The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
about
The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coliExpression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10Molecular and biochemical basis of intermediate maple syrup urine disease. Occurrence of homozygous G245R and F364C mutations at the E1 alpha locus of Hispanic-Mexican patientsNucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludisThe human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refoldingSignificant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cyclingNative-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysisInterplay of structure and disorder in cochaperonin mobile loopsSignificance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondriaDynamics, flexibility, and allostery in molecular chaperoninsChaperoninsProteotoxic stress and inducible chaperone networks in neurodegenerative disease and agingPurification and characterization of the assembly factor P17 of the lipid-containing bacteriophage PRD1.High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers.The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomerChaperonins in disease: mechanisms, models, and treatments.The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.Chaperonins--keeping a lid on folding proteins.Mechanism of substrate recognition by the chaperonin GroEL.DNA-strand exchange promoted by RecA protein in the absence of ATP: implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions.Structural transitions of confined model proteins: molecular dynamics simulation and experimental validationBiochemical characterization of pathogenic mutations in human mitochondrial methionyl-tRNA formyltransferaseType I chaperonins: not all are created equal.Suppression of amber codons in Caulobacter crescentus by the orthogonal Escherichia coli histidyl-tRNA synthetase/tRNAHis pairIsolation and characterization of Bacillus subtilis groE regulatory mutants: evidence for orf39 in the dnaK operon as a repressor gene in regulating the expression of both groE and dnaKCloning and characterization of two groESL operons of Rhodobacter sphaeroides: transcriptional regulation of the heat-induced groESL operon.Statistical mechanics of kinetic proofreading in protein folding in vivo.ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coliEvidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions.A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle.A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin.Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturantChaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirementEngineering a nanopore with co-chaperonin function.Rate theories for biologistsHSP60 gene sequences as universal targets for microbial species identification: studies with coagulase-negative staphylococci.GroEL-mediated protein folding: making the impossible, possible.
P2860
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P2860
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
@en
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
@nl
type
label
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
@en
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
@nl
prefLabel
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
@en
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
@nl
P2093
P356
P1433
P1476
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
@en
P2093
P2888
P304
P356
10.1038/366228A0
P407
P577
1993-11-01T00:00:00Z
P6179
1048865531