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4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement
4.0-A resolution cryo-EM structure mammalian chaperonin TRiC/CCT reveals unique subunit arrangement
2015/12/11
The essential double-ring eukaryotic chaperonin TRiC/CCT (TCP1-ring complex or chaperonin containing TCP1) assists the folding of approximately 5-10% of the cellular proteome. Many TRiC substrates can...
Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle
Crystal structures group II chaperonin reveal closed states associated protein folding cycle
2015/12/11
Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. Here, we de...
Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes.
Exogenous delivery chaperonin fragment ApiCCT modulates mutant Huntingtin cellular phenotypes
2015/12/11
Aggregation of misfolded proteins is characteristic of a number of neurodegenerative diseases, including Huntington disease (HD). The CCT/TRiC (chaperonin containing TCP-1/TCP-1 ring) chaperonin compl...
Modulation of STAT3 folding and function by TRiC/CCT chaperonin.
Modulation STAT3 folding function TRiC/CCT chaperonin
2015/12/11
Signal transducer and activator of transcription 3 (Stat3) transduces signals of many peptide hormones from the cell surface to the nucleus and functions as an oncoprotein in many types of cancers, ye...
A Direct Regulatory Interaction between Chaperonin TRiC and Stress-Responsive Transcription Factor HSF1
Direct Regulatory Interaction TRiC Stress-Responsive Transcription Factor HSF1
2015/12/11
Heat shock transcription factor 1 (HSF1) is an evolutionarily conserved transcription factor that protects cells from protein-misfolding-induced stress and apoptosis. The mechanisms by which cytosolic...
The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation.
dynamic conformational cycle group I chaperonin C-termini revealed molecular dynamics simulation.
2015/12/11
Chaperonins are large ring shaped oligomers that facilitate protein folding by encapsulation within a central cavity. All chaperonins possess flexible C-termini which protrude from the equatorial doma...
期刊信息
篇名
Folding Behavior of chaperonin-mediated substrate protein
语种
英文
撰写或编译
撰写
作者
Wei-xin Xu,Jun Wang,and Wei Wang
第一作者单位
Department of Physics, Nanjing University
刊物名称
Proteins: Structure, Function...