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

作者单位： CSIC, Inst Quim Fis Rocasolano, Serrano 119, E-28006 Madrid, Spain ^[1] ICGEB, Padriciano 99, I-34149 Trieste, Italy ^[2]

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

发布时间 2019-09-19

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The Journal of biological chemistry

2017年292卷28期

11992-12006页

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

The Journal of biological chemistry

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The Journal of biological chemistry

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

The Journal of biological chemistry

相似文献

The Journal of biological chemistry

相关期刊

检索历史清除