Equilibrium intermediates in the reversible unfolding of firefly (Photinus pyralis) luciferase.
about
The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitroEvaluation of similarities in the cis/trans isomerase function of trigger factor and DnaK.Identification of a redox-regulated chaperone network.Chaperones rescue luciferase folding by separating its domains.Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.Transient model of thermal deactivation of enzymesMass spectrometry analysis and transcriptome sequencing reveal glowing squid crystal proteins are in the same superfamily as firefly luciferase.Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP.Hsp72 chaperone function is dispensable for protection against stress-induced apoptosisTransient interactions of a slow-folding protein with the Hsp70 chaperone machineryInteraction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity.Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family.The Hsp70 chaperone system maintains high concentrations of active proteins and suppresses ATP consumption during heat shock.The microtubule-associated protein, NUD-1, exhibits chaperone activity in vitro.Circular permutation of 5-aminolevulinate synthase: effect on folding, conformational stability, and structure.The roles of the two zinc binding sites in DnaJ.Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.Misfolding of luciferase at the single-molecule level.Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli.Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.Folding of coliphage T4 short tail fiber in vitro. Analysing the role of a bacteriophage-encoded chaperone.Simple and ultrastable all-inclusive pullulan tablets for challenging bioassays.Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium
P2860
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P2860
Equilibrium intermediates in the reversible unfolding of firefly (Photinus pyralis) luciferase.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Equilibrium intermediates in t ...... (Photinus pyralis) luciferase.
@en
type
label
Equilibrium intermediates in t ...... (Photinus pyralis) luciferase.
@en
prefLabel
Equilibrium intermediates in t ...... (Photinus pyralis) luciferase.
@en
P2093
P2860
P356
P1476
Equilibrium intermediates in t ...... (Photinus pyralis) luciferase.
@en
P2093
P2860
P304
P356
10.1074/JBC.272.11.7099
P407
P577
1997-03-01T00:00:00Z