about
The physical relationship between infectivity and prion protein aggregates is strain-dependentEx vivo mammalian prions are formed of paired double helical prion protein fibrils.In situ photodegradation of incorporated polyanion does not alter prion infectivityIsolation of proteinase K-sensitive prions using pronase E and phosphotungstic acidBiology and genetics of prions causing neurodegenerationThe intriguing prion disorders.Genes contributing to prion pathogenesisHuman prion strain selection in transgenic mice.Does the central dogma still stand?Synthetic scrapie infectivity: interaction between recombinant PrP and scrapie brain-derived RNA.Nucleic acid induced unfolding of recombinant prion protein globular fragment is pH dependent.Human prions and plasma lipoproteins.Biological effects and use of PrPSc- and PrP-specific antibodies generated by immunization with purified full-length native mouse prions.Cell-free formation of misfolded prion protein with authentic prion infectivity.Insights into prion biology: integrating a protein misfolding pathway with its cellular environment.Phosphatidylinositol-glycan-phospholipase D is involved in neurodegeneration in prion diseaseContinuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes.Molecular pathogenesis of sporadic prion diseases in man.Purified and synthetic Alzheimer's amyloid beta (Aβ) prions.Mouse-adapted ovine scrapie prion strains are characterized by different conformers of PrPSc.Prions and their lethal journey to the brain.Mechanisms of prion protein assembly into amyloidPlasma membrane invaginations containing clusters of full-length PrPSc are an early form of prion-associated neuropathology in vivo.The same primary structure of the prion protein yields two distinct self-propagating states.The reconstitution of mammalian prion infectivity de novo.Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils.Cell-free propagation of prion strains.The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases.A structural overview of the vertebrate prion proteins.Changes in prion replication environment cause prion strain mutationInfectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions.Prion infection: seeded fibrillization or more?Natural and synthetic prion structure from X-ray fiber diffractionHighly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification.Allosteric function and dysfunction of the prion protein.Prions and Protein Assemblies that Convey Biological Information in Health and Disease.Oligonucleotide-based biosensors for in vitro diagnostics and environmental hazard detection.Mammalian prions and their wider relevance in neurodegenerative diseases.Developing Therapeutics for PrP Prion Diseases.Implications of peptide assemblies in amyloid diseases.
P2860
Q27315010-2A4FDCB4-1B36-4FC4-BC15-7303176BFC84Q27336314-39DF948B-609A-4674-AD11-081BA66A946DQ28477075-690A2636-CD0B-4013-AF52-DF488E2BCA2FQ28744075-241F35D7-D8E7-4FB4-9C20-D15617E46C3BQ33567229-C2BEDE02-7C72-438F-A454-DF3FA588F504Q33581653-BB46CEEC-9C5E-4D12-902E-95428781A00BQ33687685-800017A6-8438-42F8-9B67-F954DF085AA6Q34112488-39E99E10-EEC6-4073-98E2-D6BC418F3ABFQ34389862-1D9C5EA1-1EC9-40DA-90C1-D7A19CE8AB6FQ34458035-EDA7A72D-1503-4ACB-8DD5-24EE934BAC8DQ34621331-232F3AC1-0BE3-4D0C-8F45-1123B0FD6BDCQ34983985-872219BF-764A-442F-AD18-7F897A853C61Q35076872-1339699F-E41D-4074-87CD-CAD31278E851Q35127478-7D1637F3-C1C7-403C-B049-B9254A1DBCC1Q35194908-63B852BF-44D7-4733-80BF-D0262C1D7A5BQ35389677-FFC23761-63C1-42B9-98F1-4CCC88CE3B6BQ35539802-313310DB-8E29-4780-870D-3A812A4EB48DQ36005158-B2A2F54B-70B9-4CC4-BC88-325D0824B7CDQ36079533-90BB7A6D-6195-443B-9A1F-BA32242950BBQ36315505-81635642-B595-4068-974E-73A8639877A0Q36389302-FB26090D-33F3-488F-9384-0698FC197AB5Q36497270-2183AB1E-ADD6-4934-8ED8-752FB2519AE2Q36682404-2E804CEA-04BB-4592-89EA-433BD7FBE255Q36701859-7B22F1DB-0066-4A37-BCB1-63A14D0EF80BQ36731455-17DC1633-DA2F-480B-8B0F-859109AF9DAFQ36872897-706C18A8-8FAB-4E4F-B35A-E883339E9A47Q36936923-6E3FDE33-6DC1-4167-9E10-69D1B054DFDBQ37064056-81EF1E0B-1F17-4046-95B8-AF145F717F75Q37080692-FD96A815-227B-4A06-AEB2-B4A94B375794Q37118769-626700FC-247C-43AD-B502-5FCE26FB51DDQ37135567-95878B39-3D57-4C08-9F88-EAA759A62429Q37355529-217E4DC3-3F94-433F-868D-4CFD39ACEAEAQ37386047-2A36D9AA-F0E4-4775-8B78-1D8023254B21Q37446459-34472B46-D026-4D74-A85B-EBB5F56593D2Q37943799-3E989554-35BA-449F-A615-318BE9C0E14AQ38336025-CF96B38E-1958-4F32-A6D3-E2770375CA6EQ38701486-90C2F3F3-C021-4CE8-AA3A-3DF5B0936E01Q39004344-FCDE20BA-CA0C-4A38-876C-80F435DF2796Q39092621-43B6AE17-8C84-4755-95B9-22233CCCC972Q39431937-3FBBAC07-00CD-400C-AE0E-CF9464DEE5B9
P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Search for a prion-specific nucleic acid.
@ast
Search for a prion-specific nucleic acid.
@en
type
label
Search for a prion-specific nucleic acid.
@ast
Search for a prion-specific nucleic acid.
@en
prefLabel
Search for a prion-specific nucleic acid.
@ast
Search for a prion-specific nucleic acid.
@en
P2093
P2860
P1433
P1476
Search for a prion-specific nucleic acid.
@en
P2093
Ana Serban
Darlene Groth
Detlev Riesner
James E Cleaver
Jiri G Safar
Klaus Kellings
P2860
P304
10796-10806
P356
10.1128/JVI.79.16.10796-10806.2005
P407
P577
2005-08-01T00:00:00Z