The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.
about
Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroCryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin.Protein misfolding and aggregation in cataract disease and prospects for prevention.Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutantsInhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate.
P2860
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P2860
The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.
description
2011 nî lūn-bûn
@nan
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.
@en
type
label
The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.
@en
prefLabel
The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.
@en
P2093
P2860
P356
P1433
P1476
The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.
@en
P2093
Daniel R Goulet
Jonathan A King
Junjie Zhang
Kelly M Knee
P2860
P356
10.1002/PRO.531
P50
P577
2011-01-01T00:00:00Z