(Q48784818)

15 February 2018

title

Familial mutations and the thermodynamic stability of the recombinant human prion protein. (English)

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15 February 2018

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3

Gambetti P

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15 February 2018

author name string

Swietnicki W

series ordinal

1

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15 February 2018

Petersen RB

series ordinal

2

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15 February 2018

Surewicz WK

series ordinal

4

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15 February 2018

language of work or name

English

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publication date

1 November 1998

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15 February 2018

Journal of Biological Chemistry

published in

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15 February 2018

volume

273

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15 February 2018

page(s)

31048-31052

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15 February 2018

issue

47

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15 February 2018

Prion diseases and neurodegeneration

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Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity

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Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

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

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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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Deadly conformations--protein misfolding in prion disease

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The environmental dependency of protein folding best explains prion and amyloid diseases

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Proposed three-dimensional structure for the cellular prion protein

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Physical studies of conformational plasticity in a recombinant prion protein

21 January 2018

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Fluorescence quenching studies with proteins

21 January 2018

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Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein.

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Chaperone-supervised conversion of prion protein to its protease-resistant form

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

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.47.31048

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15 February 2018

PubMed ID

9813003

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15 February 2018