Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

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Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

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scientific article published on 19 September 2018

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wetenschappelijk artikel

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наукова стаття, опублікована у вересні 2018

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Structural investigation of a ...... regulates the functional cycle

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Structural investigation of a ...... regulates the functional cycle

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Structural investigation of a ...... regulates the functional cycle

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Structural investigation of a ...... regulates the functional cycle

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Structural investigation of a ...... regulates the functional cycle

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Structural investigation of a ...... regulates the functional cycle

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Structural investigation of a ...... regulates the functional cycle

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Elodie Crublet

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Pierre Gans

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Mechanism of folding chamber closure in a group II chaperonin

A refined solution structure of hen lysozyme determined using residual dipolar coupling data

Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle

Crystal Structure of Group II Chaperonin in the Open State

Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin

Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber

Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.

Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

NMR analysis of a 900K GroEL GroES complex

The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin

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eaau4196

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scholarly article

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10.1126/SCIADV.AAU4196

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English

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2018-09-19T00:00:00Z

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30255156

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6154984

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