Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles. - Wikidata - wikimedia - TriplyDB

Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles.

Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles.

http://www.wikidata.org/entity/Q35052071

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HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions HIV-1 Vpu targets cell surface markers CD4 and BST-2 through distinct mechanisms Magic angle spinning NMR of viruses The magic of bicelles lights up membrane protein structure NMR structures of membrane proteins in phospholipid bilayers NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles NMR Structure and Ion Channel Activity of the p7 Protein from Hepatitis C Virus Binding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural Study Atomistic detailed mechanism and weak cation-conducting activity of HIV-1 Vpu revealed by free energy calculations Assignment of oriented sample NMR resonances from a three transmembrane helix protein.Solution NMR of signal peptidase, a membrane protein.Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.Solid state NMR and protein-protein interactions in membranes Helical distortion in tryptophan- and lysine-anchored membrane-spanning alpha-helices as a function of hydrophobic mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled alanines method Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.Impact of histidine residues on the transmembrane helices of viroporins.Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Antiviral activity of the interferon-induced cellular protein BST-2/tetherin.Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.A resonance assignment method for oriented-sample solid-state NMR of proteins On the combined analysis of ²H and ¹⁵N/¹H solid-state NMR data for determination of transmembrane peptide orientation and dynamics Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers Nanotube array method for studying lipid-induced conformational changes of a membrane protein by solid-state NMR.A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field Molecular dynamics simulations reveal the HIV-1 Vpu transmembrane protein to form stable pentamers.Membrane Anchoring by a C-terminal Tryptophan Enables HIV-1 Vpu to Displace Bone Marrow Stromal Antigen 2 (BST2) from Sites of Viral Assembly Interactions of interleukin-8 with the human chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy.Transmembrane domain determinants of CD4 Downregulation by HIV-1 Vpu.'q-Titration' of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy.A Practical Implicit Membrane Potential for NMR Structure Calculations of Membrane Proteins.An efficient (1)H/(31)P double-resonance solid-state NMR probe that utilizes a scroll coil Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better.Solid-state NMR spectroscopy of a membrane protein in biphenyl phospholipid bicelles with the bilayer normal parallel to the magnetic field.Magnetically aligned bicelles to study the orientation of lipophilic ligands in membrane bilayers.NMR studies of membrane proteins.Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.Optimization of purification and refolding of the human chemokine receptor CXCR1 improves the stability of proteoliposomes for structure determination Bicelles: A natural 'molecular goniometer' for structural, dynamical and topological studies of molecules in membranes.Detergent optimized membrane protein reconstitution in liposomes for solid state NMR.

P2860

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P2860

Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles.

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2006 nî lūn-bûn

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2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2006年の論文

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Biophysical Journal

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Three-dimensional structure of ...... aligned phospholipid bicelles.

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Alexander A Nevzorov

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Anna A De Angelis

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Chin H Wu

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Sang Ho Park

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Stanley J Opella

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P2860

Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy

Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints

Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy

Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

MOLMOL: a program for display and analysis of macromolecular structures

Membrane protein folding and stability: physical principles

A solid-state NMR index of helical membrane protein structure and topology.

Dipolar waves as NMR maps of protein structure

High-resolution NMR spectroscopy of membrane proteins in aligned bicelles.

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transmembrane protein

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