PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers. - Wikidata - wikimedia - TriplyDB

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

http://www.wikidata.org/entity/Q33916451

about

The mimic chain reaction.A generic method for design of oligomer-specific antibodies.PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains.The Anti-Prion Antibody 15B3 Detects Toxic Amyloid-β Oligomers Detection of protein aggregates in brain and cerebrospinal fluid derived from multiple sclerosis patients.Prion protein (PrP) gene-knockout cell lines: insight into functions of the PrP.Flow Cytometric Detection of PrPSc in Neurons and Glial Cells from Prion-Infected Mouse Brains.An Aged Canid with Behavioral Deficits Exhibits Blood and Cerebrospinal Fluid Amyloid Beta Oligomers.Conformation-dependent epitopes recognized by prion protein antibodies probed using mutational scanning and deep sequencing.

P2860

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P2860

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

http://www.wikidata.org/entity/Q33916451

description

2011 nî lūn-bûn

@nan

2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

@ast

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

@en

type

label

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

@ast

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

@en

prefLabel

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

@ast

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.

@en

P1433

Q33916451-D3A100E6-7FAF-4799-9C2A-E09D210AC25A

P1476

Q33916451-5D2CA1AC-287F-4BA5-A656-4B81DD8C3D46

P2093

Q33916451-2444072A-EE28-4B13-8519-05FA00A52C5C

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Q33916451-4FF6F263-BD8B-4F8A-91E6-1CB47DE2C1E4

Q33916451-E6E7528B-74F6-4666-ABBB-89B50ADF142A

Q33916451-E86A9497-B7B7-4138-A99D-409ACDCBD125

P2860

Q33916451-0047C7E9-0981-4EDD-984C-0205D0A73964

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Q33916451-10E5CF42-C2C7-453D-B53D-D56A2AD3C9D4

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Q33916451-273F6F48-ADED-4DD1-AFFA-C9787B6F2250

Q33916451-2F85A530-024F-4294-A71C-128A71D15AC5

Q33916451-2FB164E3-FBC3-465F-8A08-D21B39D98ACD

Q33916451-30F2FA94-51D9-4D22-B1A7-BA2D7326261B

Q33916451-33C4284F-1016-437A-BC83-1BD5C55E2B9F

P304

Q33916451-17A0E4F8-F93E-42EB-A32B-EE3D6480E95D

P31

Q33916451-CA7FB5D5-8C18-4D1B-986E-750C93BA9EFB

P356

Q33916451-5B95C1F5-2319-4390-857C-A28D69FCA2E9

P407

Q33916451-C3565871-84A2-459F-B4A1-B9D92159258C

P433

Q33916451-C701025A-5B92-451A-8512-9105BA78259A

P478

Q33916451-1FCB8FEE-F3F2-4B54-B575-CF3949EAA3EE

P50

Q33916451-A2DC4DE8-7786-4E48-99DA-8CAEFD00C4E5

P577

Q33916451-457C85EE-8B92-4F55-9FB9-A02A6CDA1812

P5875

Q33916451-C96BD52D-B34C-4CE9-BA2A-C7C759F550D2

P698

Q33916451-C3EE0313-C0A4-49EC-926D-6E951B5985E5

P921

Q33916451-7413352C-D78E-4112-8E17-069F8BF7BFFA

P932

Q33916451-FE82D1ED-93B9-41A0-B548-198A7D820C20

P356

JOURNAL.PONE.0019998

P1433

P1476

PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers

@en

P2093

Benjamin Frederick Stileman

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

Charlotte Chapman

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

Daryl Rhys Jones

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

Deming Zhao

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

Monique David

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

William Alexander Taylor

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

P2860

A camelid anti-PrP antibody abrogates PrP replication in prion-permissive neuroblastoma cell lines

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

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

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.

Mapping the prion protein using recombinant antibodies.

The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.

P304

e19998

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

P31

scholarly article

P356

10.1371/JOURNAL.PONE.0019998

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

P407

P433

5

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

P478

6

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

P50

P577

2011-05-19T00:00:00Z

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

P5875

51177589

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

P698

21625515

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

P921

Prion protein family

P932

3098279

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