Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining.

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Flow Cytometric Detection of PrPSc in Neurons and Glial Cells from Prion-Infected Mouse Brains.Retrograde Transport by Clathrin-Coated Vesicles is Involved in Intracellular Transport of PrP in Persistently Prion-Infected Cells

P2860

Q47631657-17239A04-3DC4-4AE2-8F56-D8371B8212E6 Q56557476-702C053B-71F8-4196-BBD0-00014FF38353

P2860

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining.

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http://www.wikidata.org/entity/Q38766282

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Comparison of abnormal isoform ...... PrPSc-specific immunostaining.

@en

type

Item

label

Comparison of abnormal isoform ...... PrPSc-specific immunostaining.

@en

prefLabel

Comparison of abnormal isoform ...... PrPSc-specific immunostaining.

@en

P1476

Comparison of abnormal isoform ...... PrPSc-specific immunostaining.

@en

P2093

Ai Fujiwara

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

Akio Suzuki

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

Kentaro Masujin

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

Misaki Tanaka

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

Motohiro Horiuchi

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

Rie Hasebe

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

Takeshi Yamasaki

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

P2860

Prions

Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs

Characterization of intracellular dynamics of inoculated PrP-res and newly generated PrP(Sc) during early stage prion infection in Neuro2a cells.

Filamentous white matter prion protein deposition is a distinctive feature of multiple inherited prion diseases

Tracing conformational transition of abnormal prion proteins during interspecies transmission by using novel antibodies.

Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent.

Ultrastructural localization of prion proteins: physiological and pathological implications.

A prion protein epitope selective for the pathologically misfolded conformation.

Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis.

Comparison of the anti-prion mechanism of four different anti-prion compounds, anti-PrP monoclonal antibody 44B1, pentosan polysulfate, chlorpromazine, and U18666A, in prion-infected mouse neuroblastoma cells

P304

2030-2042

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P31

scholarly article

P356

10.1099/JGV.0.000514

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

P407

English

P433

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

P478

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

P577

2016-06-06T00:00:00Z

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P698

27267758

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

P921

Prion protein family

P932

5770843

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

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining.

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P2860

P2860

Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P932