Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. - Wikidata - awgldk - TriplyDB

Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity.

Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity.

http://www.wikidata.org/entity/Q46433690

about

Branched polyamines cure prion-infected neuroblastoma cells Prion hypothesis: the end of the controversy?Darwinian evolution of prions in cell culture Generating a prion with bacterially expressed recombinant prion protein.Prions Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice Kuru prions and sporadic Creutzfeldt-Jakob disease prions have equivalent transmission properties in transgenic and wild-type mice A short purification process for quantitative isolation of PrPSc from naturally occurring and experimental transmissible spongiform encephalopathies.The mechanism of prion strain propagation Analysis of prion strains by PrPSc profiling in sporadic Creutzfeldt-Jakob disease.Efficient transmission and characterization of Creutzfeldt-Jakob disease strains in bank voles.Prion-like properties of Tau protein: the importance of extracellular Tau as a therapeutic target The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease The physical relationship between infectivity and prion protein aggregates is strain-dependent Synthetic prions with novel strain-specified properties Evidence that bank vole PrP is a universal acceptor for prions Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform A brief history of prions De novo generation of prion strains Changing 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 protein Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.Prion diseases: dynamics of the infection and properties of the bistable transition.Solid-state NMR as a probe of amyloid structure Molecular, biochemical and genetic characteristics of BSE in Canada In situ photodegradation of incorporated polyanion does not alter prion infectivity Relationships between PrPSc stability and incubation time for United States scrapie isolates in a natural host system Defining the conformational features of anchorless, poorly neuroinvasive prions Small ruminant nor98 prions share biochemical features with human gerstmann-sträussler-scheinker disease and variably protease-sensitive prionopathy Critical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein Isolation of a Defective Prion Mutant from Natural Scrapie Correlation analysis for the incubation period of prion disease Isolation of proteinase K-sensitive prions using pronase E and phosphotungstic acid Prion protein: evolution caught en route Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions Structural polymorphism of Alzheimer Abeta and other amyloid fibrils Structural effects of PrP polymorphisms on intra- and interspecies prion transmission.Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Emergence of a novel bovine spongiform encephalopathy (BSE) prion from an atypical H-type BSE.

P2860

Q24529092-530769DD-C9D6-4354-999E-CD7CE5FE573A Q24599702-A6ECC2A7-5945-4AC7-8933-F82D9D656180 Q24607587-DC703522-9E54-4552-AFBC-151AFD229749 Q24626352-0A8605EA-93EB-4CC9-8FF1-50CD9CF82AF9 Q24633319-02386782-8104-4C3B-BA3B-9CE852CB4332 Q24641822-E784A57C-FF8A-4E18-A5AE-F34298D22050 Q24651920-F052F7ED-ED97-4118-A85E-A88C4D0538B9 Q24793769-B4FF2D86-295D-4DE7-93E6-5C959C06EB1F Q24801275-86759C85-77D3-4665-8D15-FB26F6CA4903 Q24812893-F02D1F9B-58BC-4A07-8EC9-5648A1FEF4DA Q25257725-C7B70811-EF08-4764-B288-76AF7A0C68CA Q27021159-A7558B4F-7AEC-4F66-A8CD-C9FA3C5804B0 Q27312083-4F0332A1-8A0A-4338-8F26-33693F598B02 Q27315010-2625E4C8-1D37-4D50-9DB4-322E292FEDAF Q27316313-2A91A2C1-6A61-455C-B580-F899EEEA80C8 Q27330039-F4995189-1A90-42BE-80A7-F92421000D4D Q27652925-4D09DC7B-6343-4A0F-B692-C53710B94818 Q27743024-341F355C-E81C-4E3B-ACB4-B4A55CDF7DA2 Q28085285-7C1F16F2-856D-4C56-BB17-816610CAEBE4 Q28249136-B4728A5F-FC6B-4803-84EB-61C35D6F94CA Q28359731-678F6A2E-33F4-48B7-B7A6-84EFEA2C383E Q28361583-F57AF3A5-94DB-4280-B2F9-057283008867 Q28361853-E73992E0-1645-46CB-B1FE-31A172016F2C Q28361955-0DB6DFE1-2323-4B01-8D5E-FF251084664E Q28388671-EC937735-BBFB-4369-A963-2C75867D7ED0 Q28473930-8C430D4B-20E1-44AA-A722-B83341245679 Q28477075-1003251A-A65D-4A43-83BA-F6305EAE6FCF Q28482253-E5992C4C-5AF2-49EE-8F1F-C01C49B772BA Q28486278-9E2EA93D-2016-4D14-8C20-B0183C4B6564 Q28534276-BDEC154A-BFB5-4B16-8685-6D81B4E3EFA4 Q28534369-150F7380-2499-451D-96F2-198AAE5B91BC Q28553700-8FE39B72-1FBF-4743-8E92-8BCA35CA5D1B Q28729089-03CDECE3-E301-43E0-9AF9-31CE6EC55D9F Q28744075-601506D0-B29B-4014-90A6-5FF9F83C715F Q28776299-8F2E21A8-4795-40B1-B28C-3DB4C2456F57 Q28831096-A23F1E8A-4D47-4670-A2A6-C4AB68E04E27 Q30319061-494B06FB-C5B5-4BE8-9FC5-8BBA625905A6 Q30364827-E04A7B26-AD7E-47A1-B67D-30A2AA9A362E Q30368863-FA353C40-BFE2-4595-B0FB-8069784EE12E Q30388704-BB5A9A99-956F-4253-9658-1B07C4BAB452

P2860

Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity.

http://www.wikidata.org/entity/Q46433690

description

1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年学术文章

@wuu

1996年学术文章

@zh

1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

1996年學術文章

@zh-hant

name

Evidence for the conformation ...... d propagating prion diversity.

