In vitro and in vivo neurotoxicity of prion protein oligomers. - Wikidata - awgldk - TriplyDB

In vitro and in vivo neurotoxicity of prion protein oligomers.

In vitro and in vivo neurotoxicity of prion protein oligomers.

http://www.wikidata.org/entity/Q33296885

about

Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis Insights into Mechanisms of Chronic Neurodegeneration Activation of zebrafish Src family kinases by the prion protein is an amyloid-β-sensitive signal that prevents the endocytosis and degradation of E-cadherin/β-catenin complexes in vivo.Synthetic prions with novel strain-specified properties Prion Fibrillization Is Mediated by a Native Structural Element That Comprises Helices H2 and H3 Prion disease susceptibility is affected by -structure folding propensity and local side-chain interactions in PrP Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein Solvent microenvironments and copper binding alters the conformation and toxicity of a prion fragment Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts Role of polysaccharide and lipid in lipopolysaccharide induced prion protein conversion Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Investigating the conformational stability of prion strains through a kinetic replication model.Immunopurification of pathological prion protein aggregates Efficacy of novel acridine derivatives in the inhibition of hPrP90-231 prion protein fragment toxicity.Altered Ca2+ homeostasis induces Calpain-Cathepsin axis activation in sporadic Creutzfeldt-Jakob disease PB1-F2 influenza A virus protein adopts a beta-sheet conformation and forms amyloid fibers in membrane environments.Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity.N-terminal domain of prion protein directs its oligomeric association.Prion protein-specific antibodies-development, modes of action and therapeutics application Synthetic scrapie infectivity: interaction between recombinant PrP and scrapie brain-derived RNA.αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.The intricate mechanisms of neurodegeneration in prion diseases.PrP assemblies: spotting the responsible regions in prion propagation.Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice.Highly neurotoxic monomeric α-helical prion protein.Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape.The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.Unique Properties of the Rabbit Prion Protein Oligomer Role of prion protein aggregation in neurotoxicity.Urea-Water Solvation Forces on Prion Structures A Fluorescent Oligothiophene-Bis-Triazine ligand interacts with PrP fibrils and detects SDS-resistant oligomers in human prion diseases.Strain-dependent profile of misfolded prion protein aggregates.α-Synuclein oligomers and clinical implications for Parkinson disease.Single-molecule approaches to prion protein misfolding Divergent and Convergent Evolution of Fungal Pathogenicity.Infectivity-associated PrP(Sc) and disease duration-associated PrP(Sc) of mouse BSE prions.Comparing the energy landscapes for native folding and aggregation of PrP.

P2860

Q21132346-E57A5D44-BE13-447A-9E58-B77D501C2D5E Q21558493-BD66CA56-EB24-409C-A9FF-DE2E4B2E08A9 Q24655066-28FA5F3F-6A78-4C01-8EFD-46B45E42075B Q26771732-39CF76B9-65B6-419D-A28E-28B05717D6CB Q27301257-A6258B4A-E9D6-400E-B9F9-A6A67FBCAE24 Q27316313-EE4D8219-0623-4F52-A012-7399BD0B1794 Q27660444-D1727A4A-F805-4E9A-A3BE-FB4EFF9199C0 Q27665543-DC23F929-AEDC-4940-8499-02C8613490C4 Q28535083-F272FAA0-EA2A-4B7A-AC13-4B6BB44AC891 Q28538070-3F6AFDE7-9CBD-4027-9087-76941AAF69BD Q28742804-628E1CAA-CDAF-4E9B-89B2-6CB6E5773D7B Q28817214-8C71EC55-9562-47DC-89A7-51A4E87CE0DD Q30368356-3CF4FE9D-5961-4998-AD6A-75368F8F32D2 Q30492360-8C4BF1C0-C6F7-4A2D-A0AF-93213764925F Q33478386-A67A1A9E-1E2F-4FCF-A0B0-E7AA9B90F668 Q33516017-3CCD9DDB-E84C-4962-9D73-998E5C83CC6E Q33560026-5897B227-2BA3-421A-B27D-CD1E60127A31 Q33612558-F218EC9C-3759-4416-AB37-F85A1999D9DA Q33800245-6DC0C8FC-C98F-45A1-9534-EE482B149B90 Q33916275-00A201B5-50B7-4445-9DA7-084721ED1857 Q34170632-D9D15CFE-C280-4CE0-AA8D-6EFF0BE4FFB0 Q34423386-03660053-D4AE-430C-AC7B-8E3AAEE8AA9F Q34458035-874F20B8-B842-4000-98BC-46B1DBA20247 Q34505802-799CC674-28B4-4CF3-AB59-D13B52A44395 Q34664576-F85AC428-282E-41A1-96F4-4C29A9D0E4D0 Q35194905-F79ABDAE-0632-480F-9C6D-46708261D0BC Q35574384-DB84D595-8DFA-424B-8501-736A91EFE1D4 Q35779305-4642E60A-D8A2-45BB-A271-B4DE3E87EAE9 Q35845795-25B86137-6A30-4E20-A630-5395763E51F8 Q35953172-866C1477-D126-4A76-9B7B-A8C17E29CA32 Q36104795-60C07AE4-0C32-48A3-A63C-778D07D70168 Q36197275-E0984A26-D6E3-459D-BC17-F113BBA10121 Q36304738-43DEB9F2-2E11-4114-95BD-692B6B2639FD Q36503630-FAE23F83-AAA3-4065-A94F-DDF15A89785E Q36579439-E1E0B2A2-F85D-4FB3-B15C-55462383839C Q36718306-4EF28172-4DD4-44EF-A692-898F9E6212EE Q36719202-477E46D2-32F2-4760-B9B9-872CC0ED6512 Q36983117-6A4EE647-3282-473B-9D83-FAE5C9D5022D Q37135567-6B1164CB-C763-4589-B4A5-CA238AA096A6 Q37167847-6BFFA9AE-6F23-41BB-AD77-A525ED9DD5C3

P2860

In vitro and in vivo neurotoxicity of prion protein oligomers.

http://www.wikidata.org/entity/Q33296885

description

2007 nî lūn-bûn

@nan

2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

In vitro and in vivo neurotoxicity of prion protein oligomers.

