Liquids, Fibers, and Gels: The Many Phases of Neurodegeneration

Shana Elbaum-Garfinkle; Clifford P. Brangwynne

doi:10.1016/j.devcel.2015.11.014

Liquids, Fibers, and Gels: The Many Phases of Neurodegeneration

Shana Elbaum-Garfinkle, Clifford P. Brangwynne

Research output: Contribution to journal › Short survey › peer-review

45 Scopus citations

Abstract

Recent advances suggest that phase transitions of proteins into liquid or hydrogel states could underlie pathological protein aggregation associated with neurodegenerative disease. In a recent issue of Neuron, Murakami et al. (2015) demonstrate that ALS-associated FUS mutations abrogate the reversibility of condensed liquids and/or hydrogels, leading to neurotoxicity in C. elegans.

Original language	English (US)
Pages (from-to)	531-532
Number of pages	2
Journal	Developmental cell
Volume	35
Issue number	5
DOIs	https://doi.org/10.1016/j.devcel.2015.11.014
State	Published - 2015
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Biochemistry, Genetics and Molecular Biology
Molecular Biology
Cell Biology
Developmental Biology

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10.1016/j.devcel.2015.11.014

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title = "Liquids, Fibers, and Gels: The Many Phases of Neurodegeneration",

abstract = "Recent advances suggest that phase transitions of proteins into liquid or hydrogel states could underlie pathological protein aggregation associated with neurodegenerative disease. In a recent issue of Neuron, Murakami et al. (2015) demonstrate that ALS-associated FUS mutations abrogate the reversibility of condensed liquids and/or hydrogels, leading to neurotoxicity in C. elegans.",

author = "Shana Elbaum-Garfinkle and Brangwynne, {Clifford P.}",

note = "Publisher Copyright: {\textcopyright} 2015 Elsevier Inc.",

year = "2015",

doi = "10.1016/j.devcel.2015.11.014",

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T2 - The Many Phases of Neurodegeneration

AU - Elbaum-Garfinkle, Shana

AU - Brangwynne, Clifford P.

PY - 2015

Y1 - 2015

N2 - Recent advances suggest that phase transitions of proteins into liquid or hydrogel states could underlie pathological protein aggregation associated with neurodegenerative disease. In a recent issue of Neuron, Murakami et al. (2015) demonstrate that ALS-associated FUS mutations abrogate the reversibility of condensed liquids and/or hydrogels, leading to neurotoxicity in C. elegans.

AB - Recent advances suggest that phase transitions of proteins into liquid or hydrogel states could underlie pathological protein aggregation associated with neurodegenerative disease. In a recent issue of Neuron, Murakami et al. (2015) demonstrate that ALS-associated FUS mutations abrogate the reversibility of condensed liquids and/or hydrogels, leading to neurotoxicity in C. elegans.

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DO - 10.1016/j.devcel.2015.11.014

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JO - Developmental cell

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Liquids, Fibers, and Gels: The Many Phases of Neurodegeneration

Abstract

All Science Journal Classification (ASJC) codes

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