The mechanism of the ATP-independent periplasmic chaperone SurA in outer membrane protein biogenesis

No abstract is available for this paper.

• Publication year

  2018

• Venue

  Unknown venue

• Publication date

  2018-09-01

• Fields of study

  Biology, Chemistry

• Identifiers

  No identifiers available.

• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

• A study on the biological function of heat shock factor 1 proteins in breast cancer

  2018cited by this paper
• Dynamic action of the Sec machinery during initiation, protein translocation and termination

  2018cited by this paper
• GroEL Ring Separation and Exchange in the Chaperonin Reaction.

  2018cited by this paper
• Inhibitor of intramembrane protease RseP blocks the σE response causing lethal accumulation of unfolded outer membrane proteins

  2018cited by this paper
• The gram-negative bacterial periplasm: Size matters

  2018cited by this paper
• Membrane protein insertion through a mitochondrial β-barrel gate

  2018cited by this paper
• Sequence-Specific Solution NMR Assignments of the β-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level.

  2018cited by this paper
• Single-Molecule Detection Reveals Different Roles of Skp and SurA as Chaperones.

  2018cited by this paper
• Conformational plasticity of molecular chaperones involved in periplasmic and outer membrane protein folding

  2018cited by this paper
• Monoclonal antibody targeting the β-barrel assembly machine of Escherichia coli is bactericidal

  2018cited by this paper
• Flexibility in the Periplasmic Domain of BamA Is Important for Function.

  2017cited by this paper
• Nanoscale-length control of the flagellar driveshaft requires hitting the tethered outer membrane

  2017cited by this paper
• The dynamic dimer structure of the chaperone Trigger Factor

  2017cited by this paper
• When proteostasis goes bad: Protein aggregation in the cell

  2017cited by this paper
• Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding

  2017cited by this paper
• GroEL actively stimulates folding of the endogenous substrate protein PepQ

  2017cited by this paper
• Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation

  2017cited by this paper
• Trigger factor chaperone acts as a mechanical foldase

  2017cited by this paper
• Outer membrane protein folding from an energy landscape perspective

  2017cited by this paper
• Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90

  2017cited by this paper
• A molecular mechanism of chaperone-client recognition

  2016cited by this paper
• From Chaperones to the Membrane with a BAM!

  2016cited by this paper
• Structural basis for the antifolding activity of a molecular chaperone

  2016cited by this paper
• Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins

  2016cited by this paper
• Environmental Regulation of Yersinia Pathophysiology

  2016cited by this paper
• Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

  2016cited by this paper
• Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

  2016cited by this paper
• Skp is a multivalent chaperone of outer membrane proteins

  2016cited by this paper
• The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain

  2016cited by this paper
• The CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic Membrane

  2016cited by this paper
• A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria*

  2016cited by this paper
• Structural basis of outer membrane protein insertion by the BAM complex

  2016cited by this paper
• Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins

  2016cited by this paper
• Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation

  2016cited by this paper
• In vivo aspects of protein folding and quality control

  2016cited by this paper
• The structure of the β-barrel assembly machinery complex

  2016cited by this paper
• Modulation of the Chaperone DnaK Allosterism by the Nucleotide Exchange Factor GrpE*

  2015cited by this paper
• Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR

  2015cited by this paper
• Substrate-binding domain conformational dynamics mediate Hsp70 allostery

  2015cited by this paper
• Surface Plasmon Resonance (SPR) Biosensors in Pharmaceutical Analysis

  2015cited by this paper
• Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins

  2015cited by this paper
• Multidomain Peptidyl Prolyl cis/trans Isomerases.

  2015cited by this paper
• On the lag phase in amyloid fibril formation

  2015cited by this paper
• Protein folding occurs while bound to the ATP-independent chaperone Spy

  2015cited by this paper
• HdeB functions as an acid-protective chaperone in bacteria.

  2015cited by this paper
• Dynamics, flexibility, and allostery in molecular chaperonins

  2015cited by this paper
• Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils upon Self-Association

  2015cited by this paper
• Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL.

  2015cited by this paper
• Proteostasis and the aging proteome in health and disease.

