Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.
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Contribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisStructural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography.The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosolAsymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiCSequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysisStructure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.The βγ-crystallins: native state stability and pathways to aggregation.CCT2 Mutations Evoke Leber Congenital Amaurosis due to Chaperone Complex Instability.Sexually Dimorphic Gene Expression Associated with Growth and Reproduction of Tongue Sole (Cynoglossus semilaevis) Revealed by Brain Transcriptome Analysis.Prokaryotic Chaperonins as Experimental Models for Elucidating Structure-Function Abnormalities of Human Pathogenic Mutant Counterparts.Internal (His)₆-tagging delivers a fully functional hetero-oligomeric class II chaperonin in high yield.The TCP1γ subunit of Leishmania donovani forms a biologically active homo-oligomeric complex.Chaperonin containing TCP1 subunit 5 is a tumor associated antigen of non-small cell lung cancer.Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutantsRole of CCT chaperonin in the disassembly of mitotic checkpoint complexes.Identification of an allosteric network that influences assembly and function of group II chaperonins.Genetic expansion of chaperonin-containing TCP-1 (CCT/TRiC) complex subunits yields testis-specific isoforms required for spermatogenesis in planarian flatworms.Chaperonin containing TCP-1 subunit 3 is critical for gastric cancer growth.Reconstitution of Pure Chaperonin Hetero-Oligomer Preparations in Vitro by Temperature Modulation.Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog.
P2860
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P2860
Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.
description
2013 nî lūn-bûn
@nan
2013年の論文
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2013年論文
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2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
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2013年论文
@zh-cn
name
Human CCT4 and CCT5 chaperonin ...... gically active homo-oligomers.
@en
type
label
Human CCT4 and CCT5 chaperonin ...... gically active homo-oligomers.
@en
prefLabel
Human CCT4 and CCT5 chaperonin ...... gically active homo-oligomers.
@en
P2093
P2860
P356
P1476
Human CCT4 and CCT5 chaperonin ...... gically active homo-oligomers.
@en
P2093
Cameron Haase-Pettingell
Jonathan A King
Oksana A Sergeeva
Steven J Ludtke
P2860
P304
17734-17744
P356
10.1074/JBC.M112.443929
P407
P50
P577
2013-04-23T00:00:00Z