about
Amyloid aggregates of the HET-s prion protein are infectious.Transmission of prionsPrion hypothesis: the end of the controversy?Cofactor molecules maintain infectious conformation and restrict strain properties in purified prionsPrionsA clinical study of kuru patients with long incubation periods at the end of the epidemic in Papua New GuineaA systematic survey identifies prions and illuminates sequence features of prionogenic proteinsLentivector-mediated RNAi efficiently suppresses prion protein and prolongs survival of scrapie-infected miceThe role of the cellular prion protein in the immune systemActin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in YeastYeast prions: structure, biology, and prion-handling systemsHsp104-dependent remodeling of prion complexes mediates protein-only inheritanceGenesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion diseaseNMR solution structure of the human prion proteinNMR structure of the bovine prion proteinNMR structures of three single-residue variants of the human prion proteinSheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solutionCrystal structure of human prion protein bound to a therapeutic antibodyCrystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion DiseasePrion disease susceptibility is affected by -structure folding propensity and local side-chain interactions in PrPAtomic Structures Suggest Determinants of Transmission Barriers in Mammalian Prion DiseaseInteraction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.Rebels with a cause: molecular features and physiological consequences of yeast prionsA brief history of prionsThe NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotypeElectron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion proteinIn vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoformsIn situ photodegradation of incorporated polyanion does not alter prion infectivityAnti-prion activity of a panel of aromatic chemical compounds: in vitro and in silico approachesIsolation of proteinase K-sensitive prions using pronase E and phosphotungstic acidPhysical, chemical and kinetic factors affecting prion infectivityPrions in Saccharomyces and Podospora spp.: protein-based inheritance.Prion amyloid structure explains templating: how proteins can be genes.Supersaturation-limited amyloid fibrillation of insulin revealed by ultrasonication.Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Isolation and characterization of a polymerized prion protein.The role of disulfide bridge in the folding and stability of the recombinant human prion protein.Rapid and discriminatory diagnosis of scrapie and BSE in retro-pharyngeal lymph nodes of sheep.The Malignant Protein Puzzle.
P2860
Q24530495-8EF15DE0-021D-49D6-8AB3-8509472426E1Q24540228-4FB3B315-EA74-421D-B736-E02523B0C9D5Q24599702-DE290765-6D29-426F-98F7-BBBBED838E5AQ24632206-DDD26559-3A88-4CBF-B474-DF7A273C9200Q24633319-9E246D6B-6736-4138-ADEC-926209ABE7A9Q24642582-1E3E345A-55A1-46B5-A214-F0D53F7A12F3Q24658451-D75DCB06-7524-4575-BD0D-7DD3C76D89CFQ24673105-39B7E22D-28CB-46D2-A67D-FF5C462AF1DCQ24683862-6E2663C0-BA24-41A0-972B-7614ECC71E31Q26778771-A867D0F2-5AC2-4712-956F-84AEC7D8365CQ27007482-EED7C887-2759-44D6-AF88-B829F9769B73Q27334853-57EC78DA-6ED5-488D-83CA-0741C2C1B3EDQ27348022-2CBD4C9A-0042-46AE-84D4-C412E92421A2Q27620845-D9EB0290-DEEB-47FF-9E4B-7114092F862FQ27625390-8216CB9C-8391-4050-8E0F-42C7FB9700ACQ27625393-A145452C-E0AC-472C-AD1F-F30FA5CD1B74Q27635085-63495694-2F67-4C07-BF69-F7316532C902Q27653698-62A7B655-C7B4-4119-9F8A-883F04CC840AQ27663878-89C2BA7C-86F4-4515-9003-BC4FF463A343Q27665543-50EA8CEC-C7AB-493E-B0C7-E45F370AA1CEQ27666974-9B02C11E-DCC5-4628-8297-9EC7CC54BE76Q27929839-87EE61AE-7FFC-4367-BC5C-F920841D7D8BQ28082218-30ABB1E9-A84B-4767-9EAE-D3A92FFD3F92Q28085285-450D47CA-A316-4A76-A026-D9BF657FE0E1Q28303621-4B41B384-9217-4D94-80EE-DEB6FE1F9ED5Q28367705-E13C0AF9-0626-4B11-BBCC-4989C0B69525Q28475550-0B58A5D2-03BD-4393-BE58-C1455BC63320Q28477075-582F16B3-9C54-419B-AC3A-18BE867B1CB1Q28538336-0CB47DCB-A181-49C4-8634-D98EE24B5042Q28744075-B7582B8B-93A1-42FE-86B3-3EF2C5F90B1AQ28830528-50CE256C-2BC9-4E14-81F2-290716CDDC8FQ30323934-75AE4B16-AF25-4782-B96C-15D5A8C5A7DEQ30392820-7468DCF6-FBEE-4F07-B4EF-2830805640C0Q30408452-6B605285-70F3-49DA-BE7B-97B03FD25300Q30420123-AE010579-DD46-47CB-A087-B5C45231EE61Q30492360-5EEE28D4-6EC6-47B2-915B-5ACF2EBAAC9DQ31050944-22F4BC8D-B0C7-4972-BB80-A921DEE23CB3Q31538196-52507841-C919-4CB2-BC1F-12778312D542Q33246296-E87796FB-72F4-4D14-82D4-5220CC38323DQ33363509-A3579A50-46C7-422A-B50B-08117E452F89
P2860
description
1967 nî lūn-bûn
@nan
1967 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1967 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1967年の論文
@ja
1967年論文
@yue
1967年論文
@zh-hant
1967年論文
@zh-hk
1967年論文
@zh-mo
1967年論文
@zh-tw
1967年论文
@wuu
name
Self-replication and scrapie.
@ast
Self-replication and scrapie.
@en
Self-replication and scrapie.
@nl
type
label
Self-replication and scrapie.
@ast
Self-replication and scrapie.
@en
Self-replication and scrapie.
@nl
prefLabel
Self-replication and scrapie.
@ast
Self-replication and scrapie.
@en
Self-replication and scrapie.
@nl
P356
P1433
P1476
Self-replication and scrapie.
@en
P2093
Griffith JS
P2888
P304
P356
10.1038/2151043A0
P407
P577
1967-09-01T00:00:00Z
P6179
1009533383