Sonication of proteins causes formation of aggregates that resemble amyloid.
about
De novo generation of prion strainsPlatelets retain high levels of active plasminogen activator inhibitor 1Conformational 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 sclerosisDeciphering 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.
P2860
Q28249136-3E39BC10-E9F4-446D-B92B-39AD0D4123D2Q28743269-07C01E0F-7B42-437E-B98D-D824F1424BC5Q30375808-B2EE6DE3-9031-4CFA-BF6D-0A12F9E9A791Q30378508-441146C7-6A2A-4486-B517-660755B7F4F7Q30379795-D12FF0EC-551B-4903-BE64-809FD41E3DDAQ30457664-2EB09C5E-6915-493F-B723-8C525A366773Q30459645-CB2ADFEE-5BA7-4EBA-A5F0-177DDFA164C0Q30479487-BAFD514B-5F15-46E4-B61E-FC362F98413CQ30574912-E8BE38B7-2876-4F95-8138-3A5256BFE019Q33398651-5626A881-4048-4716-A2BF-A3116624A087Q33614068-9216B935-4D6D-4D3D-81E0-5C3A61F63260Q34071628-133FEB52-087C-4360-9C8A-724D01D76316Q34438898-2A0773BB-C085-4BAB-8D8F-11E50E3FD189Q34559100-F0563F39-260F-4AAB-93E3-AD78361B3A17Q34572921-779764AD-967B-4583-B9DA-F96004F024FBQ35146724-9A29D52E-37BE-468D-97FF-3529C2A6344BQ35254110-1BE19EC3-9802-4F1F-BF8B-8ECACDA03FCAQ35968334-EA106724-584A-4D58-9637-B9FF529C980FQ36175904-CE769BB4-9E62-44F2-8EE6-F8C165F21DC3Q36398045-F209B9C3-293A-4CA3-8EC7-7EA63E824CB5Q36436203-7F50E775-16B0-4D74-9479-A7F056B4F1F7Q37791785-E9DE82E8-0FC0-44B8-B570-2C67C5D896FBQ38091029-54603F6D-09C7-4A3C-888F-A95A72C9AC5DQ38115814-6FBAE5EF-C2E4-48FE-B560-A38529D1345CQ38631878-74D8781E-14E1-4950-BF11-55D62EE3B764Q38991962-66D1AC2B-A8B9-4735-8DB0-766BEFC3E399Q39004466-9FF3AF80-2DF6-4A10-9611-DC470C5B485DQ40018633-A01A7F90-3884-441E-9D37-504F9573E446Q40182949-1742D20D-C244-453E-8FBC-A13FEE7AB231Q41057408-0822F472-6B57-47C8-887B-D65978FFDEDEQ41195349-C1B9C3AA-DEB1-4330-BD3A-984CA869A4CBQ41964030-A095F0B1-D973-49B6-A574-CB26A07C2A6EQ42176816-0CE774ED-B4E8-4CC5-B8EE-48F7473B1457Q42279346-B39EE481-EB63-428C-9C92-797113098E5CQ42830746-53EA22AC-A839-45CE-A5A5-06526A06F3F5Q43256474-9FD50A80-6C5F-4BE3-8395-DB1E1E6D3C20Q46851121-F49A4913-210E-4C72-AFE6-C10C24FE2628Q47126292-F63FAF80-9918-4D5D-8F64-219A62757D22Q47222549-DDDA0067-35E2-4029-B799-339B06BCA4BBQ47330886-933BE4B6-5FD1-4587-B52E-62AD4292972B
P2860
Sonication of proteins causes formation of aggregates that resemble amyloid.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
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
P2093
P2860
P356
P1433
P1476
Sonication of proteins causes formation of aggregates that resemble amyloid.
@en
P2093
Elizabeth M Meiering
Guenter A Scholz
James R Lepock
Jessica A O Rumfeldt
Peter B Stathopulos
Young-Mi Hwang
P2860
P304
P356
10.1110/PS.04831804
P577
2004-09-30T00:00:00Z