An Alternative Pin1 Binding and Isomerization Site in the N-Terminus Domain of PSD-95
Phosphorylation-dependent peptidyl-prolyl cis-trans isomerization plays key roles in cell cycle progression, the pathogenesis of cancer, and age-related neurodegeneration. Most of our knowledge about the role of phosphorylation-dependent peptidyl-prolyl cis-trans isomerization and the enzyme catalyz...
Main Author: | Jary Y. Delgado |
---|---|
Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2020-03-01
|
Series: | Frontiers in Molecular Neuroscience |
Subjects: | |
Online Access: | https://www.frontiersin.org/article/10.3389/fnmol.2020.00031/full |
Similar Items
-
Pin1 Binding to Phosphorylated PSD-95 Regulates the Number of Functional Excitatory Synapses
by: Jary Y. Delgado, et al.
Published: (2020-03-01) -
Prolyl Isomerase Pin1 in Human Cancer: Function, Mechanism, and Significance
by: Wenchen Pu, et al.
Published: (2020-03-01) -
Synaptic Targeting and Function of SAPAPs Mediated by Phosphorylation-Dependent Binding to PSD-95 MAGUKs
by: Jinwei Zhu, et al.
Published: (2017-12-01) -
Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides
by: Fanni Sebák, et al.
Published: (2023-06-01) -
Neurodevelopmental Disorders Associated with PSD-95 and Its Interaction Partners
by: Amanda M. Levy, et al.
Published: (2022-04-01)