@ast

In vitro and in vivo neurotoxicity of prion protein oligomers.

@en

In vitro and in vivo neurotoxicity of prion protein oligomers.

@nl

type

label

In vitro and in vivo neurotoxicity of prion protein oligomers.

@ast

In vitro and in vivo neurotoxicity of prion protein oligomers.

@en

In vitro and in vivo neurotoxicity of prion protein oligomers.

@nl

prefLabel

In vitro and in vivo neurotoxicity of prion protein oligomers.

@ast

In vitro and in vivo neurotoxicity of prion protein oligomers.

@en

In vitro and in vivo neurotoxicity of prion protein oligomers.

@nl

P1433

Q33296885-E4AB9A25-1248-4C64-85D5-B69794F11666

P1476

Q33296885-94DDD7F6-3EE2-483F-92D6-2FA9363AA32C

P2093

Q33296885-22E4A658-0303-4E2B-A0C7-3A2FBD5ADBEB

Q33296885-31BBC634-B649-4841-9149-5C0941FAB970

Q33296885-3358CEBE-AC1B-4061-A553-A2CFDFB58498

Q33296885-48A08998-3593-426F-8C5A-BE433E3D23D5

Q33296885-6850994A-1B6D-4AEA-BA52-FDDDA266CD8D

Q33296885-AA678237-A55B-494D-A9BC-ADF7BA7D56B9

Q33296885-B967065C-BFA4-4926-989E-BFA7372FC526

Q33296885-D262D2C7-7012-4932-936F-DED8C9406540

Q33296885-D662C4EE-26C9-49C0-83BA-44B499C5DFFB

Q33296885-E8718991-D79B-40DD-BBC9-A0D0D2B1AADA

P2860

Q33296885-06637081-AA61-48C6-A098-199A1AD273A0

Q33296885-0AC9BD63-1403-417A-B5F5-CA3D47B9469C

Q33296885-0ADE2894-DFE7-478C-8817-8B2BAB677DDF

Q33296885-0E8B9F32-ADFA-4FD1-8528-EEF53E42C448

Q33296885-103731F9-18BB-4C44-AB41-BCDE40513135

Q33296885-1048F437-44E3-496F-9D5C-DBEDC37A3EF1

Q33296885-11818F9C-3A83-4FD3-B908-5007DDC75ACF

Q33296885-1386EABE-7353-4EC7-B383-49852441DB7E

Q33296885-145B3F5B-5387-4015-919C-6FFF0F6619C9

Q33296885-14F683CA-422F-4233-8017-3B4402F8AB70

P304

Q33296885-541EB4B1-2BDC-46F1-9173-32FB5C769122

P31

Q33296885-6CC630D8-2684-45C6-8503-F5A8962A9DDC

P356

Q33296885-C9DF93C3-F850-417F-89BF-10B9FDFF64CC

P433

Q33296885-343827BF-3EF8-4EC5-8319-67FD1988B97D

P478

Q33296885-C7F04CB6-7C95-4F3F-9ACD-C58F55F96C0F

P50

Q33296885-361E62EF-589A-42A8-BD2D-692A228671BD

P577

Q33296885-4080E12E-5462-4D58-8A78-BF42C4D749FF

P5875

Q33296885-912C90E9-30F7-4F9D-AFF3-68A4A1641A62

P698

Q33296885-3D868F58-5A4B-4B70-938C-977267574E4B

P921

Q33296885-E798029F-090C-4CF8-861E-D19DCE8DA70E

Q33296885-F2DB3D38-101A-45A7-8A4A-34F378A892E6

P932

Q33296885-0B5F4E00-37BD-4435-A12E-61954CFCC8F1

P356

JOURNAL.PPAT.0030125

P1433

P1476

In vitro and in vivo neurotoxicity of prion protein oligomers

@en

P2093

Catherine Vidal

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

Corinne Ida Lasmézas

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

Franziska Wopfner

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

Gunnar Kaiser-Schulz

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

Human Rezaei

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

Jean-Guy Fournier

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

Jeanne Grosclaude

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

Julien Comte

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

Maxime Lefebvre-Roque

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

Nicole Salès

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

P2860

Role of Protein Aggregation in Mitochondrial Dysfunction and Neurodegeneration in Alzheimer's and Parkinson's Diseases

Doppel-induced cerebellar degeneration in transgenic mice

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

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

Protein folding and misfolding

Anchorless prion protein results in infectious amyloid disease without clinical scrapie

Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor

PrPC directly interacts with proteins involved in signaling pathways

A specific amyloid-beta protein assembly in the brain impairs memory

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

P304

e125

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

P31

scholarly article

P356

10.1371/JOURNAL.PPAT.0030125

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

P433

8

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

P478

3

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

P50

Hermann M Schätzl

P577

2007-08-01T00:00:00Z

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

P5875

6055314

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

P698

17784787

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

P921

Prion protein family

P932

1959381

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