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注意：仅列出部分参考文献，下载原文获取全部文献信息。Hydrophilic residues 526KNDAAD531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity
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Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
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An expanded protein folding cage in the GroEL-gp31 complex
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Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring
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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes
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Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
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The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein
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Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry
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Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
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The 13Å structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy
S Falke et al.
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The N terminus of the head protein of T4 bacteriophage directs proteins to the GroEL chaperonin
L Snyder et al.
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Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL
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Expansion and compression of a protein folding intermediate by GroEL
Z Lin et al.
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Role of the γ-phosphate of ATP in triggering protein folding by GroEL-GroES:: function, structure and energetics
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On the fitting of model electron densities into EM reconstructions:: a reciprocal-space formulation
J Navaza et al.
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Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
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