Cargando…
Mechanism of amyloid β−protein dimerization determined using single−molecule AFM force spectroscopy
Aβ42 and Aβ40 are the two primary alloforms of human amyloid β−protein (Aβ). The two additional C−terminal residues of Aβ42 result in elevated neurotoxicity compared with Aβ40, but the molecular mechanism underlying this effect remains unclear. Here, we used single−molecule force microscopy to chara...
Autores principales: | Lv, Zhengjian, Roychaudhuri, Robin, Condron, Margaret M., Teplow, David B., Lyubchenko, Yuri L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791449/ https://www.ncbi.nlm.nih.gov/pubmed/24096987 http://dx.doi.org/10.1038/srep02880 |
Ejemplares similares
-
Misfolding and interactions of Aß proteins: Insight from single molecule experiments and computational analyses
por: Zhengjian, Lv, et al.
Publicado: (2013) -
AFM Probing of Amyloid-Beta 42 Dimers and Trimers
por: Maity, Sibaprasad, et al.
Publicado: (2020) -
Spontaneous self-assembly of amyloid β (1–40) into dimers
por: Hashemi, Mohtadin, et al.
Publicado: (2019) -
Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses
por: Lyubchenko, Yuri L.
Publicado: (2015) -
Ligand Binding Stabilizes Cellulosomal Cohesins as Revealed by AFM-based Single-Molecule Force Spectroscopy
por: Verdorfer, Tobias, et al.
Publicado: (2018)