Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer.
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The role of short-chain conjugated poly-(R)-3-hydroxybutyrate (cPHB) in protein foldingBlock and boost DNA transfer: opposite roles of OmpA in natural and artificial transformation of Escherichia coliMass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.Hydrophobic mismatch and lipid sorting near OmpA in mixed bilayers: atomistic and coarse-grained simulations.Insights into the structure and assembly of Escherichia coli outer membrane protein AAlternative folding pathways of the major porin OprF of Pseudomonas aeruginosa.Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-domain open conformerProbing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.Gating of transient receptor potential melastatin 8 (TRPM8) channels activated by cold and chemical agonists in planar lipid bilayers.Polyester modification of the mammalian TRPM8 channel protein: implications for structure and function.Pore characteristics of nontypeable Haemophilus influenzae outer membrane protein P5 in planar lipid bilayersPolar localization of PhoN2, a periplasmic virulence-associated factor of Shigella flexneri, is required for proper IcsA exposition at the old bacterial pole.Cross-linking measurements of in vivo protein complex topologies.Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA.Physiological importance of poly-(R)-3-hydroxybutyrates.Virulence of Erwinia amylovora, a prevalent apple pathogen: Outer membrane proteins and type III secreted effectors increase fitness and compromise plant defenses.Recombinant outer membrane protein A induces a protective immune response against Escherichia coli infection in mice.Dual orientation of the outer membrane lipoprotein Pal in Escherichia coli.Resolving the native conformation of Escherichia coli OmpA.Low-resolution structures of OmpA⋅DDM protein-detergent complexes.
P2860
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P2860
Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer.
description
2005 nî lūn-bûn
@nan
2005 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Kinetics of folding of Escheri ...... formation in a planar bilayer.
@ast
Kinetics of folding of Escheri ...... formation in a planar bilayer.
@en
type
label
Kinetics of folding of Escheri ...... formation in a planar bilayer.
@ast
Kinetics of folding of Escheri ...... formation in a planar bilayer.
@en
prefLabel
Kinetics of folding of Escheri ...... formation in a planar bilayer.
@ast
Kinetics of folding of Escheri ...... formation in a planar bilayer.
@en
P356
P1433
P1476
Kinetics of folding of Escheri ...... formation in a planar bilayer.
@en
P2093
Zakharian E
P304
P356
10.1021/BI047278E
P407
P577
2005-05-01T00:00:00Z