Immunoaffinity purification and neutralization of scrapie prion infectivity
about
Prion hypothesis: the end of the controversy?PrionsAntihypertensive drug guanabenz is active in vivo against both yeast and mammalian prionsImmunopurification of pathological prion protein aggregatesMolecular mass, biochemical composition, and physicochemical behavior of the infectious form of the scrapie precursor protein monomerPrion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoformGeneration of antisera to purified prions in lipid raftsPrimary structure of prion protein may modify scrapie isolate propertiesInterventional strategies against prion diseases.Human prions and plasma lipoproteins.Structure and polymorphism of the mouse prion protein gene.Could immunomodulation be used to prevent prion diseases?Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58.A kinetic model for amyloid formation in the prion diseases: importance of seeding.Prion protein-specific antibodies for therapeutic intervention of transmissible spongiform encephalopathies.Molecular biology and pathology of scrapie and the prion diseases of humans.Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis.Molecular biology and transgenetics of prion diseases.Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysisMolecular location of a species-specific epitope on the hamster scrapie agent protein.Recent developments in mucosal vaccines against prion diseases.N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state.Genetics and polymorphism of the mouse prion gene complex: control of scrapie incubation time.Detection and control of prion diseases in food animals.Identification and removal of proteins that co-purify with infectious prion protein improves the analysis of its secondary structure.Comparative profiling of highly enriched 22L and Chandler mouse scrapie prion protein preparations.Regional mapping of prion proteins in brain.Beef and bovine spongiform encephalopathy: the risk persists.Cells and prions: a license to replicate.Therapeutic interventions ameliorating prion disease.Prion liposomes.Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus.Immunotherapy for prion diseases: opportunities and obstacles.Immunotherapeutic approaches in prion disease: progress, challenges and potential directions.Transmissible encephalopathies in animals.Proteomics applications in prion biology and structure.Brain delivery of AAV9 expressing an anti-PrP monovalent antibody delays prion disease in mice.Prions, beta-sheets and transmissible dementias: is there still something missing?Prion protein isoforms, a convergence of biological and structural investigations.The neurochemistry of prion diseases.
P2860
Q24599702-13057EE7-A5F0-4EA7-8F2F-9A5C54385DE0Q24633319-301B474F-BB91-48BF-9F81-77865ECE613EQ28472560-68120FEF-4EDA-4102-89C7-F00767FCD441Q33516017-E0A84CD3-DF81-408F-9649-F79B801357B2Q33752032-60F6CED2-7865-4FF6-8FA4-50D303EC8163Q33761104-AFFE5313-0899-433A-9644-D73B299BD013Q34102660-3BE26A38-C2A7-4830-A29F-116D0B81C916Q34307605-F0A2F154-C9CB-476D-AF92-5B08CDA110F6Q34389564-4235AD99-563E-4E8B-80FC-7C5CF307481EQ34983985-4DCEAAA5-22BA-426F-994F-200A79902904Q35573850-DE2DDA17-3537-422D-98E7-EE9AB75CF6C4Q35875915-9522E44F-EDD5-4F2E-83EC-4DBC87DE5FA4Q35921884-1BDEFBA9-7686-440D-96F9-D48B5423F68BQ36385621-2FE07E68-03DC-43F8-8D73-078C339662FFQ36407253-F9CC8171-1D6C-4E86-9608-84DA0763943FQ36477026-A7B1F6DC-1AF0-4C45-85DF-C2A602DA8734Q36521947-4ECE2A84-BA71-4E61-8BF9-DFE3E1924803Q36538997-C2605280-4B81-408A-967E-0F1EC0355345Q36682161-BC0A4329-2F5D-4F04-A84A-DAD523CFF871Q36701217-77A62C12-1A2F-436F-9781-B72BB2B22B45Q36728797-2FD1592A-B45D-4D01-B7BC-EC6342B52170Q36828108-93419756-6D0F-4388-83C4-021966E373BFQ36851207-D91C14DF-A82E-487D-890B-ADF1067125E1Q36857700-5F61E723-12EF-4ED5-BC9F-327A9CE4C9D9Q37056200-59AFE9D7-1BD4-4315-99D5-0542FD694958Q37091434-7E31D0D8-47E4-4673-899A-F437CA9E55ECQ37157028-CC49A545-9435-47E4-92BD-DA177D2AD8AAQ37397212-E8FFB172-ACE3-4FA2-B73B-987B9550FC0FQ37520006-B5BC95CD-8DAD-4729-A92F-48EDC8502C00Q37557690-1480C346-2809-40B6-BBE1-8C5C6985416DQ37581303-E797918A-9FA6-428E-8D07-C2DDA37DBC59Q37693769-0EA2FB15-354D-411E-A3E0-9E60A9F7AD98Q37773260-9E0E1CCA-3E41-44F5-BF9B-265B77549003Q38104409-00358BA7-40BB-4614-84BE-0D0D61A08766Q38145149-C04F512E-8086-4BD9-A647-B023940E9C20Q38385905-2F36BFDB-F1E5-4445-A61D-8DDD92ADA1F8Q39331076-2F3CA68C-3B1D-43A6-885C-57196C8E2859Q40372882-7A61B932-72F7-4960-9008-A9A6B666739CQ40464138-DD25A2A6-A5EA-4BB6-B107-90451CB7CE89Q40618333-BDB138B2-451A-435D-B9E8-E6FA0D1042DE
P2860
Immunoaffinity purification and neutralization of scrapie prion infectivity
description
1988 nî lūn-bûn
@nan
1988 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Immunoaffinity purification and neutralization of scrapie prion infectivity
@ast
Immunoaffinity purification and neutralization of scrapie prion infectivity
@en
type
label
Immunoaffinity purification and neutralization of scrapie prion infectivity
@ast
Immunoaffinity purification and neutralization of scrapie prion infectivity
@en
prefLabel
Immunoaffinity purification and neutralization of scrapie prion infectivity
@ast
Immunoaffinity purification and neutralization of scrapie prion infectivity
@en
P2093
P2860
P356
P1476
Immunoaffinity purification and neutralization of scrapie prion infectivity
@en
P2093
P2860
P304
P356
10.1073/PNAS.85.18.6617
P407
P577
1988-09-01T00:00:00Z