Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
about
Oral transmissibility of prion disease is enhanced by binding to soil particlesThe role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variantsInsoluble cellular prion protein and its association with prion and Alzheimer diseasesThe strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of diseaseThe physical relationship between infectivity and prion protein aggregates is strain-dependentChanging a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers.Strain-specified relative conformational stability of the scrapie prion proteinSmall ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathySpontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteinsIsolation of proteinase K-sensitive prions using pronase E and phosphotungstic acidAnalysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease PrionsCharge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Changes in protein structure and distribution observed at pre-clinical stages of scrapie pathogenesis.Prion amyloid structure explains templating: how proteins can be genes.Two amyloid States of the prion protein display significantly different folding patternsGetting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Prion formation, but not clearance, is supported by protein misfolding cyclic amplification.Isolation and characterization of a polymerized prion protein.Bank Vole Prion Protein As an Apparently Universal Substrate for RT-QuIC-Based Detection and Discrimination of Prion StrainsUltraviolet-ozone treatment reduces levels of disease-associated prion protein and prion infectivity.Prion diseases and their biochemical mechanisms.High-resolution structure of infectious prion protein: the final frontierLow density subcellular fractions enhance disease-specific prion protein misfolding.Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion proteinEfficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155.Coinfecting prion strains compete for a limiting cellular resource.Prion generation in vitro: amyloid of Ure2p is infectious.Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.Scrapie strains maintain biological phenotypes on propagation in a cell line in culture.Molecular analysis of the protease-resistant prion protein in scrapie and bovine spongiform encephalopathy transmitted to ovine transgenic and wild-type mice.Biological and biochemical characterization of sheep scrapie in JapanEffect of glycans and the glycophosphatidylinositol anchor on strain dependent conformations of scrapie prion protein: improved purifications and infrared spectra.Prion strain-dependent differences in conversion of mutant prion proteins in cell culture.Prion diseases of yeast: amyloid structure and biology.Molecular chaperone Hsp104 can promote yeast prion generationInsights into prion biology: integrating a protein misfolding pathway with its cellular environment.Amyloid polymorphism: structural basis and neurobiological relevance.Propagation of yeast prions.Increased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion proteinA Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.
P2860
Q21559510-68702D2A-E3B1-4AB9-8C61-4D0F98CFFC3BQ24545846-BEFED66F-10C5-483B-BEE5-F3B2EC32ED99Q27012706-ECE68B48-0A53-43DE-A459-FEF37495F61FQ27312083-828D3CBA-B27C-43B2-8E09-50356A640823Q27315010-284FFFD5-E59A-4A2E-B9C7-55B7E50E3F9FQ28359731-63457AF6-407C-4652-9072-D5A81C0C1EA4Q28361583-B03DA6C7-0A0A-48D2-AA78-979DEDA6AED5Q28534276-72DF4068-1F8E-4B32-85B2-29331A9CCD7CQ28534632-484C4842-9A61-4B2E-B580-74CAECFC2A32Q28744075-DA3B08B8-0483-407B-B43B-A200E8FBF635Q28831096-E894C0E1-4693-4AFE-A4B4-63136146C146Q30368863-36D2AC71-EBE9-4B83-9450-48684E7CF2EDQ30370633-31D09808-BF4E-40E6-8D48-FE462BC0EBB3Q30392820-197EFD81-7675-4FA6-A7AE-6D46217A2FBDQ30474752-AEB5CBA8-0A86-43CE-83D7-A8499E7E94B4Q30492360-2D353E30-D2A9-49BF-8098-0A392A1715FAQ30875331-BFE6AD88-E992-4AF0-805F-B5A27934F9B9Q31050944-F79024DD-AD4B-4D45-9D68-A934B9F796C6Q33457447-2213E54D-FC29-4827-BCFA-A3245F051FDCQ33478741-8F94D86A-F82D-4160-B167-68303B9E7844Q33584925-9DACEB29-315B-4F55-8063-76A4EDD0EDBAQ33725453-451351CF-1145-4120-95A8-0AD2C3E7DA3FQ33744702-DB8EDEDF-6EC1-45C8-8C15-52995E8EFA41Q33794942-4A6AB00D-8C56-42DF-A96E-8685F6B4ED21Q33840809-54EE9C87-D0F8-463D-9D02-E840B80D3E86Q33877386-850E1835-ED3B-4C6B-AD32-26D96855FDB7Q33947121-C1A07E4F-2422-449D-B0AD-1FFC2EFBDAC5Q34071628-8C97D864-99F6-4272-BD81-BFDCAF038839Q34080020-A2122D88-FD13-43F4-9A24-B0FAB4B56428Q34192646-25073157-4EA1-4206-B519-32A86D51BFF1Q34194132-5CD119A5-F434-4939-A805-CBE5CA4B4D28Q35004394-38FE70E3-CF6E-4BA2-899A-38714E65082FQ35023923-EA4F58F3-C3E1-46B1-A744-17E9EBF8520DQ35053520-6505659C-EACD-4DF7-8543-616EB6926B70Q35065489-9289E399-90B8-4E89-B165-121D400ED410Q35194908-B0E0E51D-DA8D-499C-A1CB-62F05A2AC401Q35586308-62C5D3CD-BF8D-4A14-B01B-B124D03A509CQ35587875-630F35AB-CB95-46DB-B7E8-8FC1A17C1F17Q35641189-34AEC772-6940-4FEB-BD08-B7E2A24F66E1Q35678593-E673A56C-21C2-4D60-B546-CCBD27DDBD83
P2860
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
@en
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
@nl
type
label
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
@en
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
@nl
prefLabel
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
@en
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
@nl
P2093
P2860
P356
P1476
Strain-dependent differences in beta-sheet conformations of abnormal prion protein.
@en
P2093
P2860
P304
32230-32235
P356
10.1074/JBC.273.48.32230
P407
P577
1998-11-01T00:00:00Z