Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening. - Wikidata - wikimedia - TriplyDB

Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

http://www.wikidata.org/entity/Q30441900

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Crystal structure of a two-subunit TrkA octameric gating ring assembly Membrane 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 proteins The Crystal Structure of OprG from Pseudomonas aeruginosa, a Potential Channel for Transport of Hydrophobic Molecules across the Outer Membrane Ligand-gated diffusion across the bacterial outer membrane Molecular dynamics simulation studies of GLUT4: substrate-free and substrate-induced dynamics and ATP-mediated glucose transport inhibition Expression of the ompATb operon accelerates ammonia secretion and adaptation of Mycobacterium tuberculosis to acidic environments Block and boost DNA transfer: opposite roles of OmpA in natural and artificial transformation of Escherichia coli Engineering 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 biogenesis NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel.An outer membrane protein undergoes enthalpy- and entropy-driven transitions Hydrophobic 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 footprinting One 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 channel Overcoming 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

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P2860

Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

http://www.wikidata.org/entity/Q30441900

description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2006年の論文

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Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

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Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

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Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

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Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

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Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

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Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

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Nature Chemical Biology

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Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening.

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Gabor Szabo

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Lukas K Tamm

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P2860

High-resolution structure of the OmpA membrane domain

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy

Are buried salt bridges important for protein stability and conformational specificity?

Structure of the outer membrane protein A transmembrane domain

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme

The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

Cation-pi interactions in structural biology

Molecular basis of bacterial outer membrane permeability

Modeling and simulations of a bacterial outer membrane protein: OprF from Pseudomonas aeruginosa.

Structure and function of bacterial outer membrane proteins: barrels in a nutshell.

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627-635

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10.1038/NCHEMBIO827

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11

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2

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17041590

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