Cargando…
APP dimer formation is initiated in the endoplasmic reticulum and differs between APP isoforms
The amyloid precursor protein (APP) is part of a larger gene family, which has been found to form homo- or heterotypic complexes with its homologues, whereby the exact molecular mechanism and origin of dimer formation remains elusive. In order to assess the cellular location of dimerization, we have...
Autores principales: | Isbert, Simone, Wagner, Katja, Eggert, Simone, Schweitzer, Andrea, Multhaup, Gerd, Weggen, Sascha, Kins, Stefan, Pietrzik, Claus U. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SP Birkhäuser Verlag Basel
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3314181/ https://www.ncbi.nlm.nih.gov/pubmed/22105709 http://dx.doi.org/10.1007/s00018-011-0882-4 |
Ejemplares similares
-
Structural aspects and physiological consequences of APP/APLP trans-dimerization
por: Baumkötter, Frederik, et al.
Publicado: (2011) -
LRP1 Modulates APP Intraneuronal Transport and Processing in Its Monomeric and Dimeric State
por: Herr, Uta-Mareike, et al.
Publicado: (2017) -
APP family member dimeric complexes are formed predominantly in synaptic compartments
por: Schilling, Sandra, et al.
Publicado: (2023) -
Fe65-PTB2 Dimerization Mimics Fe65-APP Interaction
por: Feilen, Lukas P., et al.
Publicado: (2017) -
Shedding of APP limits its synaptogenic activity and cell adhesion properties
por: Stahl, Ronny, et al.
Publicado: (2014)