Supplemental material
Cell Cycle
Volume 12, 2013 - Issue 19
Related Research Data
Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site.
Source:
Elsevier B.V.
Arginine methylation of FUS impairs TRN binding
Source:
Wiley
Regulated protein aggregation: stress granules and neurodegeneration
Source:
Springer Science and Business Media LLC
A new subtype of frontotemporal lobar degeneration with FUS pathology.
Source:
Oxford University Press
Understanding the role of TDP-43 and FUS/TLS in ALS and beyond
Source:
Elsevier BV
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
Source:
Oxford University Press (OUP)
RNA recognition motifs: boring? Not quite.
Source:
Elsevier BV
How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other?
Source:
Ovid Technologies (Wolters Kluwer Health)
ALS mutations in FUS cause neuronal dysfunction and death in Caenorhabditis elegans by a dominant gain-of-function mechanism
Source:
Apollo - University of Cambridge Repository
Aberrant Cleavage of TDP-43 Enhances Aggregation and Cellular Toxicity
Source:
Proceedings of the National Academy of Sciences
FUS(1-359) transgenic mice as a model of ALS: pathophysiological and molecular aspects of the proteinopathy.
Source:
(:unav)
Expression of human FUS protein in Drosophila leads to progressive neurodegeneration
Source:
Springer Science and Business Media LLC
FUS pathology in basophilic inclusion body disease
Source:
Springer Science and Business Media LLC
Mammalian stress granules and processing bodies.
Source:
Elsevier
TARDBP and FUS mutations associated with amyotrophic lateral sclerosis: summary and update.
Source:
Wiley
FUS gene mutations associated with familiar forms of amyotrophic lateral sclerosis affect cellular localization and aggregation properties of the encoded protein.
Source:
Pleiades Publishing Ltd
The role of FUS gene variants in neurodegenerative diseases
Source:
Springer Science and Business Media LLC
Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules.
Source:
Oxford University Press (OUP)
FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration.
Source:
Public Library of Science (PLoS)
Fused in Sarcoma (FUS) Protein Lacking Nuclear Localization Signal (NLS) and Major RNA Binding Motifs Triggers Proteinopathy and Severe Motor Phenotype in Transgenic Mice
Source:
American Society for Biochemistry & Molecular Biology (ASBMB)
Dynamic association–dissociation and harboring of endogenous mRNAs in stress granules
Source:
The Company of Biologists
Requirements for stress granule recruitment of fused in Sarcoma (FUS) and TAR DNA binding protein of 43 kDa (TDP-43)
Source:
American Society for Biochemistry & Molecular Biology (ASBMB)
Inhibition of TDP-43 aggregation by nucleic acid binding.
Source:
Public Library of Science (PLoS)
A “Two-hit” Hypothesis for Inclusion Formation by Carboxyl-terminal Fragments of TDP-43 Protein Linked to RNA Depletion and Impaired Microtubule-dependent Transport *
Source:
Elsevier BV
Aggresomes, inclusion bodies and protein aggregation.
Source:
Elsevier BV
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