@en

Evidence for the conformation ...... d propagating prion diversity.

@nl

type

label

Evidence for the conformation ...... d propagating prion diversity.

@en

Evidence for the conformation ...... d propagating prion diversity.

@nl

prefLabel

Evidence for the conformation ...... d propagating prion diversity.

@en

Evidence for the conformation ...... d propagating prion diversity.

@nl

P1433

Q46433690-F75E6A12-9962-4DCF-9ADA-448A6F6EADE0

P1476

Q46433690-CCD9170E-605D-4A84-9713-690EDF052C77

P2093

Q46433690-6BD97461-4165-4B9C-995B-AA05CE4EF9B5

Q46433690-7C5FE543-07E5-4F9A-B2B9-0BCD25762A71

Q46433690-86B2D9D8-D60C-45BA-83B4-9E96E2DCC3AA

Q46433690-892312CA-C9F9-4BCB-B0FD-A63781559EB0

Q46433690-89B1D0D7-7B9E-4899-A1BB-34B49E862B6E

Q46433690-CA81A231-9489-4147-ADDC-2976FC0F22EB

P2860

Q46433690-0264FD8B-9A57-437D-B031-E81C7B8C3B2E

Q46433690-06787965-65D3-4019-90EF-BC8298829BA9

Q46433690-0933A21B-5F70-47FC-8624-92CB277E1AFD

Q46433690-1C592042-35CC-4E99-A5B6-F717EECE71B5

Q46433690-1DA21BDB-6C78-4DBF-8AF3-8779E7BF5777

Q46433690-2CCBC98E-9A32-4BC7-AE7E-587DE201DBE9

Q46433690-2E5A4516-CC3E-4FCE-9FE2-E95307E01156

Q46433690-33ADF250-6BE1-4993-83CF-0B35D65D8608

Q46433690-39E8459D-F976-4407-99CE-351AE4818FB1

Q46433690-3DD21DFA-E155-4DB3-AB6B-E3E31C100DB7

P304

Q46433690-9B604ECD-43A2-4D00-81D7-C20CC3F560E2

P31

Q46433690-83944CD4-7ABE-4E34-81C5-DB03BDC8405D

P356

Q46433690-F65D82BA-7660-4D14-ABBA-A90F1B64540B

P407

Q46433690-638E26F9-0108-433D-BFF3-78DCAE798228

P433

Q46433690-D75D7D3F-F2FC-4462-A49E-DDD42632E6D8

P478

Q46433690-9BBBE017-1179-4653-B0F7-D20D374A9D73

P50

Q46433690-2CA3243C-7FD1-4D88-8A89-F782063BF98A

Q46433690-70773724-C12F-4678-8783-B02AB18CFFAF

Q46433690-9AE43B75-1CCE-404C-BB3D-2945684B3A14

Q46433690-AD1CF35B-CC0A-4F16-8122-4A72DF9F90D8

P577

Q46433690-B11B9382-B0BB-4C7A-BF29-6E0A403F4AFD

P5875

Q46433690-154933F4-F2E7-4016-9F92-EBB6E56B0798

P698

Q46433690-321183AE-9811-46A5-9972-6460C1D83CE4

P921

Q46433690-4A2E1607-0A3C-418E-BE9F-46A193A257DF

P356

SCIENCE.274.5295.2079

P1433

P1476

Evidence for the conformation ...... d propagating prion diversity.

@en

P2093

Gabizon R

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

Gambetti P

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

Lugaresi E

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

Mastrianni J

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

Montagna P

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

Telling GC

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

P2860

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

NMR structure of the mouse prion protein domain PrP(121-231)

Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene

Principles that govern the folding of protein chains

Transmission dynamics and epidemiology of BSE in British cattle

Unconventional viruses and the origin and disappearance of kuru.

Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein.

Structural clues to prion replication.

Fatal familial insomnia and familial Creutzfeldt-Jakob disease: different prion proteins determined by a DNA polymorphism.

Transmission of Creutzfeldt-Jakob disease from humans to transgenic mice expressing chimeric human-mouse prion protein.

P304

2079-2082

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

P31

scholarly article

P356

10.1126/SCIENCE.274.5295.2079

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

P407

P433

5295

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

P478

274

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

P50

Stanley B. Prusiner

Pietro Cortelli

Stephen J DeArmond

P577

1996-12-01T00:00:00Z

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

P5875

14254499

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

P698

8953038

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

P921

Prion protein family