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Hans F.,University of Tubingen | Hans F.,German Center for Neurodegenerative Diseases | Hans F.,Laboratory of Functional Neurogenetics | Fiesel F.C.,Laboratory of Functional Neurogenetics | And 12 more authors.
Journal of Biological Chemistry | Year: 2014

Background: Ubiquitin-modified TDP-43 protein aggregates characterize common neurodegenerative diseases. Results: UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y (UBPY) are functional interactors of TDP-43 in cell culture and fly models. Conclusion: Specific regulators of TDP-43 ubiquitination influence its aggregation and neurotoxic properties. Significance: UBE2E and UBPY enzymes may modulate the course of TDP-43 diseases. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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