نتایج جستجو برای: n 43

تعداد نتایج: 1053784  

Journal: :Brain Research 2016
Hiroki Sasaguri Jeannie Chew Ya-Fei Xu Tania F. Gendron Aliesha Garrett Chris W. Lee Karen Jansen-West Peter O. Bauer Emilie A. Perkerson Jimei Tong Caroline Stetler Yong-Jie Zhang

Inclusions of Tar DNA- binding protein 43 (TDP-43) are a pathological hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43-positive inclusions (FTLD-TDP). Pathological TDP-43 exhibits the disease-specific biochemical signatures, which include its ubiquitination, phosphorylation and truncation. Recently, we demonstrated that the extreme N-terminus of ...

Journal: :Lan Harremanak - Revista de Relaciones Laborales 2020

Journal: :Journal of neuropathology and experimental neurology 2008
Kimmo J Hatanpaa Eileen H Bigio Nigel J Cairns Kyle B Womack Sandra Weintraub John C Morris Chan Foong Guanghua Xiao Christa Hladik Tina Y Mantanona Charles L White

TAR DNA-binding protein 43 (TDP-43) is a major component of the inclusions in frontotemporal lobar degeneration with ubiquitinated inclusions (FTLD-U). We studied TDP-43 pathology in the hippocampus and frontal cortex of autopsy brains from patients with FTLD-U (n = 68), dementia lacking distinctive histopathology (n = 4), other neurodegenerative diseases (n = 23), and controls (n = 12) using a...

2013
Yong-Jie Zhang Thomas Caulfield Ya-Fei Xu Tania F. Gendron Jaime Hubbard Caroline Stetler Hiroki Sasaguri Ena C. Whitelaw Shuyi Cai Wing Cheung Lee Leonard Petrucelli

TAR DNA-binding protein-43 (TDP-43) is the principal component of ubiquitinated inclusions in amyotrophic lateral sclerosis (ALS) and the most common pathological subtype of frontotemporal dementia-frontotemporal lobar degeneration with TDP-43-positive inclusions (FTLD-TDP). To date, the C-terminus of TDP-43, which is aggregation-prone and contains almost all ALS-associated mutations, has garne...

Journal: :The Journal of biological chemistry 1998
T Toyofuku M Yabuki K Otsu T Kuzuya M Hori M Tada

The gap junction protein connexin-43 is normally located at the intercalated discs of cardiac myocytes, and it plays a critical role in the synchronization of their contraction. The mechanism by which connexin-43 is localized within cardiac myocytes is unknown. However, localization of connexin-43 likely involves an interaction with the cytoskeleton; immunofluorescence microscopy showed that in...

Journal: :The Journal of biological chemistry 2010
Rodrigo A Fuentealba Maria Udan Shaughn Bell Iga Wegorzewska Jieya Shao Marc I Diamond Conrad C Weihl Robert H Baloh

The identification of pathologic TDP-43 aggregates in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration, followed by the discovery of dominantly inherited point mutations in TDP-43 in familial ALS, have been critical insights into the mechanism of these untreatable neurodegenerative diseases. However, the biochemical basis of TDP-43 aggregation and the mechanism of how m...

Journal: :Plastic and Reconstructive Surgery - Global Open 2020

Journal: :Cidades comunidades e territórios 2021

Journal: :Journal of neuropathology and experimental neurology 2011
Cyntia Tremblay Isabelle St-Amour Julie Schneider David A Bennett Frédéric Calon

Transactive response DNA binding protein 43 (TDP-43) plays a central role in the neuropathology of frontotemporal lobar degeneration and amyotrophic lateral sclerosis, but the relationship between TDP-43 abnormalities and Alzheimer disease (AD) remains unclear. To determine whether TDP-43 can serve as a neuropathologic marker of AD, we performed biochemical characterization and quantification o...

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