Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions. - sprookjes - yvandenbroek - TriplyDB

Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.

Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.

http://www.wikidata.org/entity/Q33790418

about

The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Mass spectrometry--from peripheral proteins to membrane motors Optimized purification of a heterodimeric ABC transporter in a highly stable form amenable to 2-D crystallization Tuning the drug efflux activity of an ABC transporter in vivo by in vitro selected DARPin binders Structural model of FeoB, the iron transporter from Pseudomonas aeruginosa, predicts a cysteine lined, GTP-gated pore Hoechst 33342 Is a Hidden "Janus" amongst Substrates for the Multidrug Efflux Pump LmrP Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.Dodecyl maltoside protects membrane proteins in vacuo.Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes.Revealing Higher Order Protein Structure Using Mass Spectrometry.Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent.The 'sticky business' of cleaning gas-phase membrane proteins: a detergent oriented perspective.Traveling-wave Ion Mobility-Mass Spectrometry Reveals Additional Mechanistic Details in the Stabilization of Protein Complex Ions through Tuned Salt Additives.Dramatically stabilizing multiprotein complex structure in the absence of bulk water using tuned Hofmeister salts.A multidrug ABC transporter with a taste for salt.Toward atomic force microscopy and mass spectrometry to visualize and identify lipid rafts in plasmodesmata Native MS: an 'ESI' way to support structure- and fragment-based drug discovery.Top Down proteomics: facts and perspectives.Native capillary isoelectric focusing for the separation of protein complex isoforms and subcomplexes Norwalk virus assembly and stability monitored by mass spectrometry.Dynamic protein ligand interactions--insights from MS.Sizing up large protein complexes by electrospray ionisation-based electrophoretic mobility and native mass spectrometry: morphology selective binding of Fabs to hepatitis B virus capsids Native electrospray and electron-capture dissociation FTICR mass spectrometry for top-down studies of protein assemblies.Mass spectrometry: come of age for structural and dynamical biology.Applying mass spectrometry to study non-covalent biomolecule complexes.Joining forces: integrating proteomics and cross-linking with the mass spectrometry of intact complexes.High-resolution mass spectrometry of small molecules bound to membrane proteins Probing Asymmetric Charge Partitioning of Protein Oligomers during Tandem Mass Spectrometry.Native mass spectrometry characterization of intact nanodisc lipoprotein complexes.Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.Structural and functional analysis of the native peripherin-ROM1 complex isolated from photoreceptor cells.Detergent-free mass spectrometry of membrane protein complexes.Interpretation and deconvolution of nanodisc native mass spectra.Mass spectrometry accelerates membrane protein analysis.Finding the right balance: a personal journey from individual proteins to membrane-embedded motors: based on a lecture delivered at the 36th FEBS Congress in Torino, Italy, June 2011.Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry.Protein-protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches.Investigating macromolecular complexes using top-down mass spectrometry.A new window into the molecular physiology of membrane proteins.

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Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.

http://www.wikidata.org/entity/Q33790418

description

2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2009 թվականի հուլիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Mass spectrometry of membrane ...... toichiometry and interactions.

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Mass spectrometry of membrane ...... toichiometry and interactions.

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Mass spectrometry of membrane ...... toichiometry and interactions.

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Mass spectrometry of membrane ...... toichiometry and interactions.

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Mass spectrometry of membrane ...... toichiometry and interactions.

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Mass spectrometry of membrane ...... toichiometry and interactions.

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Mass spectrometry of membrane ...... toichiometry and interactions.

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P2093

Adrian R Walmsley

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Alex Welch

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

Markus A Seeger

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

Min Zhou

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

Nelson P Barrera

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

Ricardo Núñez Miguel

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

Shoshanna C Isaacson

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

Vladimir M Korkhov

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

P2860

PROCHECK: a program to check the stereochemical quality of protein structures

The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism

X-ray structure of EmrE supports dual topology model.

Comparative protein modelling by satisfaction of spatial restraints

FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution

JOY: protein sequence-structure representation and analysis.

The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids.

The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 A resolution

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585-587

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scholarly article

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10.1038/NMETH.1347

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8

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6

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Christopher G. Tate

Vassiliy N. Bavro

Henrietta Venter

Carol V. Robinson

Theresia A Schaedler

Hendrik W van Veen

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2009-07-05T00:00:00Z

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1026056322

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19578383

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