Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.

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作者： Miguel,Mompeán ^[1] ; Valentina,Romano ^[2] ; David,Pantoja-Uceda ^[1] ; Cristiana,Stuani ^[2] ; Francisco E,Baralle ^[2] ; Emanuele,Buratti ^[3] ; Douglas V,Laurents ^[4]

作者单位： Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Serrano 119, E-28006 Madrid, Spain. ^[1] International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, I-34149 Trieste, Italy. ^[2] International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, I-34149 Trieste, Italy. Electronic address: buratti@icgeb.org. ^[3] Instituto de Química Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Serrano 119, E-28006 Madrid, Spain. Electronic address: dlaurents@iqfr.csic.es. ^[4]

关键词 amyotrophic lateral sclerosis (ALS) (Lou Gehrig disease)microscopic imaging nuclear magnetic resonance (NMR)protein aggregation site-directed mutagenesis structure–function subcellular fractionation