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SAXS
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RNDr. Lenka Faltová Ph.D.
Academic staff at Faculty of Science
10 publications
Publications
publication
Role of the EF-hand-like Motif in the 14-3-3 Protein-mediated Activation of Yeast Neutral Trehalase Nth1
2014 |
Faculty of Science, Central Library of Charles University, First Faculty of Medicine, Faculty of Physical Education and Sport
publication
Biophysical and Structural Characterization of the Thioredoxin-binding Domain of Protein Kinase ASK1 and Its Interaction with Reduced Thioredoxin*
2014 |
Faculty of Science, Faculty of Mathematics and Physics, Central Library of Charles University
publication
Structural Basis for the 14-3-3 Protein-dependent Inhibition of the Regulator of G Protein Signaling 3 (RGS3) Function
2011 |
Faculty of Science, Faculty of Mathematics and Physics, Central Library of Charles University
publication
Mechanisms of the 14-3-3 Protein Function: Regulation of Protein Function Through Conformational Modulation
2014 |
Faculty of Science, Central Library of Charles University
publication
Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5
2013 |
Faculty of Science
publication
Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding
2012 |
Faculty of Science, Faculty of Mathematics and Physics
publication
Role of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1
2012 |
Faculty of Science
publication
The C-Terminal Segment of Yeast BMH Proteins Exhibits Different Structure Compared to Other 14-3-3 Protein Isoforms
2010 |
Faculty of Science, Faculty of Mathematics and Physics
publication
14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)
2010 |
Faculty of Science, Faculty of Mathematics and Physics
publication
Structure of the human FOXO4-DBD-DNA complex at 1.9 A resolution reveals new details of FOXO binding to the DNA.
2010 |
Faculty of Science
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