Cargando…
Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses
It is well established that the formation of transthyretin (TTR) amyloid fibrils is linked to the destabilization and dissociation of its tetrameric structure into insoluble aggregates. Isotope labeling is used for the study of TTR by NMR, neutron diffraction, and mass spectrometry (MS). Here MS, th...
Autores principales: | Yee, Ai Woon, Moulin, Martine, Breteau, Nina, Haertlein, Michael, Mitchell, Edward P., Cooper, Jonathan B., Boeri Erba, Elisabetta, Forsyth, V. Trevor |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5094506/ https://www.ncbi.nlm.nih.gov/pubmed/27311939 http://dx.doi.org/10.1002/anie.201602747 |
Ejemplares similares
-
A molecular mechanism for transthyretin amyloidogenesis
por: Yee, Ai Woon, et al.
Publicado: (2019) -
The Production of Matchout-Deuterated Cholesterol and the Study of Bilayer-Cholesterol Interactions
por: Waldie, Sarah, et al.
Publicado: (2019) -
The Importance of a Gatekeeper Residue on the Aggregation of Transthyretin: IMPLICATIONS FOR TRANSTHYRETIN-RELATED AMYLOIDOSES
por: Sant'Anna, Ricardo, et al.
Publicado: (2014) -
Back-exchange of deuterium in neutron crystallography: characterization by IR spectroscopy
por: Yee, Ai Woon, et al.
Publicado: (2017) -
A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines
por: Puglisi, Rita, et al.
Publicado: (2020)