In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
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A novel CHCHD10 mutation implicates a Mia40-dependent mitochondrial import deficit in ALS.An integration of fast alignment and maximum-likelihood methods for electron subtomogram averaging and classification.Could a Common Mechanism of Protein Degradation Impairment Underlie Many Neurodegenerative Diseases?
P2860
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
description
2018 nî lūn-bûn
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2018年の論文
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2018年学术文章
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2018年学术文章
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2018年学术文章
@zh-cn
2018年学术文章
@zh-hans
2018年学术文章
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2018年学术文章
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2018年學術文章
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name
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
@en
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
@nl
type
label
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
@en
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
@nl
prefLabel
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
@en
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.
@nl
P2093
P2860
P50
P1433
P1476
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment
@en
P2093
Carina Lehmer
Dieter Edbauer
F Ulrich Hartl
Florian Beck
Hannelore Hartmann
Manuela Pérez-Berlanga
Rubén Fernández-Busnadiego
Till Rudack
Wolfgang Baumeister
P2860
P304
696-705.e12
P356
10.1016/J.CELL.2017.12.030
P407
P577
2018-02-01T00:00:00Z