct cellular and subcellular localization by B subunits

3. Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Bα subunit

4. Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits

5. Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo

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