about
Expanding proteostasis by membrane trafficking networksComparing protein folding in vitro and in vivo: foldability meets the fitness challengeIndividual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingQuantifying chaperone-mediated transitions in the proteostasis network of E. coliViewing protein fitness landscapes through a next-gen lens.Bacterial proteostasis balances energy and chaperone utilization efficientlyBiP clustering facilitates protein folding in the endoplasmic reticulumMetabolomic and proteomic investigations of impacts of titanium dioxide nanoparticles on Escherichia coli.The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate proteinSingle-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.Understanding protein aggregation from the view of monomer dynamicsMultilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism.A systems biology approach to optimising hosts for industrial protein production.Computer Simulations of the Bacterial Cytoplasm.Combating neurodegenerative disease with chemical probes and model systems.How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.When proteostasis goes bad: Protein aggregation in the cell.The physical dimensions of amyloid aggregates control their infective potential as prion particles.Ligand-promoted protein folding by biased kinetic partitioning.Altered Co-Translational Processing Plays a Role in Huntington's Pathogenesis-A Hypothesis.Thermosensitivity of growth is determined by chaperone-mediated proteome reallocation.Translation efficiency is maintained at elevated temperature in E. coli.Outer membrane protein folding from an energy landscape perspective.Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.Protein folding in the cell, from atom to organism
P2860
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P2860
description
2012 nî lūn-bûn
@nan
2012 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մարտին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
FoldEco: a model for proteostasis in E. coli.
@ast
FoldEco: a model for proteostasis in E. coli.
@en
type
label
FoldEco: a model for proteostasis in E. coli.
@ast
FoldEco: a model for proteostasis in E. coli.
@en
prefLabel
FoldEco: a model for proteostasis in E. coli.
@ast
FoldEco: a model for proteostasis in E. coli.
@en
P2093
P2860
P1433
P1476
FoldEco: a model for proteostasis in E. coli.
@en
P2093
David L Powers
Evan T Powers
Lila M Gierasch
P2860
P304
P356
10.1016/J.CELREP.2012.02.011
P577
2012-03-01T00:00:00Z