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- W1593716627 abstract "TDP-43 nuclear protein is involved in several major neurodegenerative diseases that include frontotemporal lobar degeneration with ubiquitin (FTLD-U) bodies and amyotrophic lateral sclerosis (ALS). As a consequence, the role played by this protein in both normal and diseased cellular metabolism has come under very close scrutiny. In the neuronal tissues of affected individuals TDP-43 undergoes aberrant localization to the cytoplasm to form insoluble aggregates. Furthermore, it is subject to degradation, ubiquitination, and phosphorylation. Understanding the pathways that lead to these changes will be crucial to define the functional role played by this protein in disease. Several recent biochemical and molecular studies have provided new information regarding the potential physiological consequences of these modifications. Moreover, the discovery of TDP-43 mutations associated with disease in a limited number of cases and the data from existing animal models have strengthened the proposed links between this protein and disease. In this review we will discuss the available data regarding the biochemical and functional changes that transform the wild-type endogenous TDP-43 in its pathological form. Furthermore, we will concentrate on examining the potential pathological mechanisms mediated by TDP-43 in different gain- versus loss-of-function scenarios. In the near future, this knowledge will hopefully increase our knowledge on disease progression and development. Moreover, it will allow the design of innovative therapeutic strategies for these pathologies based on the specific molecular defects causing the disease." @default.
- W1593716627 created "2016-06-24" @default.
- W1593716627 creator A5029821144 @default.
- W1593716627 creator A5032436476 @default.
- W1593716627 date "2009-01-01" @default.
- W1593716627 modified "2023-10-18" @default.
- W1593716627 title "Chapter 1 The Molecular Links Between TDP‐43 Dysfunction and Neurodegeneration" @default.
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