Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
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Crystal structure of a two-subunit TrkA octameric gating ring assemblyMembrane simulations of OpcA: gating in the loops?Structure of outer membrane protein G by solution NMR spectroscopy.Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteinsThe Crystal Structure of OprG from Pseudomonas aeruginosa, a Potential Channel for Transport of Hydrophobic Molecules across the Outer MembraneLigand-gated diffusion across the bacterial outer membraneMolecular dynamics simulation studies of GLUT4: substrate-free and substrate-induced dynamics and ATP-mediated glucose transport inhibitionExpression of the ompATb operon accelerates ammonia secretion and adaptation of Mycobacterium tuberculosis to acidic environmentsBlock and boost DNA transfer: opposite roles of OmpA in natural and artificial transformation of Escherichia coliEngineering a Novel Porin OmpGF Via Strand Replacement from Computational Analysis of Sequence Motif.Quasithermodynamic contributions to the fluctuations of a protein nanopore.Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins.Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.Molecular basis of usher pore gating in Escherichia coli pilus biogenesisNMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel.An outer membrane protein undergoes enthalpy- and entropy-driven transitionsHydrophobic mismatch and lipid sorting near OmpA in mixed bilayers: atomistic and coarse-grained simulations.The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel.The transition state for folding of an outer membrane protein.Fast-time scale dynamics of outer membrane protein A by extended model-free analysis of NMR relaxation data.Elucidating in vivo structural dynamics in integral membrane protein by hydroxyl radical footprintingOne membrane protein, two structures and six environments: a comparative molecular dynamics simulation study of the bacterial outer membrane protein PagP.Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro.Outer membrane protein G: Engineering a quiet pore for biosensing.Outer Membrane Protein Folding and Topology from a Computational Transfer Free Energy Scale.Functional dynamics in the voltage-dependent anion channelOvercoming hysteresis to attain reversible equilibrium folding for outer membrane phospholipase A in phospholipid bilayers.Establishing knowledge on the sequence arrangement pattern of nucleated protein folding.Global redesign of a native β-barrel scaffold.Two salt bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function.Ins and outs of major facilitator superfamily antiporters.Structural model of a putrescine-cadaverine permease from Trypanosoma cruzi predicts residues vital for transport and ligand binding.Computational studies of membrane proteins: models and predictions for biological understanding.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Identification of opsA, a gene involved in solute stress mitigation and survival in soil, in the polycyclic aromatic hydrocarbon-degrading bacterium Novosphingobium sp. strain LH128.Refining the treatment of membrane proteins by coarse-grained models.Oligo-(R)-3-hydroxybutyrate modification of sorting signal enables pore formation by Escherichia coli OmpA.Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.STIM1 activates CRAC channels through rotation of the pore helix to open a hydrophobic gate.Full-Length OmpA: Structure, Function, and Membrane Interactions Predicted by Molecular Dynamics Simulations
P2860
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P2860
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
@ast
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
@en
type
label
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
@ast
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
@en
prefLabel
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
@ast
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
@en
P2860
P356
P1476
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.
@en
P2093
Gabor Szabo
Lukas K Tamm
P2860
P2888
P304
P356
10.1038/NCHEMBIO827
P50
P577
2006-10-15T00:00:00Z