Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.
about
Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.Identification of an allosteric network that influences assembly and function of group II chaperonins.Development of a yeast internal-subunit eGFP labeling strategy and its application in subunit identification in eukaryotic group II chaperonin TRiC/CCT.In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle
P2860
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
@yue
2016年學術文章
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2016年學術文章
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name
Staggered ATP binding mechanis ...... rough high-resolution cryo-EM.
@en
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC
@nl
type
label
Staggered ATP binding mechanis ...... rough high-resolution cryo-EM.
@en
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC
@nl
prefLabel
Staggered ATP binding mechanis ...... rough high-resolution cryo-EM.
@en
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC
@nl
P2093
P2860
P356
P1476
Staggered ATP binding mechanis ...... rough high-resolution cryo-EM.
@en
P2093
Caixuan Liu
Huping Wang
Liangliang Kong
Mingliang Jin
Yunxiang Zang
Zhicheng Cui
P2860
P2888
P304
P356
10.1038/NSMB.3309
P577
2016-10-24T00:00:00Z