C-terminal Substitution of MDM2 interacting peptides modulates binding affinity by distinctive mechanisms
10.1371/journal.pone.0024122
Saved in:
Main Authors: | Brown, C.J., Dastidar, S.G., Quah, S.T., Lim, A., Chia, B., Verma, C.S. |
---|---|
Other Authors: | BIOLOGICAL SCIENCES |
Format: | Article |
Published: |
2014
|
Online Access: | http://scholarbank.nus.edu.sg/handle/10635/100380 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | National University of Singapore |
Similar Items
-
Why is F19Ap53 unable to bind MDM2? Simulations suggest crack propagation modulates binding
by: Dastidar, S.G., et al.
Published: (2014) -
Modulation of p53 binding to MDM2: Computational studies reveal important roles of Tyr100
by: Dastidar, S.G., et al.
Published: (2014) -
Systematic mutational analysis of an ubiquitin ligase (MDM2)-binding peptide: Computational studies
by: Liu, Y., et al.
Published: (2014) -
Mechanism of stapled peptide binding to MDM2: Possible consequences for peptide design
by: Sim, A.Y.L., et al.
Published: (2014) -
Mechanism of stapled peptide binding to MDM2 : possible consequences for peptide design
by: Sim, Adelene Y. L., et al.
Published: (2015)