首页> The Journal of biological chemistry> DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine

DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine

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第一作者： Doyle,S.M.

作者： Doyle,S.M. ^[1] ; Hoskins,J.R. ; Wickner,S.

作者单位： Laboratory of Molecular Biology, NCI, National Institutes of Health, 37 Convent Dr., Bethesda, MD ^[1]

发布时间 2014-01-21

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The Journal of biological chemistry

2012年287卷34期

28470-28479页

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The Journal of biological chemistry

2012年287卷34期

28470-28479页

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DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine

The Journal of biological chemistry

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The Journal of biological chemistry

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DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine

The Journal of biological chemistry

相似文献

同项目论文

The Journal of biological chemistry

相关期刊

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