Detalhe da pesquisa
1.
Identification of the Tau phosphorylation pattern that drives its aggregation.
Proc Natl Acad Sci U S A
; 114(34): 9080-9085, 2017 08 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-28784767
2.
Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase.
J Biol Chem
; 291(14): 7742-53, 2016 Apr 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-26858248
3.
A ß-Turn Motif in the Steroid Hormone Receptor's Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52.
Biochemistry
; 55(38): 5366-76, 2016 09 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-27641460
4.
Nuclear magnetic resonance spectroscopy characterization of interaction of Tau with DNA and its regulation by phosphorylation.
Biochemistry
; 54(7): 1525-33, 2015 Feb 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-25623359
5.
Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein.
Biochemistry
; 53(18): 3020-32, 2014 May 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-24708343
6.
The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein.
Methods Mol Biol
; 1523: 179-213, 2017.
Artigo
em Inglês
| MEDLINE | ID: mdl-27975251
7.
NMR Meets Tau: Insights into Its Function and Pathology.
Biomolecules
; 6(2)2016 Jun 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-27338491
8.
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.
J Vis Exp
; (118)2016 12 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-28060278