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

Beyer Léon | Zendy; Günther René | Zendy; Koch Jan Christoph | Zendy; Klebe Stephan | Zendy; Hagenacker Tim | Zendy; Lingor Paul | Zendy; Biesalski AnneSophie | Zendy; Hermann Andreas | Zendy; Nabers Andreas | Zendy; Gold Ralf | Zendy; Tönges Lars | Zendy; Gerwert Klaus | Zendy

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

Author(s) -

Beyer Léon,

Günther René,

Koch Jan Christoph,

Klebe Stephan,

Hagenacker Tim,

Lingor Paul,

Biesalski AnneSophie,

Hermann Andreas,

Nabers Andreas,

Gold Ralf,

Tönges Lars,

Gerwert Klaus

Publication year - 2021

Publication title -

annals of clinical and translational neurology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.824

H-Index - 42

ISSN - 2328-9503

DOI - 10.1002/acn3.51256

Subject(s) - amyotrophic lateral sclerosis , medicine , biomarker , transactivation , cerebrospinal fluid , pathology , oncology , disease , gene , gene expression , biochemistry , biology

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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