about
14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)Structure of the human FOXO4-DBD-DNA complex at 1.9 Å resolution reveals new details of FOXO binding to the DNAThe 14-3-3 protein affects the conformation of the regulatory domain of human tyrosine hydroxylaseBoth the N-terminal loop and wing W2 of the forkhead domain of transcription factor Foxo4 are important for DNA bindingRole of the EF-hand-like motif in the 14-3-3 protein-mediated activation of yeast neutral trehalase Nth1.The interactions of the C-terminal region of the TRPC6 channel with calmodulin.Role of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1.14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.Ligand binding to the human MT2 melatonin receptor: the role of residues in transmembrane domains 3, 6, and 7.A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.Structural basis of 14-3-3 protein functions.Cysteine residues mediate high-affinity binding of thioredoxin to ASK1.Hippo/Mst1 stimulates transcription of the proapoptotic mediator NOXA in a FoxO1-dependent manner.Participation of the Lys313-Ile333 sequence of the purinergic P2X4 receptor in agonist binding and transduction of signals to the channel gate.Molecular modeling of human MT2 melatonin receptor: the role of Val204, Leu272 and Tyr298 in ligand binding.Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein.Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1).Functional characterization of mutants in the transmembrane domains of the rat P2X7 receptor that regulate pore conductivity and agonist sensitivity.Biophysical and structural characterization of the thioredoxin-binding domain of protein kinase ASK1 and its interaction with reduced thioredoxinStructural basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.Detailed kinetic analysis of the interaction between the FOXO4-DNA-binding domain and DNA.14-3-3zeta C-terminal stretch changes its conformation upon ligand binding and phosphorylation at Thr232.Two 14-3-3 binding motifs are required for stable association of Forkhead transcription factor FOXO4 with 14-3-3 proteins and inhibition of DNA binding.14-3-3 protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding.Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1.Structural aspects of protein kinase ASK1 regulation.Modulators of 14-3-3 Protein-Protein Interactions.Human procaspase-2 phosphorylation at both S139 and S164 is required for 14-3-3 binding.Structural Basis for the 14-3-3 Protein-Dependent Inhibition of Phosducin Function.14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2).14-3-3 protein masks the nuclear localization sequence of caspase-2Different cation binding to the I domains of α1 and α2 integrins: implication of the binding site structureEffects of fluorescent pseudo-ATP and ATP-metal analogs on secondary structure of Na(+)/K(+)-ATPaseThe isolated H4-H5 cytoplasmic loop of Na,K-ATPase overexpressed in Escherichia coli retains its ability to bind ATPMolecular distance measurements reveal an (alpha beta)2 dimeric structure of Na+/K+-ATPase. High affinity ATP binding site and K+-activated phosphatase reside on different alpha-subunitsErythrosin 5'-isothiocyanate labels Cys549 as part of the low-affinity ATP binding site of Na+/K+-ATPaseMicroenvironment of the high affinity ATP-binding site of Na+/K+-ATPase is slightly acidicEffect of aminophospholipid glycation on order parameter and hydration of phospholipid bilayerATP binding site on the C-terminus of the vanilloid receptorModulating FOXO3 transcriptional activity by small, DBD-binding molecules
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description
researcher ORCID ID = 0000-0003-4602-1272
@en
wetenschapper
@nl
name
Tomas Obsil
@ast
Tomas Obsil
@en
Tomas Obsil
@es
Tomas Obsil
@nl
type
label
Tomas Obsil
@ast
Tomas Obsil
@en
Tomas Obsil
@es
Tomas Obsil
@nl
prefLabel
Tomas Obsil
@ast
Tomas Obsil
@en
Tomas Obsil
@es
Tomas Obsil
@nl
P106
P108
P21
P31
P496
0000-0003-4602-1272