Prion protein self-peptides

Alan Rigter; Jan Priem; Drophatie Timmers-Parohi; Jan P.M. Langeveld; Fred G. van Zijderveld; Alex Bossers

Prion protein self-peptides

Alan Rigter, Jan Priem, Drophatie Timmers-Parohi, Jan P.M. Langeveld, Fred G. van Zijderveld, Alex Bossers

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic › peer-review

Abstract

Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (^PrPC) into the scrapie associated isoform (PrP^Sc), are poorly understood. Selective self-interaction between PrP molecules forms a basis underlying the observed differences of the PrP^C into PrPSc conversion process (agent replication). The importance of previously peptide-scanning mapped ovine PrP self-interaction domains on this conversion was investigated by studying the ability of six of these ovine PrP based peptides to modulate two processes, PrP self-interaction and conversion.

Original language	English
Title of host publication	Prion Biology
Subtitle of host publication	Research and Advances
Editors	V. Beringue
Publisher	Apple Academic Press Inc
Pages	87-112
Number of pages	26
Edition	1
ISBN (Electronic)	9781466578166
ISBN (Print)	9781926895376
Publication status	Published - 1 Jan 2013

Keywords

Glycosaminoglycan
Peptides
Scrapie
Sonication
Western blotting

Cite this

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title = "Prion protein self-peptides",

abstract = "Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood. Selective self-interaction between PrP molecules forms a basis underlying the observed differences of the PrPC into PrPSc conversion process (agent replication). The importance of previously peptide-scanning mapped ovine PrP self-interaction domains on this conversion was investigated by studying the ability of six of these ovine PrP based peptides to modulate two processes, PrP self-interaction and conversion.",

keywords = "Glycosaminoglycan, Peptides, Scrapie, Sonication, Western blotting",

author = "Alan Rigter and Jan Priem and Drophatie Timmers-Parohi and Langeveld, {Jan P.M.} and {van Zijderveld}, {Fred G.} and Alex Bossers",

year = "2013",

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language = "English",

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T1 - Prion protein self-peptides

AU - Rigter, Alan

AU - Priem, Jan

AU - Timmers-Parohi, Drophatie

AU - Langeveld, Jan P.M.

AU - van Zijderveld, Fred G.

AU - Bossers, Alex

PY - 2013/1/1

Y1 - 2013/1/1

N2 - Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood. Selective self-interaction between PrP molecules forms a basis underlying the observed differences of the PrPC into PrPSc conversion process (agent replication). The importance of previously peptide-scanning mapped ovine PrP self-interaction domains on this conversion was investigated by studying the ability of six of these ovine PrP based peptides to modulate two processes, PrP self-interaction and conversion.

AB - Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood. Selective self-interaction between PrP molecules forms a basis underlying the observed differences of the PrPC into PrPSc conversion process (agent replication). The importance of previously peptide-scanning mapped ovine PrP self-interaction domains on this conversion was investigated by studying the ability of six of these ovine PrP based peptides to modulate two processes, PrP self-interaction and conversion.

KW - Glycosaminoglycan

KW - Peptides

KW - Scrapie

KW - Sonication

KW - Western blotting

M3 - Chapter

AN - SCOPUS:85054219913

SN - 9781926895376

SP - 87

EP - 112

BT - Prion Biology

A2 - Beringue, V.

PB - Apple Academic Press Inc

ER -

Prion protein self-peptides

Abstract

Keywords

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