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

By T. Arai, M. Hasegawa, H. Akiyama, K. Ikeda, T. Nonaka, H. Mori, D. Mann, K. Tsuchiya, Mari Yoshida, Y. Hashizume and 1 more. Biochemical and Biophysical Research Communications - BBRC, 2006

2,657 citations recorded by the source corpus.

Subfields: Genetics, Neurology

View Paper: https://www.semanticscholar.org/paper/a89a8b785f3c8525d0fc266991ee801e7ab43987

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Genetics

In Neurology

Citations in the corpus

Phosphorylated TDP-43 in frontotemporal lobar degeneration and ALS (2008, methodology): “In addition, and again in analogy with tauopathies, these antibodies may be useful for detecting abnormal TDP-43 in biological fluids such as cerebrospinal fluid.33 The results suggest that CK1 is involved in the abnormal phosphorylation and accumulation of TDP-43.”
Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration (2007, methodology): “mosome 9p [4, 5, 20, 55, 56, 57, 68, 75, 77], and the novel (TDP-43) proteinopathy, which is present in most cases of FTLD-U with or without MND [3, 16, 21, 61].”
Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity (2009, background): “Recently, TAR DNA-binding protein of 43-kDa molecular mass (TDP-43) was identified as the major component of the predominately cytoplasmic inclusions observed in ALS and FTLD with ubiquitin-positive inclusions (FTLD-U), the most common form of FTLD (1, 2).”
Oxidative stress in ALS: key role in motor neuron injury and therapeutic target. (2010, background): “One of the major protein constituents of ubiquitinated inclusions in ALS is TDP-43 [142] [143].”
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration (2011, background): “TDP43 truncation As described above, the biochemical signature of FTLD-TDP includes the presence of truncated TDP43 protein, evident as 20–25-kDa species in sarkosyl-insoluble brain lysate”
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease (2012, background): “TDP-43: the first of many? TDP-43 was the first RNA-binding protein with a prion-like domain (amino acids 277-414, Figure 2) to emerge in connection with neurodegenerative disease (Arai et al., 2006; Neumann et al., 2006).”
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis (2019, background): “Post-translational Modifications The two most pathologically significant common posttranslational modifications (PTMs) in TDP-43 are phosphorylation and ubiquitination (Arai et al., 2006; Neumann et al., 2006, 2009; Hasegawa et al., 2008; Inukai et al., 2008).”
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. (2010, background): “A major shift in our understanding of ALS pathogenesis started in 2006 (6,7) with the identification of the 43 kDa transactive response (TAR) DNA-binding protein (TDP-43) as the main component of ubiquitinated protein aggregates found in sporadic ALS patients and in patients with frontotemporal loba”
Rethinking ALS: the FUS about TDP-43. (2009, background): “This seismic shift in our understanding of ALS pathogenesis began with the identification (Arai et al., 2006; Neumann et al., 2006) of the 43 kDa TAR DNA-binding protein (TDP-43) as a major component of ubiquitinated protein aggregates found in many patients with sporadic ALS or the most common…”