Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine
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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityGroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingDynamic Complexes in the Chaperonin-Mediated Protein Folding CycleChaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteinsMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsProbing water density and dynamics in the chaperonin GroEL cavity.Knotting and unknotting proteins in the chaperonin cage: Effects of the excluded volumeThe C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate proteinFormation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formA human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model.Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function.Crystal structure of the human mitochondrial chaperonin symmetrical football complex.Structural insight into the cooperation of chloroplast chaperonin subunits.Probing allosteric mechanisms using native mass spectrometry.How do chaperonins fold protein?The chaperone toolbox at the single-molecule level: From clamping to confining.Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development.Folding of maltose binding protein outside of and in GroEL.Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis.Quaternary structures of GroEL and naïve-Hsp60 chaperonins in solution: a combined SAXS-MD study
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Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 28 October 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Symmetric GroEL:GroES2 complex ...... of the chaperonin nanomachine
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Symmetric GroEL:GroES2 complex ...... of the chaperonin nanomachine.
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Symmetric GroEL:GroES2 complex ...... of the chaperonin nanomachine
@en
Symmetric GroEL:GroES2 complex ...... of the chaperonin nanomachine.
@nl
prefLabel
Symmetric GroEL:GroES2 complex ...... of the chaperonin nanomachine
@en
Symmetric GroEL:GroES2 complex ...... of the chaperonin nanomachine.
@nl
P2860
P356
P1476
Symmetric GroEL:GroES2 complex ...... of the chaperonin nanomachine
@en
P2093
George H Lorimer
P2860
P304
P356
10.1073/PNAS.1318862110
P407
P50
P577
2013-10-28T00:00:00Z