Nonmicellar systems for solution NMR spectroscopy of membrane proteins - Wikidata - awgldk - TriplyDB

Nonmicellar systems for solution NMR spectroscopy of membrane proteins

Nonmicellar systems for solution NMR spectroscopy of membrane proteins

http://www.wikidata.org/entity/Q34086382

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The magic of bicelles lights up membrane protein structure A saposin-lipoprotein nanoparticle system for membrane proteins.Nanodiscs allow phage display selection for ligands to non-linear epitopes on membrane proteins Covalently circularized nanodiscs for studying membrane proteins and viral entry.How amphipols embed membrane proteins: global solvent accessibility and interaction with a flexible protein terminus.NMR structures of polytopic integral membrane proteins.Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces Long-term stability of a vaccine formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis Membrane protein structure and dynamics from NMR spectroscopy.Reconstitution of integral membrane proteins into isotropic bicelles with improved sample stability and expanded lipid composition profile Construction of covalent membrane protein complexes and high-throughput selection of membrane mimics.Synthesis, characterization and applications of a perdeuterated amphipol.The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media.EmrE dimerization depends on membrane environment.Sulfonated amphipols: synthesis, properties, and applications.Antiparallel EmrE exports drugs by exchanging between asymmetric structures Nanodiscs as a new tool to examine lipid-protein interactions.Characterizing the structure of lipodisq nanoparticles for membrane protein spectroscopic studies.Detergent/nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain.Amphipols for each season.Nano-size uni-lamellar lipodisq improved in situ auto-phosphorylation analysis of E. coli tyrosine kinase using (19)F nuclear magnetic resonance.Real-time and label-free analysis of binding thermodynamics of carbohydrate-protein interactions on unfixed cancer cell surfaces using a QCM biosensor.When detergent meets bilayer: birth and coming of age of lipid bicelles.Helical membrane protein conformations and their environment Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.A view into the blind spot: solution NMR provides new insights into signal transduction across the lipid bilayer.New amphiphiles for membrane protein structural biology.High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument.Solution NMR studies of peptide-lipid interactions in model membranes.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?A helix heterodimer in a lipid bilayer: prediction of the structure of an integrin transmembrane domain via multiscale simulations.Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility.Synthesis and characterization of pHLIP® coated gold nanoparticles Bicelles at low concentrations Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment High Yield Non-detergent Isolation of Photosystem I-Light-harvesting Chlorophyll II Membranes from Spinach Thylakoids: IMPLICATIONS FOR THE ORGANIZATION OF THE PS I ANTENNAE IN HIGHER PLANTS.From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins.Nanodiscs in the studies of membrane-bound cytochrome P450 enzymes.Application of methyl-TROSY to a large paramagnetic membrane protein without perdeuteration: 13C-MMTS-labeled NADPH-cytochrome P450 oxidoreductase.Dodecyl-β-melibioside Detergent Micelles as a Medium for Membrane Proteins.

P2860

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P2860

Nonmicellar systems for solution NMR spectroscopy of membrane proteins

http://www.wikidata.org/entity/Q34086382

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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type

label

Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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prefLabel

Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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J.SBI.2010.05.006

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Current Opinion in Structural Biology

P1476

Nonmicellar systems for solution NMR spectroscopy of membrane proteins

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P2093

Gerhard Wagner

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

Thomas Raschle

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P2860

The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling

Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state

A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor

Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Redox potential control by drug binding to cytochrome P450 3A4

The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins.

Solution NMR mapping of water-accessible residues in the transmembrane beta-barrel of OmpX.

Amphipathic polymers: tools to fold integral membrane proteins to their active form.

NMR study of a membrane protein in detergent-free aqueous solution.

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471-479

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scholarly article

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10.1016/J.SBI.2010.05.006

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4

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20

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Sebastian Hiller

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2010-08-01T00:00:00Z

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44694886

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