Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients (scientific article published on 01 May 2020)

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SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins

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Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins

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Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics

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Dynamic action of the Sec machinery during initiation, protein translocation and termination.

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C-terminal kink formation is required for lateral gating in BamA

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SurA assists the folding of Escherichia coli outer membrane proteins

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Hsp90 interaction with clients.

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P433

issue

P921

main subject

membrane protein

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