PuSH - Publikationsserver des Helmholtz Zentrums München

Giannopoulou, E.A.* ; Emmanouilidis, L. ; Sattler, M. ; Dodt, G.* ; Wilmanns, M.*

Towards the molecular mechanism of the integration of peroxisomal membrane proteins.

Biochim. Biophys. Acta-Mol. Cell Res. 1863, 863-869 (2016)
Verlagsversion Postprint DOI PMC
Open Access Hybrid
Creative Commons Lizenzvertrag
The correct topogenesis of peroxisomal membrane proteins is a crucial step for the formation of functioning peroxisomes. Although this process has been widely studied, the exact mechanism with which it occurs has not yet been fully characterized. Nevertheless, it is generally accepted that peroxisomes employ three proteins - Pex3, Pex19 and Pex16 in mammals - for the insertion of peroxisomal membrane proteins into the peroxisomal membrane. Structural biology approaches have been utilized for the elucidation of the mechanistic questions of peroxisome biogenesis, mainly by providing information on the architecture of the proteins significant for this process. This review aims to summarize, compare and put into perspective the structural knowledge that has been generated mainly for Pex3 and Pex19 and their interaction partners in recent years.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
5.128
1.311
13
14
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Peroxisomal Membrane Proteins ; Peroxisome Biogenesis ; Pex19 ; Pex3 ; Structural Biology; Tail-anchored Proteins; Endoplasmic-reticulum; Saccharomyces-cerevisiae; Targeting Signals; Import Receptor; Mammalian Peroxisomes; Structural Basis; Matrix Proteins; Human Pex19p; Biogenesis
Sprache englisch
Veröffentlichungsjahr 2016
HGF-Berichtsjahr 2016
ISSN (print) / ISBN 0167-4889
e-ISSN 1879-2596
Quellenangaben Band: 1863, Heft: 5, Seiten: 863-869 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort Amsterdam
Begutachtungsstatus Peer reviewed
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503000-001
Scopus ID 84975807155
Scopus ID 84961179297
Scopus ID 84951086434
PubMed ID 26434995
Erfassungsdatum 2016-01-01