Detalhe da pesquisa
1.
Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage.
PLoS Pathog
; 17(11): e1009728, 2021 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-34780577
2.
HACANCOi: a new Hα-detected experiment for backbone resonance assignment of intrinsically disordered proteins.
J Biomol NMR
; 74(12): 741-752, 2020 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-33118136
3.
Dispersion from Cα or NH: 4D experiments for backbone resonance assignment of intrinsically disordered proteins.
J Biomol NMR
; 74(2-3): 147-159, 2020 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-31932991
4.
Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2.
J Biol Chem
; 291(31): 16307-17, 2016 07 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-27268056
5.
Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner.
Biophys J
; 108(4): 903-917, 2015 Feb 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-25692595
6.
A novel structural unit in the N-terminal region of filamins.
J Biol Chem
; 289(12): 8588-98, 2014 Mar 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-24469451
7.
1H, 13C, and 15N NMR chemical shift assignment of LytM N-terminal domain (residues 26-184).
Biomol NMR Assign
; 17(2): 257-263, 2023 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-37742292
8.
Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM.
Biomol NMR Assign
; 2023 Nov 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-37914968
9.
Model of a six immunoglobulin-like domain fragment of filamin A (16-21) built using residual dipolar couplings.
J Am Chem Soc
; 134(15): 6660-72, 2012 Apr 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-22452512
10.
Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs.
Structure
; 30(6): 828-839.e6, 2022 06 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-35390274
11.
1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain.
Biomol NMR Assign
; 15(1): 213-217, 2021 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-33475933
12.
Decreased temperature increases the expression of a disordered bacterial late embryogenesis abundant (LEA) protein that enhances natural transformation.
Virulence
; 12(1): 1239-1257, 2021 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-33939577
13.
The solution structure of the amino-terminal domain of human DNA polymerase epsilon subunit B is homologous to C-domains of AAA+ proteins.
Nucleic Acids Res
; 36(15): 5102-10, 2008 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-18676977
14.
An intraresidual i(HCA)CO(CA)NH experiment for the assignment of main-chain resonances in 15N, 13C labeled proteins.
J Biomol NMR
; 45(3): 301-10, 2009 Nov.
Artigo
em Inglês
| MEDLINE | ID: mdl-19768387
15.
Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins.
BMC Struct Biol
; 9: 17, 2009 Mar 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-19309529
16.
NMR structure of a non-conjugatable, ADP-ribosylation associated, ubiquitin-like domain from Tetrahymena thermophila polyubiquitin locus.
Biochim Biophys Acta Gen Subj
; 1863(4): 749-759, 2019 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-30690122
17.
Arabidopsis RCD1 coordinates chloroplast and mitochondrial functions through interaction with ANAC transcription factors.
Elife
; 82019 02 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-30767893
18.
Structural and Functional Insights Into Lysostaphin-Substrate Interaction.
Front Mol Biosci
; 5: 60, 2018.
Artigo
em Inglês
| MEDLINE | ID: mdl-30018958
19.
1H, 13C and 15N resonance assignments of the new lysostaphin family endopeptidase catalytic domain from Staphylococcus aureus.
Biomol NMR Assign
; 11(1): 69-73, 2017 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-27943001
20.
1H, 13C and 15N NMR chemical shift assignments of A. thaliana RCD1 RST.
Biomol NMR Assign
; 11(2): 207-210, 2017 Oct.
Artigo
em Inglês
| MEDLINE | ID: mdl-28593560