ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS
- 6 November 2020
- journal article
- research article
- Published by Elsevier BV in Molecular Cell
- Vol. 80 (4), 666-681.e8
- https://doi.org/10.1016/j.molcel.2020.10.014
Abstract
No abstract availableFunding Information
- National Science Foundation
- National Institutes of Health
This publication has 80 references indexed in Scilit:
- ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granulesHuman Molecular Genetics, 2013
- TDP-43 and FUS RNA-binding Proteins Bind Distinct Sets of Cytoplasmic Messenger RNAs and Differently Regulate Their Post-transcriptional Fate in Motoneuron-like CellsOnline Journal of Public Health Informatics, 2012
- Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALSNeuron, 2011
- The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life spanJCI Insight, 2011
- FUS and TARDBP but Not SOD1 Interact in Genetic Models of Amyotrophic Lateral SclerosisPLoS Genetics, 2011
- Changepoint Analysis for Single-Molecule Polarized Total Internal Reflection Fluorescence Microscopy ExperimentsMethods in Enzymology, 2010
- Fus gene mutations in familial and sporadic amyotrophic lateral sclerosisMuscle & Nerve, 2010
- Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohortNeurology, 2009
- High-resolution, long-term characterization of bacterial motility using optical tweezersNature Methods, 2009
- Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 1993