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 bindingArtificial proteins as allosteric modulators of PDZ3 and SH3 in two-domain constructs: A computational characterization of novel chimeric proteins.Role 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.In-situ enrichment of phosphopeptides on MALDI plates modified by ambient ion landing.Structural basis of 14-3-3 protein functions.Cysteine residues mediate high-affinity binding of thioredoxin to ASK1.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).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 Thr232.14-3-3 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.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-2Effect 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 moleculesThe C-terminal segment of yeast BMH proteins exhibits different structure compared to other 14-3-3 protein isoformsCaMKK2 kinase domain interacts with the autoinhibitory region through the N-terminal lobe including the RP insert14-3-3 protein binding blocks the dimerization interface of caspase-2
P50
Q27660347-6593A10D-A5E0-458C-B670-47C1FE5234B0Q27666143-7649EDF9-C687-4947-9978-CCB07624ED86Q28263962-9BE3274C-365C-4263-9779-97C34286F449Q28284616-61D813A0-9AAA-4B04-B792-BB5E04A359A4Q30008902-E2BF5284-AAB9-4E8E-9B9E-A5A0247D3A70Q30361175-5757C0A1-BB9F-4F2A-B82C-17A77819EC68Q30909863-8DC50A38-FC8E-438B-9757-B21F95755BC9Q31048647-3E651DDE-D9A8-4709-9592-788EC73F778EQ33439373-EA441F15-CE21-428D-AD81-67B790D0D4F3Q34421022-123DACF7-A6A4-493F-9C20-CCAB48BC1CC2Q34423510-0BCB5738-9DB5-4072-9A52-91C66229035BQ37932715-BCBABF40-6F66-4D4A-8EE6-F50190351559Q39428397-87AD0FB3-F00D-420D-AD93-F51BC59D653EQ40496239-E0656D51-3D25-459F-BECA-025D96B3FB36Q40942320-4BB16BC9-940B-4315-9805-45742D19C749Q41161844-0D183B6A-1929-46E9-A60B-1824F7D27F42Q42282984-3EAE10C2-D709-4CFA-A849-0B8E68BC54F1Q43891825-3F7A667A-3104-466A-A28F-30EE5A432D6EQ44352809-FCD4F983-023B-487E-B25C-F7201F8CEA1BQ44653252-99E4D2F1-980A-458B-96A3-45F8D5975951Q45044242-D0ACEF0B-C322-4C34-8FBD-0FD8B5C09C26Q47583534-446FC4C9-D689-4C43-AC54-86AD89A6BE6BQ47608984-2C968F07-1F23-4710-8744-BB276A1DE0F6Q47751647-A3F84218-438C-4AAF-8C83-02FBE8F5EAD4Q51062260-CA4E1483-B73F-49E1-8AB4-139FBBEC4972Q52323429-583FB409-15C3-4B19-99CF-2FECDB264E09Q57036396-CD9C4022-8381-481E-B87E-1F9358C92000Q79214656-B923AC38-BE0A-4854-9229-3CCA49A42319Q80812573-13B5FB34-D739-423A-9659-B1DE3FECB1C3Q83225642-E9B1C513-BA43-47B7-90BD-2A3602EFEAC3Q84042551-E5C29C42-4084-44EE-BE21-CEA0AEEB86F2Q90573965-A6526BA3-0D0E-447C-86F8-E9C6CE7756D5Q92796504-D85F0BE1-FFDD-4C08-B18A-C1B2DF6836DD
P50
description
biofyzička
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researcher
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հետազոտող
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name
Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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type
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Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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Veronika Obšilová
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prefLabel
Veronika Obšilová
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Veronika Obšilová
@cs
Veronika Obšilová
@en
Veronika Obšilová
@es
Veronika Obšilová
@nl
Veronika Obšilová
@sl
P214
P21
P214
P31
P496
0000-0003-4887-0323