Structural analysis of prion proteins by means of drift cell and traveling wave ion mobility mass spectrometry. (Q51774612)

12 April 2018

title

Structural analysis of prion proteins by means of drift cell and traveling wave ion mobility mass spectrometry. (English)

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12 April 2018

main subject

prion protein family

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author

Konstantinos Thalassinos

2

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Philip J. Robinson

7

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James Scrivens

10

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Megan Grabenauer

object named as

Megan Grabenauer

3

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author name string

Gillian R Hilton

1

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Narinder Sanghera

4

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Susan E Slade

5

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Thomas Wyttenbach

6

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Teresa J T Pinheiro

8

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Michael T Bowers

9

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publication date

28 January 2010

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Journal of the American Society for Mass Spectrometry

published in

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volume

21

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issue

5

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page(s)

845-854

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https://scigraph.springernature.com/pub.10.1016/j.jasms.2010.01.017

exact match

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cites work

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Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells

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

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12 December 2020

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The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive

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Darwinian evolution of prions in cell culture

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Unraveling the details of prion (con)formation(s): recent advances by mass spectrometry

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Formation of soluble oligomers and amyloid fibrils with physical properties of the scrapie isoform of the prion protein from the C-terminal domain of recombinant murine prion protein mPrP-(121-231)

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DOI

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12 April 2018

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12 April 2018