Academic staff at Second Faculty of Medicine, Faculty of Physical Education and Sport
Classes
- Biophysics +10D0101032 | Second Faculty of Medicine
- Tissue and protein engineering +3D0100015 | Second Faculty of Medicine
- Bionanotechnology in regenerative medicineD01000202 | Second Faculty of Medicine
- Clinical Biophysics +1D0108234 | Second Faculty of Medicine
- Clinical Radiobiology +1D0110255 | Second Faculty of Medicine
- Physics +1D0201301 | Second Faculty of Medicine
- Basic Biophysic +1D0302132 | Second Faculty of Medicine
- Essentials of Biophysics +1D0402008 | Second Faculty of Medicine
- RadiobiologyD0502016 | Second Faculty of Medicine
- Molecular and Clinical RadiobiologyD1502018 | Second Faculty of Medicine
Publications
- Collagen/hydroxyapatite scaffold enriched with polycaprolactone nanofibers, thrombocyte-rich solution and mesenchymal stem cells promotes regeneration in large bone defect in vivo2015 | Second Faculty of Medicine, Faculty of Medicine in Pilsen
- Abdominal closure reinforcement by using polypropylene mesh functionalized with poly-ε-caprolactone nanofibers and growth factors for prevention of incisional hernia formation2014 | Faculty of Physical Education and Sport, Second Faculty of Medicine, Faculty of Medicine in Pilsen, Central Library of Charles University
- Auto-model based computer simulation of Plateau-Rayleigh instability of mixtures of immiscible liquids2010 | Second Faculty of Medicine
- Novel Composite Hyaluronan/Type I Collagen/Fibrin Scaffold Enhances Repair of Osteochondral Defect in Rabbit Knee2008 | Second Faculty of Medicine
- Composite hyaluronate-type I collagen-fibrin scaffold in the therapy of osteochondral defects in miniature pigs2007 | Second Faculty of Medicine
- The phosphatase activity of the isolated H-4-H-5 loop of Na+/K+ ATPase resides outside its ATP binding site2004 | Second Faculty of Medicine
- Protein modeling combined with spectroscopic techniques: An attractive quick alternative to obtain structural information2004 | Second Faculty of Medicine
- The hydrogen bonds between Arg(423) and Glu(472) and other key residues, Asp(443), Ser(477), and Pro(489), are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na+/K+-ATPase2004 | Second Faculty of Medicine
- Eight amino acids are forming the ATP recognition site of Na+/K+ - ATPase2003 | Second Faculty of Medicine
- Hollow nanofibers enriched with liposomesPublication without faculty affiliation
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