Protein folding in the cell: competing models of chaperonin function.
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The effect of macromolecular crowding on chaperonin-mediated protein foldingUse of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid proteinDecoding mechanisms by which silent codon changes influence protein biogenesis and functionChaperone activity and structure of monomeric polypeptide binding domains of GroELA structural model for GroEL-polypeptide recognitionIdentification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.Specific interaction between GroEL and denatured protein measured by compression-free force spectroscopy.Subtractive hybridization-mediated analysis of genes and in silico prediction of associated microRNAs under waterlogged conditions in sugarcane (Saccharum spp.).A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.The substrate binding domain of DnaK facilitates slow protein refoldingProtein multifunctionality: principles and mechanisms.Chaperonin 60 unfolds its secrets of cellular communicationMechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.Dissecting intrinsic chaperonin activityDetection of changes in pairwise interactions during allosteric transitions: coupling between local and global conformational changes in GroELRefolding chromatography with immobilized mini-chaperonesAnfinsen comes out of the cage during assembly of the bacterial pilus.Structural basis for accommodation of nonsteroidal ligands in the androgen receptorIn vivo activities of GroEL minichaperonesProtein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunitA monomeric mutant of Clostridium symbiosum glutamate dehydrogenase: comparison with a structured monomeric intermediate obtained during refolding.Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.Distinguishing between sequential and nonsequentially folded proteins: implications for folding and misfoldingStrategies for achieving high-level expression of genes in Escherichia coli.Nitrogen-Deficiency Stress Induces Protein Expression Differentially in Low-N Tolerant and Low-N Sensitive Maize Genotypes.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.BAG3, a host cochaperone, facilitates varicella-zoster virus replication.Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae.Expression differences in mitochondrial and secretory chaperonin 60 (Cpn60) in pancreatic acinar cellsThe folding competence of HIV-1 Tat mediated by interaction with TAR RNA.GroEL binds a late folding intermediate of phage P22 coat protein.In vivo newly translated polypeptides are sequestered in a protected folding environment.GroES/GroEL and DnaK/DnaJ have distinct roles in stress responses and during cell cycle progression in Caulobacter crescentus.Chaperonin function: folding by forced unfolding.Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli.Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease.Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera.
P2860
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P2860
Protein folding in the cell: competing models of chaperonin function.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Protein folding in the cell: competing models of chaperonin function.
@en
type
label
Protein folding in the cell: competing models of chaperonin function.
@en
prefLabel
Protein folding in the cell: competing models of chaperonin function.
@en
P1433
P1476
Protein folding in the cell: competing models of chaperonin function
@en
P2093
P356
10.1096/FASEBJ.10.1.8566542
P407
P577
1996-01-01T00:00:00Z