Structural evidence of amyloid fibril formation in the putative aggregation domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran… - The journal of …, 2015 - ACS Publications
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341–366 can recruit …
被引用次数：82 相关文章
[HTML] nih.gov

[HTML][HTML] Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran… - The journal of …, 2015 - ncbi.nlm.nih.gov
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341–366 can recruit …

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran, C Guarnaccia… - 2015 - digital.csic.es
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341-366 can recruit …

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.

M Mompeán, R Hervás, Y Xu, TH Tran… - The Journal of …, 2015 - europepmc.org
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341–366 can recruit …

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran… - Journal of Physical …, 2015 - hero.epa.gov
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341-366 can recruit …

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran… - Journal of Physical …, 2015 - hub.hku.hk
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341-366 can recruit …
[PDF] imdeananociencia.org

[PDF][PDF] Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran… - 2015 - repositorio.imdeananociencia.org
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341− 366 can recruit …

Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu… - The journal of …, 2015 - pubmed.ncbi.nlm.nih.gov
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341-366 can recruit …
[PDF] imdeananociencia.org

[PDF][PDF] Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu… - J. Phys …, 2015 - repositorio.imdeananociencia.org
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341− 366 can recruit …

[引用][C] Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran, C Guarnaccia… - 2015