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Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Quantifying chaperone-mediated transitions in the proteostasis network of E. coliFoldEco: a model for proteostasis in E. coli.Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system.BiP clustering facilitates protein folding in the endoplasmic reticulumSmall molecule DnaK modulators targeting the beta-domain.Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumptionA pharmacological investigation of Hippophae salicifolia (HS) and Hippophae rhamnoides turkestanica (HRT) against multiple stress (C-H-R): an experimental study using rat modelHSP70 expression: does it a novel fatigue signalling factor from immune system to the brain?Rapid perturbation of free-energy landscapes: from in vitro to in vivo.Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome.Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.The Hsp70 chaperone system maintains high concentrations of active proteins and suppresses ATP consumption during heat shock.Thermosensitivity of growth is determined by chaperone-mediated proteome reallocation.Changes in phosphorylated heat-shock protein 27 in response to acute ureteral obstruction in rats.Cochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium
P2860
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P2860
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Modeling Hsp70-mediated protein folding.
@en
type
label
Modeling Hsp70-mediated protein folding.
@en
prefLabel
Modeling Hsp70-mediated protein folding.
@en
P2093
P2860
P1433
P1476
Modeling Hsp70-mediated protein folding.
@en
P2093
Masaru Tomita
Matthias P Mayer
P2860
P304
P356
10.1529/BIOPHYSJ.106.083394
P407
P577
2006-04-28T00:00:00Z