The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases-Reference-Cited by-同舟云学术

The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases

Published:2017-06-12 Issue:1 Volume:23 Page:1-12
ISSN:1355-8145
Container-title:Cell Stress and Chaperones
language:en
Short-container-title:Cell Stress and Chaperones

Author:

Cristofani Riccardo,Crippa Valeria,Vezzoli Giulia,Rusmini Paola,Galbiati Mariarita,Cicardi Maria Elena,Meroni Marco,Ferrari Veronica,Tedesco Barbara,Piccolella Margherita,Messi Elio,Carra Serena,Poletti Angelo^ORCID

Funder

Fondazione Telethon

Fondazione Cariplo

Fondazione Arisla

Fondazione AriSLA

Association Française contre les Myopathies

Regione Lombardia

Università degli studi di Milano

Ministero della Salute

Joint Programme on Neurodegenerative Diseases

Joint Programme Neurodegenerative Disease

Fondazione regionale per la ricerca biomedica (FRRB), Regione Lombardia

MIUR Rita Levi Montalcini

Ministero dell’Istruzione, dell’Università e della Ricerca

European Molecular Biology Organization

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry

Link

http://link.springer.com/article/10.1007/s12192-017-0806-9/fulltext.html

Reference60 articles.

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3. Ash PE, Bieniek KF, Gendron TF, Caulfield T, Lin WL, Dejesus-Hernandez M, van Blitterswijk MM, Jansen-West K et al (2013) Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS. Neuron 77:639–646. doi: 10.1016/j.neuron.2013.02.004

4. Aulas A, Vande Velde C (2015) Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS? Front Cell Neurosci 9:423. doi: 10.3389/fncel.2015.00423

5. Bruinsma IB, Bruggink KA, Kinast K, Versleijen AA, Segers-Nolten IM, Subramaniam V, Kuiperij HB, Boelens W et al (2011) Inhibition of alpha-synuclein aggregation by small heat shock proteins. Proteins 79:2956–2967. doi: 10.1002/prot.23152

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