about
Aerosols transmit prions to immunocompetent and immunodeficient miceNanobacteria are mineralo fetuin complexesA miRNA signature of prion induced neurodegenerationGlypican-1 mediates both prion protein lipid raft association and disease isoform formationScrapie Agent (Strain 263K) can transmit disease via the oral route after persistence in soil over yearsMechanisms of cellular uptake of cell-penetrating peptidesβ-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptidesA camelid anti-PrP antibody abrogates PrP replication in prion-permissive neuroblastoma cell linesThe prion hypothesis in Parkinson's disease: Braak to the futureCellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomersThe genetic epidemiology of neurodegenerative disease.Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examplesMolecular features of the copper binding sites in the octarepeat domain of the prion proteinDeficiency of disulfide bonds facilitating fibrillogenesis of endostatinPrion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfateCharacterizing affinity epitopes between prion protein and β-amyloid using an epitope mapping immunoassayMAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune responseAnchorless 23-230 PrPC interactomics for elucidation of PrPC protective roleConformational diversity in prion protein variants influences intermolecular beta-sheet formationThe novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP sheddingLeu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experimentAmyloid aggregates of the HET-s prion protein are infectious.Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection.Dehydron: a structurally encoded signal for protein interaction.Transmission of prionsPrion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewalThe role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variantsJ. B. S. Haldane (1949) on infectious disease and evolutionIntracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion diseasePauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid diseasePrion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells2-Aminothiazoles as therapeutic leads for prion diseasesThe toxicity of amyloid β oligomersSpontaneous generation of prion infectivity in fatal familial insomnia knockin miceGenetic susceptibility, evolution and the kuru epidemicElimination of prions by branched polyamines and implications for therapeuticsTransmission and spreading of tauopathy in transgenic mouse brainKuru prions and sporadic Creutzfeldt-Jakob disease prions have equivalent transmission properties in transgenic and wild-type miceA heritable switch in carbon source utilization driven by an unusual yeast prionProbing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions
P2860
Q21089612-29DC1419-C028-42CD-9F9B-7B305119171BQ21090525-D6335481-D359-44F8-AF5F-6891AC9811F8Q21092168-60623C0F-5E49-4883-8FEB-B997F65988DBQ21131569-FA069184-0000-4C92-A002-3CB2A1D396D0Q21144451-5E826134-6ADF-46A9-B840-7DEF35C740EBQ21296784-BBC19318-A468-4A3C-B016-E1052CFBC6EFQ21558493-13AB49A6-7DEC-4040-8C33-4DD5274D09D7Q21562652-A8DB5826-5351-4121-92B5-4515AB201525Q22001062-B66014A2-8460-4462-905F-C248FD02BC5EQ22251089-CBBE4B94-2ED6-456B-BECB-81C58BADAAEEQ22306301-0A573310-88B4-41ED-93DD-7E5EF1C6409DQ24289511-4F7BFB69-122C-4D07-8655-FCDDCC26F3E3Q24292484-AC0E5CD2-A030-440E-87B6-0DF52293EABAQ24293595-B82A45CD-2134-41A7-800E-CF7C04767168Q24301330-3B9F7599-65C4-45F9-994A-62A1E1202658Q24313479-CDB79F6B-B1CE-44BF-B669-0E4A4D024697Q24316320-8BD62C87-0E10-4520-92EA-8E930B57F78BQ24317448-DA00CBC0-A0A5-4012-BA9A-EDCD7965E0C3Q24318672-245E795D-A3EE-4C53-AD96-709F4B7FE2F7Q24322760-625C541C-138B-4746-9084-CB33E6F6AA24Q24337989-36114278-FDCD-43EC-BCD4-9206F10C5088Q24530495-85A1AB6A-F9B0-4973-9EC0-DC594F5D5973Q24534939-4BB5790F-A596-4789-B3F9-810456FA0AFAQ24537703-9EDCAA3F-1A87-4F10-95DC-81EDB5A2705FQ24540228-E1E71D4E-C292-4D1D-BF74-0B02EE357704Q24541459-3E1037CF-579F-481C-A966-064F5C538AC0Q24545846-BF227A4A-3EB7-43E0-9B55-99EF044F83B7Q24548068-2D6F9642-1AEF-40D7-A870-F4A5CA8B05A5Q24550300-7C70F689-17B7-4C65-8BF0-A979310875A6Q24564070-B484EF23-97F8-4674-903E-E579FB804546Q24610255-E2C3A8FC-BE53-47F2-8192-7DEB2505FAB1Q24618566-33BF460D-D88E-4417-9736-9578E9588CB0Q24631757-AFD2CBAB-B48A-4EE4-A2F0-925211FB0272Q24641822-AFD6FBD4-01D1-4F9A-B22B-6C2CCE2287DDQ24645692-809D7538-D7AB-488F-A6D2-5A6A04C677B9Q24646752-2EBCB77F-9280-4B0D-ABFF-803BFC260475Q24651334-5A63E501-D930-4251-90E7-E312C31F38B8Q24651920-F4EB3C1A-725D-4837-82F5-537788DFBA83Q24655783-4123F227-69D2-415D-A89D-E623FAED8960Q24657467-50A25C83-2001-427D-B804-C21DE1015FBC
P2860
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Prions
@ast
Prions
@en
Prions
@nl
type
label
Prions
@ast
Prions
@en
Prions
@nl
prefLabel
Prions
@ast
Prions
@en
Prions
@nl
P2860
P3181
P356
P1476
Prions
@en
P2860
P304
P3181
P356
10.1073/PNAS.95.23.13363
P407
P577
1998-11-10T00:00:00Z