Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level. - Wikidata - wikimedia - TriplyDB

Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level.

Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level.

http://www.wikidata.org/entity/Q34098577

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Mass spectrometry-based methods to study protein architecture and dynamics NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286 Extraction of local hydrogen exchange data from HDX CAD MS measurements by deconvolution of isotopic distributions of fragment ions.Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation Controlling hydrogen scrambling in multiply charged protein ions during collisional activation: implications for top-down hydrogen/deuterium exchange MS utilizing collisional activation in the gas phase.A new approach to explore the impact of freeze-thaw cycling on protein structure: hydrogen/deuterium exchange mass spectrometry (HX-MS).Post-translational modifications in PrP expand the conformational diversity of prions in vivo Advanced mass spectrometry-based methods for the analysis of conformational integrity of biopharmaceutical products Many overlapping peptides for protein hydrogen exchange experiments by the fragment separation-mass spectrometry method.Insight into the structure of amyloid fibrils from the analysis of globular proteins.Granular assembly of alpha-synuclein leading to the accelerated amyloid fibril formation with shear stress.H/D exchange and mass spectrometry in the studies of protein conformation and dynamics: is there a need for a top-down approach?Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.Probing the conformation of a prion protein fibril with hydrogen exchange.Emerging mass spectrometry-based approaches to probe protein-receptor interactions: focus on overcoming physiological barriers DNA binding restricts the intrinsic conformational flexibility of methyl CpG binding protein 2 (MeCP2).Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.Structural determinants of phenotypic diversity and replication rate of human prions.Segmental polymorphism in a functional amyloid.Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange Dynamical Behavior of Human α-Synuclein Studied by Quasielastic Neutron Scattering.High Resolution Mapping of Bactericidal Monoclonal Antibody Binding Epitopes on Staphylococcus aureus Antigen MntC.ETD in a traveling wave ion guide at tuned Z-spray ion source conditions allows for site-specific hydrogen/deuterium exchange measurements Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.Core sequence of PAPf39 amyloid fibrils and mechanism of pH-dependent fibril formation: the role of monomer conformation Hydrogen exchange and mass spectrometry: A historical perspective.Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Molecular structures of amyloid and prion fibrils: consensus versus controversy Comparison of apoA-I helical structure and stability in discoidal and spherical HDL particles by HX and mass spectrometry.Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease Using leucine zipper to facilitate alpha-synuclein assembly.Novel therapeutic strategies for the treatment of protein-misfolding diseases.Modulating the Amyloidogenesis of α-Synuclein A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation Differential accessibilities of dibasic prohormone processing sites of proenkephalin to the aqueous environment revealed by H-D exchange mass spectrometry.Structural dynamics of soluble chloride intracellular channel protein CLIC1 examined by amide hydrogen-deuterium exchange mass spectrometry.Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange.

P2860

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P2860

Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level.

http://www.wikidata.org/entity/Q34098577

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2005 nî lūn-bûn

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Structure and properties of al ...... mined at the amino acid level.

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Charyl Del Mar

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Eric A Greenbaum

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Leland Mayne

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S Walter Englander

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Virgil L Woods

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P2860

Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease

The structural basis of protein folding and its links with human disease

Structure of the cross-beta spine of amyloid-like fibrils

Protein complexes studied by NMR spectroscopy

Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils

Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange

Primary structure effects on peptide group hydrogen exchange

Investigating protein structure and dynamics by hydrogen exchange MS.

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