Semisynthetic Modification of Tau Protein with Di-Ubiquitin Chains for Aggregation Studies
Ubiquitin, a protein modifier that regulates diverse essential cellular processes, is also a component of the protein inclusions characteristic of many neurodegenerative disorders. In Alzheimer’s disease, the microtubule associated tau protein accumulates within damaged neurons in the form of cross-...
Main Authors: | Francesca Munari, Carlo Giorgio Barracchia, Francesca Parolini, Roberto Tira, Luigi Bubacco, Michael Assfalg, Mariapina D’Onofrio |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2020-06-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | https://www.mdpi.com/1422-0067/21/12/4400 |
Similar Items
-
Unsaturated Fatty Acid-Induced Conformational Transitions and Aggregation of the Repeat Domain of Tau
by: Carlo Giorgio Barracchia, et al.
Published: (2020-06-01) -
The determinants of chain type specificity and the mechanism of polyubiquitination by HECT E3s
by: Kim, Hyung Cheol
Published: (2011) -
Mechanisms of Generating Polyubiquitin Chains of Different Topology
by: Randy Suryadinata, et al.
Published: (2014-07-01) -
9-Norlignans: Occurrence, Properties and Their Semisynthetic Preparation from Hydroxymatairesinol
by: Patrik Eklund, et al.
Published: (2019-01-01) -
The ubiquitin system and Kaposi’s sarcoma-associated herpesvirus
by: Akira eAshizawa, et al.
Published: (2012-02-01)