Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
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Crystal Structure of YaeT: Conformational Flexibility and Substrate RecognitionConserved Properties of Polypeptide Transport-associated (POTRA) Domains Derived from Cyanobacterial Omp85Structure and Flexibility of the Complete Periplasmic Domain of BamA: The Protein Insertion Machine of the Outer MembraneActivation of Colicin M by the FkpA Prolyl Cis-Trans Isomerase/ChaperoneCovalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic CagesCrystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative BacteriaHigh-resolution structure of a new crystal form of BamA POTRA4–5 fromEscherichia coliCrystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural FeaturesCrystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamCStructural basis for the interaction of BamB with the POTRA3-4 domains of BamAThe yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress.Cellular disulfide bond formation in bioactive peptides and proteinsGenetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathwaysIdentification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coliInvestigation of Yersinia pestis Laboratory Adaptation through a Combined Genomics and Proteomics ApproachThe CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic MembraneProtein targeting and transport as a necessary consequence of increased cellular complexityPpiA, a surface PPIase of the cyclophilin family in Lactococcus lactisExtreme Dynamics in the BamA β-Barrel Seam.Membrane integration of an essential β-barrel protein prerequires burial of an extracellular loop.The β-barrel assembly machinery in motion.Flexibility in the Periplasmic Domain of BamA Is Important for Function.Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM.Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins.From Chaperones to the Membrane with a BAM!BamA POTRA Domain Interacts with a Native Lipid Membrane SurfaceA Suppressor Mutation That Creates a Faster and More Robust σE Envelope Stress ResponseA Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria.How does a β-barrel integral membrane protein insert into the membrane?Outer membrane protein biogenesis in Gram-negative bacteriaImpact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins.A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria.Computational redesign of the lipid-facing surface of the outer membrane protein OmpA.A Homology Model Reveals Novel Structural Features and an Immunodominant Surface Loop/Opsonic Target in the Treponema pallidum BamA Ortholog TP_0326Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAINLytM proteins play a crucial role in cell separation, outer membrane composition, and pathogenesis in nontypeable Haemophilus influenzae.Evolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein.Lateral opening and exit pore formation are required for BamA functionDegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli.
P2860
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P2860
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
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2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
@ast
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
@en
type
label
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
@ast
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
@en
prefLabel
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
@ast
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
@en
P2093
P2860
P356
P1433
P1476
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
@en
P2093
Daniel Kahne
Joseph G Sklar
P2860
P304
P356
10.1101/GAD.1581007
P577
2007-10-01T00:00:00Z