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Continuous quinacrine treatment results in the formation of drug-resistant prionsTowards 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 examplesGerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" modelPathogenic protein seeding in Alzheimer disease and other neurodegenerative disordersWhole Blood Gene Expression Profiling in Preclinical and Clinical Cattle Infected with Atypical Bovine Spongiform EncephalopathySynthetic prions with novel strain-specified propertiesPrion protein paralog doppel protein interacts with alpha-2-macroglobulin: a plausible mechanism for doppel-mediated neurodegenerationA decade and a half of protein intrinsic disorder: biology still waits for physicsStyryl-based and tricyclic compounds as potential anti-prion agentsEarly onset prion disease from octarepeat expansion correlates with copper binding propertiesInvestigation of the molecular similarity in closely related protein systems: The PrP case study.Understanding protein non-folding.Early noninvasive diagnosis of neurodegenerative diseases.Early behavioral changes and quantitative analysis of neuropathological features in murine prion disease: stereological analysis in the albino Swiss mice model.The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidylinositol anchor, partially impairs amyloid fibril formation.The efficacy of tetracyclines in peripheral and intracerebral prion infection.Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.Misassembly of full-length Disrupted-in-Schizophrenia 1 protein is linked to altered dopamine homeostasis and behavioral deficits.[A retrospective study of Creutzfeldt-Jakob disease in North of Portugal 1993-2002: demographic, clinical and neuropathological features].From high-throughput cell culture screening to mouse model: identification of new inhibitor classes against prion disease.Discovery of 2-aminothiazoles as potent antiprion compounds.Efficacy of novel acridine derivatives in the inhibition of hPrP90-231 prion protein fragment toxicity.Biology and genetics of prions causing neurodegenerationContext dependent neuroprotective properties of prion protein (PrP).Epidemiological mechanisms of genetic resistance to kuru.Genetics and molecular pathogenesis of sporadic and hereditary cerebral amyloid angiopathiesMolecular genealogy tools for white-tailed deer with chronic wasting disease.Chemical induction of misfolded prion protein conformers in cell culture.Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Acridine and phenothiazine derivatives as pharmacotherapeutics for prion diseasePros and cons of a prion-like pathogenesis in Parkinson's diseaseMad cow and other maladies: update on emerging infectious diseasesProtease-sensitive conformers in broad spectrum of distinct PrPSc structures in sporadic Creutzfeldt-Jakob disease are indicator of progression rate.Successes and challenges in phenotype-based lead discovery for prion diseasesHuman prion strain selection in transgenic mice.PrPTSE distribution in a primate model of variant, sporadic, and iatrogenic Creutzfeldt-Jakob disease.Allelic origin of protease-sensitive and protease-resistant prion protein isoforms in Gerstmann-Sträussler-Scheinker disease with the P102L mutation.Neurogenetics: advancing the "next-generation" of brain research.Calcium binding promotes prion protein fragment 90-231 conformational change toward a membrane destabilizing and cytotoxic structure.
P2860
Q21090510-28546F85-D507-4DFA-BB95-8D8A0D74AB54Q24289511-C7F0D20A-1FA0-43F9-BFC3-31BC64DFD080Q24294784-E8852F2C-09E1-4D1D-9F35-CAE296521203Q26850298-3CA71711-8650-43E7-A4EA-50435BE1CD90Q27314189-ADA5EF31-9C0E-43C1-93A6-3ADAE0E657ECQ27316313-EDA3EC6D-1736-431B-B58F-A185B7CD3A94Q28475611-3654D655-58A4-4BFD-80F4-081AC71E29E3Q28681184-2AC5736D-3A02-44BE-8A9E-3D917A5C9112Q28740431-A62A61DA-C7DC-45EC-A7E2-174C740F036AQ28910222-A59252D5-2273-4238-B124-5E27A3158A8EQ30375050-92CEACB0-38B5-4219-A245-A1BD2DD2C64DQ30385084-2FAA641A-8554-40E2-9DCA-80C11969AC8AQ30393556-B109B636-926F-4662-9F1A-F235D76E89EBQ30466255-C6471349-2A9D-47A7-B9DB-ED2F617C4F16Q30485085-60720E02-0446-42AC-9FD5-4CC059F168FAQ30493642-C86FA5F6-CABB-4ED5-8B3D-88D457C2A3C7Q30496598-2E2FF40F-B4B1-459B-8ED1-D200DDAF5937Q30593594-EB275CDA-BE06-44BE-8525-716D6FCBB2AFQ30826347-E7C0AE26-CCCF-47F4-821D-1C11A5ECFE1AQ30892024-8220548D-45BE-4B6D-AB7E-7DB832338FE5Q31023317-92A61C17-63A2-4A17-8727-73AC6723DB84Q33520644-4F09408D-7904-449C-B58E-2EB1DF38DF19Q33560026-28A78DD6-87D5-410D-A67D-5980E853F1D9Q33567229-22100A12-AA14-443A-AB81-27AA07C0A0E5Q33595425-21A1C4F0-2584-4602-BD50-936ADF49996BQ33704994-31C083A4-1ACE-4AD6-8D42-6A396B236C17Q33747695-F28C5276-ACAB-4790-8B09-9327F5D47A37Q33777544-C69214B6-5357-4758-BE3C-A876911B3228Q33796040-1503C904-747E-4A17-AE4F-171EA2974CDDQ33892707-1F1A0223-5081-47A0-BB8A-94A29F02051FQ33933969-2DB0E892-2F6A-42B7-A16A-BC55E8AD153AQ33937407-BC613957-9AA1-45F5-9642-4D91557BB50DQ33945003-CBB0AA09-0009-4461-A84D-964DDA5492EFQ34023019-884D8D3C-077F-4EE1-9E4D-DFBA2C11000BQ34104276-F8ED789B-9710-4E9A-9995-70C0DAE69437Q34112488-45D1BB02-3904-4D48-B358-47109F35F252Q34123943-EE361AB2-60F0-423E-A267-0F73C42DC9D2Q34182647-D7D34E55-C2E7-4FBF-AE7F-FBC838B241DFQ34315505-C3C2E25E-92C8-4709-9CAD-8B6FBBD7750EQ34343507-451413EE-9E63-4DAC-A326-7D229287D7E0
P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Shattuck lecture--neurodegenerative diseases and prions
@ast
Shattuck lecture--neurodegenerative diseases and prions
@en
Shattuck lecture--neurodegenerative diseases and prions
@nl
type
label
Shattuck lecture--neurodegenerative diseases and prions
@ast
Shattuck lecture--neurodegenerative diseases and prions
@en
Shattuck lecture--neurodegenerative diseases and prions
@nl
altLabel
Neurodegenerative Diseases and Prions
@en
prefLabel
Shattuck lecture--neurodegenerative diseases and prions
@ast
Shattuck lecture--neurodegenerative diseases and prions
@en
Shattuck lecture--neurodegenerative diseases and prions
@nl
P3181
P1476
Neurodegenerative Diseases and Prions
@en
Shattuck lecture--neurodegenerative diseases and prions
@en
P304
P3181
P356
10.1056/NEJM200105173442006
P407
P577
2001-05-17T00:00:00Z