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

@article{Mompen2017PointMI,
  title={Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.},
  author={Miguel Mompe{\'a}n and Valentina Romano and David Pantoja-Uceda and Cristiana Stuani and Francisco E. Baralle and Emanuele Buratti and Douglas V Laurents},
  journal={The Journal of biological chemistry},
  year={2017},
  volume={292 28},
  pages={
          11992-12006
        }
}
Transactive response DNA-binding protein 43 (TDP-43) performs multiple tasks in mRNA processing, transport, and translational regulation, but it also forms aggregates implicated in amyotrophic lateral sclerosis. TDP-43's N-terminal domain (NTD) is important for these activities and dysfunctions; however, there is an open debate about whether or not it adopts a specifically folded, stable structure. Here, we studied NTD mutations designed to destabilize its structure utilizing NMR and… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 1 time. VIEW TWEETS

References

Publications referenced by this paper.
Showing 1-10 of 59 references

TDP-43 Dimerizes in Human Cells in Culture

Cellular and Molecular Neurobiology • 2009
View 6 Excerpts
Highly Influenced

Inter-domain interactions of TDP-43 as decoded by NMR.

Biochemical and biophysical research communications • 2016
View 4 Excerpts
Highly Influenced

The dynamic genome of Hydra

View 4 Excerpts
Highly Influenced

Phase to Phase with TDP-43.

Biochemistry • 2017
View 2 Excerpts

Similar Papers

Loading similar papers…