Generation and characterization of novel conformation-specific monoclonal antibodies for α-synuclein pathology-Reference-Cited by-同舟云学术

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Generation and characterization of novel conformation-specific monoclonal antibodies for α-synuclein pathology

Published:2015-07 Issue: Volume:79 Page:81-99
ISSN:0969-9961
Container-title:Neurobiology of Disease
language:en
Short-container-title:Neurobiology of Disease

Author:

Vaikath Nishant N.,Majbour Nour K.,Paleologou Katerina E.,Ardah Mustafa T.,van Dam Esther,van de Berg Wilma D.J.,Forrest Shelley L.,Parkkinen Laura,Gai Wei-Ping,Hattori Nobutaka,Takanashi Masashi,Lee Seung-Jae,Mann David M.A.,Imai Yuzuru,Halliday Glenda M.,Li Jia-Yi.,El-Agnaf Omar M.A.

Funder

UAE University

National Health and Medical Research Council

Neuroscience Research Australia

Alzheimer Brian Bank UK

Stichting Parkinson Fonds (SPF; The Netherlands)

Neuroscience Campus Amsterdam

Alzheimer’s Research UK

Alzheimer’s Society

Netherlands Brain Bank (Amsterdam, the Netherlands)

neuropathologist, VUmc

(Jutendo University Graduate School of Medicine, Japan

National Hospital Organization, Sagamihara National Hospital, Japan

Publisher

Elsevier BV

Subject

Neurology

Reference70 articles.

1. Elevated levels of cerebrospinal fluid alpha-synuclein oligomers in healthy asymptomatic LRRK2 mutation carriers;Aasly;Front. Aging Neurosci.,2014

2. Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease;Anderson;J. Biol. Chem.,2006

3. Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease;Appel-Cresswell;Mov. Disord.,2013

4. Structure activity relationship of phenolic acid inhibitors of alpha-synuclein fibril formation and toxicity;Ardah;Front. Aging Neurosci.,2014

5. Ginsenoside Rb1 inhibits fibrillation and toxicity of alpha-synuclein and disaggregates preformed fibrils;Ardah;Neurobiol. Dis.,2015

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