4.6 Article

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

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WILEY
DOI: 10.1002/acn3.51256

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  1. Protein Research Unit within Europe (PURE)
  2. Center for Protein Diagnostics (ProDi)
  3. niemALS aufgeben e. V
  4. Hermann und Lilly SchillingStiftung fur medizinische Forschung im Stifterverband

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The study shows that measuring the misfolding of TDP-43 in the cerebrospinal fluid of ALS patients using immuno-infrared sensor technology has the potential to serve as a biomarker for ALS. The technology can accurately distinguish ALS patients from other control groups.
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.

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