The Periplasmic Molecular Chaperone Protein SurA Binds a Peptide Motif That Is Characteristic of Integral Outer Membrane Proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference17 articles.
1. SurA assists the folding of Escherichia coli outer membrane proteins
2. New components of protein folding in extracytoplasmic compartments ofEscherichia coliSurA, FkpA and Skp/OmpH
3. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.
4. surA, an Escherichia coli gene essential for survival in stationary phase
5. A new heat-shock gene, ppiD, encodes a peptidyl–prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
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1. Dual client binding sites in the ATP-independent chaperone SurA;Nature Communications;2024-09-14
2. Outer membrane protein assembly mediated by BAM-SurA complexes;Nature Communications;2024-09-01
3. Molecular Machines that Facilitate Bacterial Outer Membrane Protein Biogenesis;Annual Review of Biochemistry;2024-08-02
4. A team of chaperones play to win in the bacterial periplasm;Trends in Biochemical Sciences;2024-08
5. Dual recognition of multiple signals in bacterial outer membrane proteins enhances assembly and maintains membrane integrity;eLife;2024-01-16
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