Detalhe da pesquisa
1.
Residue alterations within a conserved hydrophobic pocket influence light, oxygen, voltage photoreceptor dark recovery.
Photochem Photobiol Sci
; 22(4): 713-727, 2023 Apr.
Artigo
em Inglês
| MEDLINE | ID: mdl-36480084
2.
The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria.
Biochemistry
; 55(4): 659-74, 2016 Feb 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-26685112
3.
The Short Term Influence of Chest Physiotherapy on Lung Function Parameters in Children With Cystic Fibrosis and Primary Ciliary Dyskinesia.
Front Pediatr
; 10: 858410, 2022.
Artigo
em Inglês
| MEDLINE | ID: mdl-35676908
4.
Proline Restricts Loop I Conformation of the High Affinity WW Domain from Human Nedd4-1 to a Ligand Binding-Competent Type I ß-Turn.
J Phys Chem B
; 122(15): 4219-4230, 2018 04 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-29595969
5.
Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis.
ACS Catal
; 8(5): 3971-3984, 2018 May 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-30101036
6.
1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase.
Biomol NMR Assign
; 11(2): 197-201, 2017 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-28560616
7.
Data describing the solution structure of the WW3* domain from human Nedd4-1.
Data Brief
; 8: 605-12, 2016 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-27419198