A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing-Reference-Cited by-同舟云学术

A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing

Published:2018-02-09 Issue:5 Volume:37 Page:
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:EMBO J

Author:

Wang Ailin¹,Conicella Alexander E²,Schmidt Hermann Broder³,Martin Erik W⁴,Rhoads Shannon N⁵,Reeb Ashley N⁶,Nourse Amanda⁴,Ramirez Montero Daniel¹,Ryan Veronica H⁷,Rohatgi Rajat³⁸,Shewmaker Frank⁵,Naik Mandar T¹,Mittag Tanja⁴^ORCID,Ayala Yuna M⁶,Fawzi Nicolas L¹²^ORCID

Affiliation:

1. Department of Molecular Pharmacology, Physiology, and Biotechnology Brown University Providence RI USA

2. Graduate Program in Molecular Biology, Cell Biology and Biochemistry Brown University Providence RI USA

3. Department of Biochemistry Stanford University School of Medicine Stanford CA USA

4. Department of Structural Biology St. Jude Children's Research Hospital Memphis TN USA

5. Department of Pharmacology and Molecular Therapeutics Uniformed Services University Bethesda MD USA

6. Edward Doisy Department of Biochemistry and Molecular Biology Saint Louis University School of Medicine St. Louis MO USA

7. Neuroscience Graduate Program Brown University Providence RI USA

8. Department of Medicine Stanford University School of Medicine Stanford CA USA

Funder

National Institute of Mental Health

National Center for Research Resources

National Institute of General Medical Sciences

National Science Foundation

Amyotrophic Lateral Sclerosis Association

Judith and Jean Pape Adams Charitable Foundation

Deutsche Forschungsgemeinschaft

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.201797452

Reference83 articles.

1. Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

2. Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations

3. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

4. ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43

5. pH-dependent self-association of zinc-free insulin characterized by concentration-gradient static light scattering

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