Search Results - "Hofbauerová, Kateřina"

Refine Results
  1. 1

    Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models by Pazderková, Markéta, Maloň, Petr, Zíma, Vlastimil, Hofbauerová, Kateřina, Kopecký, Jr, Vladimír, Kočišová, Eva, Pazderka, Tomáš, Čeřovský, Václav, Bednárová, Lucie

    “…We have investigated structural changes of peptides related to antimicrobial peptide Halictine-1 (HAL-1) induced by interaction with various membrane-mimicking…”
    Get full text
    Journal Article
  2. 2
  3. 3
  4. 4
  5. 5

    Influence of ligand binding on structure and thermostability of human α1-acid glycoprotein by Kopecký Jr, Vladimír, Ettrich, Rüdiger, Pazderka, Tomáš, Hofbauerová, Kateřina, Řeha, David, Baumruk, Vladimír

    Published in Journal of molecular recognition (01-02-2016)
    “…Ligand binding of neutral progesterone, basic propranolol, and acidic warfarin to human α1‐acid glycoprotein (AGP) was investigated by Raman spectroscopy. The…”
    Get full text
    Journal Article
  6. 6
  7. 7
  8. 8
  9. 9

    Eight Amino Acids Form the ATP Recognition Site of Na+/K+-ATPase by Kubala, Martin, Teisinger, Jan, Ettrich, Rüdiger, Hofbauerová, Kateřina, Kopecký, Vladimír, Baumruk, Vladimír, Krumscheid, Rita, Plášek, Jaromír, Schoner, Wilhelm, Amler, Evžen

    Published in Biochemistry (Easton) (03-06-2003)
    “…Point mutations of a part of the H4−H5 loop (Leu354−Ile604) of Na+/K+-ATPase have been used to study the ATP and TNP-ATP binding affinities. Besides the…”
    Get full text
    Journal Article
  10. 10

    The phosphatase activity of the isolated H4‐H5 loop of Na+/K+ ATPase resides outside its ATP binding site by Krumscheid, Rita, Ettrich, Rüdiger, Sovová, Zofie, Sušánková, Klára, Lánský, Zdeněk, Hofbauerová, Kateřina, Linnertz, Holger, Teisinger, Jan, Amler, Evz̆en, Schoner, Wilhelm

    Published in European journal of biochemistry (01-10-2004)
    “…The structural stability of the large cytoplasmic domain (H4‐H5 loop) of mouse α1 subunit of Na+/K+ ATPase (L354–I777), the number and the location of its…”
    Get full text
    Journal Article
  11. 11

    Structure of human [formula omitted]-acid glycoprotein and its high-affinity binding site by Kopecký, Vladimı́r, Ettrich, Rüdiger, Hofbauerová, Kateřina, Baumruk, Vladimı́r

    “…Secondary and tertiary structures of human blood α 1-acid glycoprotein, a member of the lipocalin family, have been studied for the first time by infrared and…”
    Get full text
    Journal Article
  12. 12

    Phe(475) and Glu(446) but not Ser(445) participate in ATP-binding to the alpha-subunit of Na(+)/K(+)-ATPase by Kubala, Martin, Hofbauerová, Katerina, Ettrich, Rüdiger, Kopecký, Jr, Vladimír, Krumscheid, Rita, Plásek, Jaromír, Teisinger, Jan, Schoner, Wilhelm, Amler, Evzen

    “…The ATP-binding site of Na(+)/K(+)-ATPase is localized on the large cytoplasmic loop of the alpha-subunit between transmembrane helices H(4) and H(5)…”
    Get full text
    Journal Article
  13. 13

    Different amyloid β42 preparations induce different cell death pathways in the model of SH-SY5Y neuroblastoma cells by Özdemir, Alp Yigit, Hofbauerová, Kateřina, Kopecký, Vladimír, Novotný, Jiří, Rudajev, Vladimír

    Published in Cellular & molecular biology letters (17-11-2024)
    “…Abstract Amyloid β42 (Aβ42) plays a decisive role in the pathology of Alzheimer’s disease. The Aβ42 peptide can aggregate into various supramolecular…”
    Get full text
    Journal Article
  14. 14

    ATP-binding is stabilized by a stacking interaction within the binding site of Na +/K +-ATPase by Hofbauerová, Kateřina, Kopecký, Vladimı́r, Ettrich, Rüdiger, Kubala, Martin, Teisinger, Jan, Amler, Evžen

    “…Site-directed mutagenesis was applied to modify phenylalanines (Phe 475Trp, Phe 548Tyr, and both) to generate mutants on the basis of molecular modeling of the…”
    Get full text
    Journal Article
  15. 15
  16. 16
  17. 17
  18. 18
  19. 19

    TRPM6 N-Terminal CaM- and S100A1-Binding Domains by Zouharova, Monika, Herman, Petr, Hofbauerová, Kateřina, Vondrasek, Jiri, Bousova, Kristyna

    “…Transient receptor potential (TRPs) channels are crucial downstream targets of calcium signalling cascades. They can be modulated either by calcium itself…”
    Get full text
    Journal Article
  20. 20