Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
about
A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesisStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneStructural basis for the antifolding activity of a molecular chaperoneThe CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic MembraneLateral opening in the intact β-barrel assembly machinery captured by cryo-EM.From Chaperones to the Membrane with a BAM!Outer membrane protein biogenesis in Gram-negative bacteriaImpact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins.Dimeric Structure of the Bacterial Extracellular Foldase PrsA.Revisiting the interaction between the chaperone Skp and lipopolysaccharideHdeB chaperone activity is coupled to its intrinsic dynamic properties.The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane ProteinsA molecular mechanism of chaperone-client recognition.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.Protein folding in the cell envelope of Escherichia coli.Envelope Stress Responses: An Interconnected Safety Net.Skp is a multivalent chaperone of outer-membrane proteinsSkp Trimer Formation Is Insensitive to Salts in the Physiological Range.A protean clamp guides membrane targeting of tail-anchored proteins.Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding.Outer membrane protein folding from an energy landscape perspective.Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.Job contenders: roles of the β-barrel assembly machinery and the translocation and assembly module in autotransporter secretion.Slow Interconversion in a Heterogeneous Unfolded-State Ensemble of Outer-Membrane Phospholipase A.Analyzing the Role of Periplasmic Folding Factors in the Biogenesis of OMPs and Members of the Type V Secretion System.Structural Mapping of a Chaperone-Substrate Interaction SurfaceStructural Mapping of a Chaperone-Substrate Interaction SurfaceStructural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space
P2860
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P2860
Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh
2013年學術文章
@zh-hant
name
Conformation and dynamics of t ...... plexes OmpX-Skp and tOmpA-Skp.
@en
Conformation and dynamics of t ...... plexes OmpX-Skp and tOmpA-Skp.
@nl
type
label
Conformation and dynamics of t ...... plexes OmpX-Skp and tOmpA-Skp.
@en
Conformation and dynamics of t ...... plexes OmpX-Skp and tOmpA-Skp.
@nl
prefLabel
Conformation and dynamics of t ...... plexes OmpX-Skp and tOmpA-Skp.
@en
Conformation and dynamics of t ...... plexes OmpX-Skp and tOmpA-Skp.
@nl
P2860
P356
P1476
Conformation and dynamics of t ...... plexes OmpX-Skp and tOmpA-Skp.
@en
P2093
Congwei Wang
P2860
P2888
P304
P356
10.1038/NSMB.2677
P577
2013-09-29T00:00:00Z