  2014cited by this paper
• The Sec translocon mediated protein transport in prokaryotes and eukaryotes

  2014cited by this paper
• Multitasking SecB chaperones in bacteria

  2014cited by this paper
• Supplementary Materials for Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

  2014cited by this paper
• Thermal-triggerd Proteinquake Leads to Disassembly of DegP Hexamer as an Imperative Activation Step

  2014cited by this paper
• Molecular chaperones in cellular protein folding: the birth of a field.

  2014cited by this paper
• Clustal Omega

  2014cited by this paper
• Mechanisms of protein-folding diseases at a glance

  2014cited by this paper
• Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function.

  2014cited by this paper
• Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins*

  2014cited by this paper
• Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

  2014cited by this paper
• Structural mapping of a chaperone-substrate interaction surface.

  2014cited by this paper
• Proteostasis impairment in protein-misfolding and -aggregation diseases.

  2014cited by this paper
• Genetic regulation of spy gene expression in Escherichia coli in the presence of protein unfolding agent ethanol.

  2014cited by this paper
• Super Spy variants implicate flexibility in chaperone action

  2014cited by this paper
• Diverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA.

  2014cited by this paper
• Assembly of β-barrel proteins into bacterial outer membranes.

  2014cited by this paper
• Structure of the AcrAB-TolC multidrug efflux pump

  2014cited by this paper
• Lateral opening and exit pore formation are required for BamA function.

  2014cited by this paper
• Screening and classifying small molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry

  2014cited by this paper
• Reconstitution of bacterial autotransporter assembly using purified components

  2014cited by this paper
• Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress

  2014cited by this paper
• Structural basis for lipopolysaccharide insertion in the bacterial outer membrane

  2014cited by this paper
• Folding membrane proteins in vitro: a table and some comments.

  2014cited by this paper
• Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion

  2014cited by this paper
• Folding mechanisms of periplasmic proteins.

  2014cited by this paper
• Demarcating SurA Activities Required for Outer Membrane Targeting of Yersinia pseudotuberculosis Adhesins

  2013cited by this paper
• Disulfide Bond Formation in the Bacterial Periplasm: Major Achievements and Challenges Ahead

  2013cited by this paper
• TROSY NMR spectroscopy of large soluble proteins.

  2013cited by this paper
• Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm

  2013cited by this paper
• Protein rescue from aggregates by powerful molecular chaperone machines

  2013cited by this paper
• Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins.

  2013cited by this paper
• Identification of FkpA as a Key Quality Control Factor for the Biogenesis of Outer Membrane Proteins under Heat Shock Conditions

  2013cited by this paper
• Dissecting the Effects of Periplasmic Chaperones on the In Vitro Folding of the Outer Membrane Protein PagP

  2013cited by this paper
• Molecular chaperone functions in protein folding and proteostasis.

  2013cited by this paper
• Cooperative Binding

  2013cited by this paper
• Conformation and dynamics of the periplasmic membrane-protein–chaperone complexes OmpX–Skp and tOmpA–Skp

  2013cited by this paper
• The lipid bilayer-inserted membrane protein BamA of Escherichia coli facilitates insertion and folding of outer membrane protein A from its complex with Skp.

  2013cited by this paper
• Binding and folding of the small bacterial chaperone HdeA.

  2013cited by this paper
• Chaperone-protease networks in mitochondrial protein homeostasis.

  2013cited by this paper
• Restrictions to protein folding determined by the protein size

  2013cited by this paper
• Chaperone machines for protein folding, unfolding and disaggregation

  2013cited by this paper
• Structural insight into the biogenesis of β-barrel membrane proteins

  2013cited by this paper
• Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics

  2012cited by this paper
• NIH Image to ImageJ: 25 years of image analysis

  2012cited by this paper
• Insights into the Function and Structural Flexibility of the Periplasmic Molecular Chaperone SurA

  2012cited by this paper
• Conditional disorder in chaperone action.

  2012cited by this paper
• Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding.

  2012cited by this paper
• The FKBP families of higher plants: Exploring the structures and functions of protein interaction specialists

  2012cited by this paper
• BRICHOS Domains Efficiently Delay Fibrillation of Amyloid β-Peptide*

  2012cited by this paper
• Massign: an assignment strategy for maximizing information from the mass spectra of heterogeneous protein assemblies.

  2012cited by this paper
• Conformational Properties of the Unfolded State of Im7 in Nondenaturing Conditions

  2012cited by this paper

• No citing papers are available for this paper.