The amino-terminal domain of ClpB protein plays a crucial role in its substrate disaggregation activity

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The amino-terminal domain of ClpB protein plays a crucial role in its substrate disaggregation activity

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wetenschappelijk artikel

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наукова стаття, опублікована в жовтні 2018

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The amino-terminal domain of C ...... strate disaggregation activity

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The amino-terminal domain of C ...... strate disaggregation activity

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The amino-terminal domain of C ...... strate disaggregation activity

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The amino-terminal domain of C ...... strate disaggregation activity

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The amino-terminal domain of C ...... strate disaggregation activity

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The amino-terminal domain of C ...... strate disaggregation activity

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P1476

The amino-terminal domain of C ...... strate disaggregation activity

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P2093

Janendra K Batra

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Prajna Tripathi

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Priyanka Parijat

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Virendra Kumar Patel

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P2860

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

Analysis of the function of mycobacterial DnaJ proteins by overexpression and microarray profiling

The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis

Molecular chaperones and protein quality control

Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein

Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation.

Construction and characterization of a Helicobacter pylori clpB mutant and role of the gene in the stress response.

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

P304

1669-1690

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P31

scholarly article

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10.1002/2211-5463.12509

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English

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P478

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P577

2018-10-01T00:00:00Z

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30338218

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6168691

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