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[HTML][HTML] Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

T Afroz, EM Hock, P Ernst, C Foglieni… - Nature …, 2017 - nature.com
TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal phosphorylation and
cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral …
被引用次数：278 相关文章

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.

T Afroz, EM Hock, P Ernst, C Foglieni… - Nature …, 2017 - folia.unifr.ch
English TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal
phosphorylation and cytoplasmic aggregation characterizes affected neurons in patients …
[PDF] uzh.ch

[PDF][PDF] Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

T Afroz, EM Hock, P Ernst, C Foglieni, M Jambeau… - dqbm.uzh.ch
Results TDP-43 forms physiological oligomers in human tissues. In order to capture the in
vivo protein state, we systematically analyzed physiological TDP-43 in cells and tissues by …

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

T Afroz, EM Hock, P Ernst, C Foglieni… - Nature …, 2017 - ideas.repec.org
TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal phosphorylation and
cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral …

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.

T Afroz, EM Hock, P Ernst, C Foglieni, M Jambeau… - Nature …, 2017 - sonar.ch
English TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal
phosphorylation and cytoplasmic aggregation characterizes affected neurons in patients …

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.

T Afroz, EM Hock, P Ernst, C Foglieni… - Nature …, 2017 - europepmc.org
TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal phosphorylation and
cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral …

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

T Afroz, EM Hock, P Ernst, C Foglieni… - Nature …, 2017 - pubmed.ncbi.nlm.nih.gov
TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal phosphorylation and
cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral …
[PDF] uzh.ch

[PDF][PDF] Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

T Afroz, EM Hock, P Ernst, C Foglieni, M Jambeau… - imls.uzh.ch
Results TDP-43 forms physiological oligomers in human tissues. In order to capture the in
vivo protein state, we systematically analyzed physiological TDP-43 in cells and tissues by …

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

T Afroz, EM Hock, P Ernst, C Foglieni… - Nature …, 2017 - ui.adsabs.harvard.edu
TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal phosphorylation and
cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral …
[PDF] engineerbiology.org

[PDF][PDF] Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

T Afroz, EM Hock, P Ernst, C Foglieni, M Jambeau… - engineerbiology.org
Results TDP-43 forms physiological oligomers in human tissues. In order to capture the in
vivo protein state, we systematically analyzed physiological TDP-43 in cells and tissues by …