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TDP‐43 as structure‐based biomarker in amyotrophic lateral sclerosis

Pathologic alterations of Transactivation response DNA‐binding protein 43 kilo Dalton (TDP‐43) are a major hallmark of amyotrophic lateral sclerosis (ALS). In this pilot study, we analyzed the secondary structure distribution of TDP‐43 in cerebrospinal fluid of ALS patients (n = 36) compared to Park...

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Detalles Bibliográficos
Autores principales: Beyer, Léon, Günther, René, Koch, Jan Christoph, Klebe, Stephan, Hagenacker, Tim, Lingor, Paul, Biesalski, Anne‐Sophie, Hermann, Andreas, Nabers, Andreas, Gold, Ralf, Tönges, Lars, Gerwert, Klaus
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7818221/
https://www.ncbi.nlm.nih.gov/pubmed/33263951
http://dx.doi.org/10.1002/acn3.51256
Descripción
Sumario:Pathologic alterations of Transactivation response DNA‐binding protein 43 kilo Dalton (TDP‐43) are a major hallmark of amyotrophic lateral sclerosis (ALS). In this pilot study, we analyzed the secondary structure distribution of TDP‐43 in cerebrospinal fluid of ALS patients (n = 36) compared to Parkinson´s disease patients (PD; n = 30) and further controls (Ctrl; n = 24) using the immuno‐infrared sensor technology. ALS patients could be discriminated from PD and Ctrl with a sensitivity/specificity of 89 %/77 % and 89 %/83 %, respectively. Our findings demonstrate that TDP‐43 misfolding measured by the immuno‐infrared sensor technology has the potential to serve as a biomarker candidate for ALS.