Detalhe da pesquisa
1.
A Consensus Binding Motif for the PP4 Protein Phosphatase.
Mol Cell
; 76(6): 953-964.e6, 2019 12 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-31585692
2.
Proteome-wide analysis of phospho-regulated PDZ domain interactions.
Mol Syst Biol
; 14(8): e8129, 2018 08 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-30126976
3.
The Sign of Nuclear Magnetic Resonance Chemical Shift Difference as a Determinant of the Origin of Binding Selectivity: Elucidation of the Position Dependence of Phosphorylation in Ligands Binding to Scribble PDZ1.
Biochemistry
; 57(1): 66-71, 2018 01 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-29144123
4.
Identification of PDZ Interactions by Proteomic Peptide Phage Display.
Methods Mol Biol
; 2256: 41-60, 2021.
Artigo
em Inglês
| MEDLINE | ID: mdl-34014515
5.
Emergence and evolution of an interaction between intrinsically disordered proteins.
Elife
; 62017 04 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-28398197
6.
Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions.
Sci Rep
; 6: 34269, 2016 10 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-27694853
7.
Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin.
FEBS Lett
; 590(1): 3-12, 2016 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-26787460
8.
Structural basis of Sorcin-mediated calcium-dependent signal transduction.
Sci Rep
; 5: 16828, 2015 Nov 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-26577048
9.
Interaction analysis through proteomic phage display.
Biomed Res Int
; 2014: 176172, 2014.
Artigo
em Inglês
| MEDLINE | ID: mdl-25295249