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Diverse functions of the prion protein - Does proteolytic processing hold the key?

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Diverse functions of the prion protein - Does proteolytic processing hold the key? / Linsenmeier, Luise; Altmeppen, Hermann C; Wetzel, Sebastian; Mohammadi, Behnam; Saftig, Paul; Glatzel, Markus.

in: BBA-MOL CELL RES, Jahrgang 1864, Nr. 11 Pt B, 11.2017, S. 2128-2137.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Linsenmeier, L, Altmeppen, HC, Wetzel, S, Mohammadi, B, Saftig, P & Glatzel, M 2017, 'Diverse functions of the prion protein - Does proteolytic processing hold the key?', BBA-MOL CELL RES, Jg. 1864, Nr. 11 Pt B, S. 2128-2137. https://doi.org/10.1016/j.bbamcr.2017.06.022

APA

Linsenmeier, L., Altmeppen, H. C., Wetzel, S., Mohammadi, B., Saftig, P., & Glatzel, M. (2017). Diverse functions of the prion protein - Does proteolytic processing hold the key? BBA-MOL CELL RES, 1864(11 Pt B), 2128-2137. https://doi.org/10.1016/j.bbamcr.2017.06.022

Vancouver

Linsenmeier L, Altmeppen HC, Wetzel S, Mohammadi B, Saftig P, Glatzel M. Diverse functions of the prion protein - Does proteolytic processing hold the key? BBA-MOL CELL RES. 2017 Nov;1864(11 Pt B):2128-2137. https://doi.org/10.1016/j.bbamcr.2017.06.022

Bibtex

@article{5890a445803e402cad04dd43e2947bdd,
title = "Diverse functions of the prion protein - Does proteolytic processing hold the key?",
abstract = "Proteolytic processing of the cellular and disease-associated form of the prion protein leads to generation of bioactive soluble prion protein fragments and modifies the structure and function of its cell-bound form. The nature of proteases responsible for shedding, α-, β-, and γ-cleavage of the prion protein are only partially identified and their regulation is largely unknown. Here, we provide an overview of the increasingly multifaceted picture of prion protein proteolysis and shed light on physiological and pathological roles associated with these cleavages. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.",
keywords = "Journal Article, Review",
author = "Luise Linsenmeier and Altmeppen, {Hermann C} and Sebastian Wetzel and Behnam Mohammadi and Paul Saftig and Markus Glatzel",
note = "Copyright {\textcopyright} 2017 Elsevier B.V. All rights reserved.",
year = "2017",
month = nov,
doi = "10.1016/j.bbamcr.2017.06.022",
language = "English",
volume = "1864",
pages = "2128--2137",
journal = "BBA-MOL CELL RES",
issn = "0167-4889",
publisher = "Elsevier",
number = "11 Pt B",

}

RIS

TY - JOUR

T1 - Diverse functions of the prion protein - Does proteolytic processing hold the key?

AU - Linsenmeier, Luise

AU - Altmeppen, Hermann C

AU - Wetzel, Sebastian

AU - Mohammadi, Behnam

AU - Saftig, Paul

AU - Glatzel, Markus

N1 - Copyright © 2017 Elsevier B.V. All rights reserved.

PY - 2017/11

Y1 - 2017/11

N2 - Proteolytic processing of the cellular and disease-associated form of the prion protein leads to generation of bioactive soluble prion protein fragments and modifies the structure and function of its cell-bound form. The nature of proteases responsible for shedding, α-, β-, and γ-cleavage of the prion protein are only partially identified and their regulation is largely unknown. Here, we provide an overview of the increasingly multifaceted picture of prion protein proteolysis and shed light on physiological and pathological roles associated with these cleavages. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.

AB - Proteolytic processing of the cellular and disease-associated form of the prion protein leads to generation of bioactive soluble prion protein fragments and modifies the structure and function of its cell-bound form. The nature of proteases responsible for shedding, α-, β-, and γ-cleavage of the prion protein are only partially identified and their regulation is largely unknown. Here, we provide an overview of the increasingly multifaceted picture of prion protein proteolysis and shed light on physiological and pathological roles associated with these cleavages. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.

KW - Journal Article

KW - Review

U2 - 10.1016/j.bbamcr.2017.06.022

DO - 10.1016/j.bbamcr.2017.06.022

M3 - SCORING: Journal article

C2 - 28693923

VL - 1864

SP - 2128

EP - 2137

JO - BBA-MOL CELL RES

JF - BBA-MOL CELL RES

SN - 0167-4889

IS - 11 Pt B

ER -