Identification of cryptic nuclear localization signals in the prion protein (Q48350176)

10 February 2018

title

Identification of cryptic nuclear localization signals in the prion protein (English)

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10 February 2018

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Yaping Gu

1

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10 February 2018

Joerg Hinnerwisch

2

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10 February 2018

Rebecca Fredricks

3

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10 February 2018

Sudheera Kalepu

4

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10 February 2018

Ravi Shankar Mishra

5

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10 February 2018

Neena Singh

6

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10 February 2018

publication date

1 March 2003

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10 February 2018

published in

Neurobiology of Disease

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10 February 2018

volume

12

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10 February 2018

issue

2

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10 February 2018

page(s)

133-149

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10 February 2018

Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

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7 January 2021

Predicted secondary structure and membrane topology of the scrapie prion protein

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Prion diseases: what is the neurotoxic molecule?

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Prion diseases of humans and animals: their causes and molecular basis

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Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

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Prion protein amyloidosis

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Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP.

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Nucleocytoplasmic transport

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7 January 2021

Prion peptide 106-126 modulates the aggregation of cellular prion protein and induces the synthesis of potentially neurotoxic transmembrane PrP

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7 January 2021

Mutant prion proteins are partially retained in the endoplasmic reticulum

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7 January 2021

Search for a nuclear localization signal in the prion protein

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7 January 2021

The Chaperone Protein BiP Binds to a Mutant Prion Protein and Mediates Its Degradation by the Proteasome

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7 January 2021

A short amino acid sequence able to specify nuclear location

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7 January 2021

Internalization of mammalian fluorescent cellular prion protein and N-terminal deletion mutants in living cells

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A Mutant Prion Protein Displays an Aberrant Membrane Association When Expressed in Cultured Cells

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Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform.

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7 January 2021

Mutant and infectious prion proteins display common biochemical properties in cultured cells.

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7 January 2021

Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases

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7 January 2021

De novo generation of a PrPSc-like conformation in living cells.

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7 January 2021

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

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7 January 2021

Transport of proteins and RNAs in and out of the nucleus

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The Metabolism and Imaging in Live Cells of the Bovine Prion Protein in Its Native Form or Carrying Single Amino Acid Substitutions

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7 January 2021

Different patterns of truncated prion protein fragments correlate with distinct phenotypes in P102L Gerstmann-Sträussler-Scheinker disease

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Kinetics of expression of prion protein in uninfected and scrapie-infected N2a mouse neuroblastoma cells

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7 January 2021

Basolateral protein transport in streptolysin O-permeabilized MDCK cells

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7 January 2021

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7 January 2021

NMR characterization of the full‐length recombinant murine prion protein, mPrP(23–231)

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7 January 2021

Prion Protein Aggregation Reverted by Low Temperature in Transfected Cells Carrying a Prion Protein Gene Mutation

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7 January 2021

PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase

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A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Sträussler-Scheinker disease A117V.

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7 January 2021

Molecular genetics of transmissible spongiform encephalopathies

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7 January 2021

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

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7 January 2021

Proteasomal Degradation and N-terminal Protease Resistance of the Codon 145 Mutant Prion Protein

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7 January 2021

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Identifiers

DOI

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10 February 2018

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10 February 2018