Sonication of proteins causes formation of aggregates that resemble amyloid. - Wikidata - awgldk - TriplyDB

Sonication of proteins causes formation of aggregates that resemble amyloid.

Sonication of proteins causes formation of aggregates that resemble amyloid.

http://www.wikidata.org/entity/Q42078881

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De novo generation of prion strains Platelets retain high levels of active plasminogen activator inhibitor 1 Conformational transitions induced by in vitro macromolecular crowding lead to the amyloidogenesis of buffalo heart cystatin.Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils.Probing insulin bioactivity in oral nanoparticles produced by ultrasonication-assisted emulsification/internal gelation.Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation.Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process.Isolation of biologically active nanomaterial (inclusion bodies) from bacterial cells.Isolation of microplastics in biota-rich seawater samples and marine organisms.Albumin fibrillization induces apoptosis via integrin/FAK/Akt pathway.Single-molecule pull-down for investigating protein-nucleic acid interactions.Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis Deciphering structural intermediates and genotoxic fibrillar aggregates of albumins: a molecular mechanism underlying for degenerative diseases.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.Structural changes of ultrasonicated bovine serum albumin revealed by hydrogen-deuterium exchange and mass spectrometry.Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPres level disparity.Nonnative protein polymers: structure, morphology, and relation to nucleation and growth.Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.Prions, proteinase K and infectivity.Structural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C).Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Devices and formulations for pulmonary vaccination.Glycation, Oxidation and Glycoxidation of IgG: A Biophysical, Biochemical, Immunological and Hematological study.Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid Protofibrils.Sonication-induced formation of size-controlled self-assemblies of amphiphilic Janus-type polymers as optical tumor-imaging agents.Contact lens physical properties and lipid deposition in a novel characterized artificial tear solution.Sensitization of K562 Leukemia Cells to Doxorubicin by the Viscum album Extract.Self-assembling diblock copolymers of poly[N-(2-hydroxypropyl)methacrylamide] and a beta-sheet peptide.A Flow-Cytometry-Based Approach to Facilitate Quantification, Size Estimation and Characterization of Sub-visible Particles in Protein Solutions.The complex fate in plasma of gadolinium incorporated into high-density lipoproteins used for magnetic imaging of atherosclerotic plaques.Sonication-induced gelation of silk fibroin for cell encapsulation.Evidence that the Human Innate Immune Peptide LL-37 may be a Binding Partner of Amyloid-β and Inhibitor of Fibril Assembly.Effect of microencapsulation shear stress on the structural integrity and biological activity of a model monoclonal antibody, trastuzumab.Shear flow promotes amyloid-{beta} fibrilization.Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR.A specific form of prefibrillar aggregates that functions as a precursor of amyloid nucleation.Formation and properties of amyloid fibrils of prion protein.

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P2860

Sonication of proteins causes formation of aggregates that resemble amyloid.

http://www.wikidata.org/entity/Q42078881

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

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name

Sonication of proteins causes formation of aggregates that resemble amyloid.

@en

Sonication of proteins causes formation of aggregates that resemble amyloid.

@nl

type

label

Sonication of proteins causes formation of aggregates that resemble amyloid.

@en

Sonication of proteins causes formation of aggregates that resemble amyloid.

@nl

prefLabel

Sonication of proteins causes formation of aggregates that resemble amyloid.

@en

Sonication of proteins causes formation of aggregates that resemble amyloid.

@nl

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P1433

Protein Science

P1476

Sonication of proteins causes formation of aggregates that resemble amyloid.

@en

P2093

Elizabeth M Meiering

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

Guenter A Scholz

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

James R Lepock

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

Jessica A O Rumfeldt

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

Peter B Stathopulos

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Young-Mi Hwang

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P2860

Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima

An NMR approach to structural proteomics.

A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain

The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease

Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set

Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).

Protein instability in poly(lactic-co-glycolic acid) microparticles.

Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae.

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3017-3027

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scholarly article

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10.1110/PS.04831804

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11

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13

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227758107

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15459333

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2286572

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