
Amyotrophic lateral sclerosis (ALS) pathology is linked to the aberrant aggregation of specific proteins, including TDP‐43, FUS, and SOD1, but it is not clear why these aggregation events cause ALS. In this issue of The EMBO Journal , Mateju et al (2017) report a direct link between misfolded proteins accumulating in stress granules and the phase transition of these stress granules from liquid to solid. This discovery provides a model connecting protein aggregation to stress granule dysfunction.
Stress, Physiological, 610, Humans, RNA, Messenger, Cytoplasmic Granules
Stress, Physiological, 610, Humans, RNA, Messenger, Cytoplasmic Granules
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| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
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