(Q35172963)

6 August 2017

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title

Prion protein trafficking and the development of neurodegeneration (English)

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6 August 2017

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Ramanujan Shankar Hegde

series ordinal

1

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6 August 2017

Neena S Rane

2

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6 August 2017

publication date

1 July 2003

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6 August 2017

published in

Trends in Neurosciences

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6 August 2017

volume

26

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6 August 2017

issue

7

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6 August 2017

page(s)

337-339

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Shattuck lecture--neurodegenerative diseases and prions

6 August 2017

cites work

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https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Normal host prion protein necessary for scrapie-induced neurotoxicity.

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents

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https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Inherited prion diseases and transmission to rodents

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https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Transmissible and genetic prion diseases share a common pathway of neurodegeneration

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol

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https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel

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https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Quality control in the endoplasmic reticulum

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https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Retro-translocation of proteins from the endoplasmic reticulum into the cytosol

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https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells.

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Mutant prion proteins are partially retained in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

A transmembrane form of the prion protein in neurodegenerative disease

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Impairment of the ubiquitin-proteasome system by protein aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation

1 reference

https://api.crossref.org/works/10.1016%2FS0166-2236%2803%2900143-7

7 January 2021

10.1016/S0166-2236(03)00143-7

Identifiers

DOI

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6 August 2017

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