Norwalk virus assembly and stability monitored by mass spectrometry. - Test2 - elhamkhani - TriplyDB

Norwalk virus assembly and stability monitored by mass spectrometry.

Norwalk virus assembly and stability monitored by mass spectrometry.

http://www.wikidata.org/entity/Q34121907

about

The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Principles of virus structural organization Studying 18 MDa virus assemblies with native mass spectrometry Robotically assisted titration coupled to ion mobility-mass spectrometry reveals the interface structures and analysis parameters critical for multiprotein topology mapping Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent.Sampling protein form and function with the atomic force microscope.Inactivation of the Tulane virus, a novel surrogate for the human norovirus Structure of a Venezuelan equine encephalitis virus assembly intermediate isolated from infected cells 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 Identifying carbohydrate ligands of a norovirus P particle using a catch and release electrospray ionization mass spectrometry assay.Qualitative and quantitative analysis of the binding of GII.4 norovirus variants onto human blood group antigens.Affinities of human histo-blood group antigens for norovirus capsid protein complexes.Analysis of a common cold virus and its subviral particles by gas-phase electrophoretic mobility molecular analysis and native mass spectrometry Characterization and control of surfactant-mediated Norovirus interactions.Native tandem and ion mobility mass spectrometry highlight structural and modular similarities in clustered-regularly-interspaced shot-palindromic-repeats (CRISPR)-associated protein complexes from Escherichia coli and Pseudomonas aeruginosa Capturing protein structural kinetics by mass spectrometry.Studying protein-protein affinity and immobilized ligand-protein affinity interactions using MS-based methods.Mass spectrometry based tools to investigate protein-ligand interactions for drug discovery.A critical review of methods for detecting human noroviruses and predicting their infectivity.The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis.Measuring masses of large biomolecules and bioparticles using mass spectrometric techniques.Next generation vaccines and vectors: Designing downstream processes for recombinant protein-based virus-like particles.Detection of late intermediates in virus capsid assembly by charge detection mass spectrometry.Persistence and Elimination of Human Norovirus in Food and on Food Contact Surfaces: A Critical Review.Norwalk Virus Minor Capsid Protein VP2 Associates within the VP1 Shell Domain.Proteomics and integrative omic approaches for understanding host-pathogen interactions and infectious diseases.Prestress strengthens the shell of Norwalk virus nanoparticles.Folding of Protein Ions in the Gas Phase after Cation-to-Anion Proton-Transfer Reactions Zeta Potential and Aggregation of Virus-Like Particle of Human Norovirus and Feline Calicivirus Under Different Physicochemical Conditions.Using ion mobility spectrometry-mass spectrometry to decipher the conformational and assembly characteristics of the hepatitis B capsid protein.Staying Alive: Measuring Intact Viable Microbes with Electrospray Ionization Mass Spectrometry.Probing bunyavirus N protein oligomerisation using mass spectrometry.Uncovering the stoichiometry of Pyrococcus furiosus RNase P, a multi-subunit catalytic ribonucleoprotein complex, by surface-induced dissociation and ion mobility mass spectrometry.Surface induced dissociation yields quaternary substructure of refractory noncovalent phosphorylase B and glutamate dehydrogenase complexes.Effects of Solution Structure on the Folding of Lysozyme Ions in the Gas Phase.

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P2860

Norwalk virus assembly and stability monitored by mass spectrometry.

http://www.wikidata.org/entity/Q34121907

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին 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

@zh-hant

2010年論文

@zh-hk

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

Norwalk virus assembly and stability monitored by mass spectrometry.

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Norwalk virus assembly and stability monitored by mass spectrometry.

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Norwalk virus assembly and stability monitored by mass spectrometry.

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type

label

Norwalk virus assembly and stability monitored by mass spectrometry.

@ast

Norwalk virus assembly and stability monitored by mass spectrometry.

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Norwalk virus assembly and stability monitored by mass spectrometry.

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prefLabel

Norwalk virus assembly and stability monitored by mass spectrometry.

@ast

Norwalk virus assembly and stability monitored by mass spectrometry.

@en

Norwalk virus assembly and stability monitored by mass spectrometry.

@nl

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MCP.M900620-MCP200

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Molecular & Cellular Proteomics

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Norwalk virus assembly and stability monitored by mass spectrometry

@en

P2093

Esther van Duijn

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

Gijs J L Wuite

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

Glen K Shoemaker

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

Marian Baclayon

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

Mary K Estes

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Sue E Crawford

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P2860

Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3

Bacteriophage capsids: tough nanoshells with complex elastic properties

X-ray crystallographic structure of the Norwalk virus capsid

Probing genuine strong interactions and post-translational modifications in the heterogeneous yeast exosome protein complex.

Three-dimensional structure of baculovirus-expressed Norwalk virus capsids

Three-dimensional ion mobility/TOFMS analysis of electrosprayed biomolecules.

Subunit architecture of intact protein complexes from mass spectrometry and homology modeling.

Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.

The familiar and the unexpected in structures of icosahedral viruses.

Structural requirements for the assembly of Norwalk virus-like particles

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1742-1751

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scholarly article

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10.1074/MCP.M900620-MCP200

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8

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9

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Albert J.R. Heck

Charlotte Uetrecht

B.V.Venkataram Prasad

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2010-04-22T00:00:00Z

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20418222

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2938053

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