A more precise characterization of chaperonin substrates.
about
What distinguishes GroEL substrates from other Escherichia coli proteins?T3SEdb: data warehousing of virulence effectors secreted by the bacterial Type III Secretion System.Interplay between chaperones and protein disorder promotes the evolution of protein networks.Difference in the distribution pattern of substrate enzymes in the metabolic network of Escherichia coli, according to chaperonin requirement.Reduced selective constraint in endosymbionts: elevation in radical amino acid replacements occurs genome-wide.Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.Indole-3-glycerol-phosphate synthase is recognized by a cold-inducible group II chaperonin in Thermococcus kodakarensis.Identification of a novel protein binding motif within the T-synthase for the molecular chaperone Cosmc.Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.How do eubacterial organisms manage aggregation-prone proteome?Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.
P2860
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P2860
A more precise characterization of chaperonin substrates.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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name
A more precise characterization of chaperonin substrates.
@en
A more precise characterization of chaperonin substrates.
@nl
type
label
A more precise characterization of chaperonin substrates.
@en
A more precise characterization of chaperonin substrates.
@nl
prefLabel
A more precise characterization of chaperonin substrates.
@en
A more precise characterization of chaperonin substrates.
@nl
P2093
P2860
P356
P1433
P1476
A more precise characterization of chaperonin substrates.
@en
P2093
Emanuele Raineri
Luis Serrano
Paolo Ribeca
Tobias Maier
P2860
P304
P356
10.1093/BIOINFORMATICS/BTQ287
P407
P577
2010-06-02T00:00:00Z