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Two-step mechanism of J-domain action in driving Hsp70 function

https://doi.org/10.1371/journal.pcbi.1007913

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Outgoing claims: the papers this work cites, builds on, or argues with.

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The Specialized Hsp70 (HscA) Interdomain Linker Binds to Its Nucleotide-Binding Domain and Stimulates ATP Hydrolysis in Both cis and trans Configurations

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Correction to The Specialized Hsp70 (HscA) Interdomain Linker Binds to Its Nucleotide-Binding Domain and Stimulates ATP Hydrolysis in Both cis and trans Configurations

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Real‐time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET

inferredcites →https://doi.org/10.1038/embor.2010.29openalex-snapshot

Co‐evolution‐driven switch of J‐protein specificity towards an Hsp70 partner

inferredcites →https://doi.org/10.1038/msb.2011.75openalex-snapshot

Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega

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The ClusPro web server for protein–protein docking

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Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions

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Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation

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Incoming claims: where this work appears in other papers’ reference lists and arguments.

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