Protonation drives the conformational switch in the multidrug transporter LmrP. - Wikidata - awgldk - TriplyDB

Protonation drives the conformational switch in the multidrug transporter LmrP.

Protonation drives the conformational switch in the multidrug transporter LmrP.

http://www.wikidata.org/entity/Q36567205

about

Energy coupling mechanisms of MFS transporters Hoechst 33342 Is a Hidden "Janus" amongst Substrates for the Multidrug Efflux Pump LmrP TMalphaDB and TMbetaDB: web servers to study the structural role of sequence motifs in α-helix and β-barrel domains of membrane proteins.Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy.A Straightforward Approach to the Analysis of Double Electron-Electron Resonance Data Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter.Conformational cycle and ion-coupling mechanism of the Na+/hydantoin transporter Mhp1.Functionally important carboxyls in a bacterial homologue of the vesicular monoamine transporter (VMAT).Structure and pH-induced structural rearrangements of the putative multidrug efflux pump EmrD in liposomes probed by site-directed spin labeling.Emulating proton-induced conformational changes in the vesicular monoamine transporter VMAT2 by mutagenesis.EPR characterization of Mn(ii) complexes for distance determination with pulsed dipolar spectroscopy.Lipids modulate the conformational dynamics of a secondary multidrug transporter.A Numbering System for MFS Transporter Proteins.Singular Value Decomposition Method to Determine Distance Distributions in Pulsed Dipolar Electron Spin Resonance.Mechanism of Substrate Translocation in an Alternating Access Transporter.A New Wavelet Denoising Method for Experimental Time-Domain Signals: Pulsed Dipolar Electron Spin Resonance.Direct protein-lipid interactions shape the conformational landscape of secondary transporters

P2860

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P2860

Protonation drives the conformational switch in the multidrug transporter LmrP.

http://www.wikidata.org/entity/Q36567205

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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2013年论文

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2013年论文

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name

Protonation drives the conformational switch in the multidrug transporter LmrP.

@ast

Protonation drives the conformational switch in the multidrug transporter LmrP.

@en

type

label

Protonation drives the conformational switch in the multidrug transporter LmrP.

@ast

Protonation drives the conformational switch in the multidrug transporter LmrP.

@en

prefLabel

Protonation drives the conformational switch in the multidrug transporter LmrP.

@ast

Protonation drives the conformational switch in the multidrug transporter LmrP.

@en

P1433

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P2860

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P932

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P356

P1433

Nature Chemical Biology

P1476

Protonation drives the conformational switch in the multidrug transporter LmrP.

@en

P2093

Chloé Martens

http://www.w3.org/2001/XMLSchema#string

Cédric Govaerts

http://www.w3.org/2001/XMLSchema#string

Hassane S Mchaourab

http://www.w3.org/2001/XMLSchema#string

Jean-Marie Ruysschaert

http://www.w3.org/2001/XMLSchema#string

Matthieu Masureel

http://www.w3.org/2001/XMLSchema#string

Richard A Stein

http://www.w3.org/2001/XMLSchema#string

Smriti Mishra

http://www.w3.org/2001/XMLSchema#string

P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Efflux-mediated drug resistance in bacteria: an update

Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli

Structural determination of wild-type lactose permease

Structure of a fucose transporter in an outward-open conformation

Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2

Structures of a Na+-coupled, substrate-bound MATE multidrug transporter

Crystal structure of a bacterial homologue of glucose transporters GLUT1-4

UCSF Chimera--a visualization system for exploratory research and analysis

Structure of the multidrug transporter EmrD from Escherichia coli

P2888

P304

149-155

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P31

scholarly article

P356

10.1038/NCHEMBIO.1408

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P433

2

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P478

10

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P50

Jean-Marie Ruysschaert

P577

2013-12-08T00:00:00Z

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P698

24316739

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P932

4749020

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