Search Results - "Niemiec, Moritz S."

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  1. 1

    Role of metal in folding and stability of copper proteins in vitro by Palm-Espling, Maria E., Niemiec, Moritz S., Wittung-Stafshede, Pernilla

    Published in Biochimica et biophysica acta (01-09-2012)
    “…Metal coordination is required for function of many proteins. For biosynthesis of proteins coordinating a metal, the question arises if the metal binds before,…”
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  2. 2
  3. 3

    In vitro thermodynamic dissection of human copper transfer from chaperone to target protein by Niemiec, Moritz S, Weise, Christoph F, Wittung-Stafshede, Pernilla

    Published in PloS one (04-05-2012)
    “…Transient protein-protein and protein-ligand interactions are fundamental components of biological activity. To understand biological activity, not only the…”
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  4. 4

    Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro by Petzoldt, Svenja, Kahra, Dana, Kovermann, Michael, Dingeldein, Artur PG, Niemiec, Moritz S., Ådén, Jörgen, Wittung-Stafshede, Pernilla

    Published in Biometals (01-06-2015)
    “…After Ctr1-mediated copper ion (Cu) entry into the human cytoplasm, chaperones Atox1 and CCS deliver Cu to P 1B -type ATPases and to superoxide dismutase,…”
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  5. 5

    Human Copper Chaperone Atox1 Translocates to the Nucleus but does not Bind DNA In Vitro by Kahra, Dana, Mondol, Tanumoy, Niemiec, Moritz S, Wittung-Stafshede, Pernilla

    Published in Protein and peptide letters (01-01-2015)
    “…After Ctr1-mediated cell uptake, copper (Cu) is transported by the cytoplasmic Cu chaperone Atox1 to P1B type ATPases ATP7A and ATP7B in the Golgi network, for…”
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  6. 6

    Enthalpy-entropy compensation at play in human copper ion transfer by Niemiec, Moritz S., Dingeldein, Artur P. G., Wittung-Stafshede, Pernilla

    Published in Scientific reports (27-05-2015)
    “…Copper (Cu) is an essential trace element but toxic in free form. After cell uptake, Cu is transferred, via direct protein-protein interactions, from the…”
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  7. 7

    T versus D in the MTCXXC motif of copper transport proteins plays a role in directional metal transport by Niemiec, Moritz S., Dingeldein, Artur P. G., Wittung-Stafshede, Pernilla

    Published in Journal of biological inorganic chemistry (01-08-2014)
    “…To avoid toxicity and control levels of metal ions, organisms have developed specific metal transport systems. In humans, the cytoplasmic Cu chaperone Atox1…”
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  8. 8

    Small pH and Salt Variations Radically Alter the Thermal Stability of Metal-Binding Domains in the Copper Transporter, Wilson Disease Protein by Nilsson, Lina, Ådén, Jörgen, Niemiec, Moritz S, Nam, Kwangho, Wittung-Stafshede, Pernilla

    Published in The journal of physical chemistry. B (24-10-2013)
    “…Although strictly regulated, pH and solute concentrations in cells may exhibit temporal and spatial fluctuations. Here we study the effect of such changes on…”
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  9. 9

    Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase by Berg, Lotta, Niemiec, Moritz S., Qian, Weixing, Andersson, C. David, Wittung-Stafshede, Pernilla, Ekström, Fredrik, Linusson, Anna

    Published in Angewandte Chemie International Edition (14-12-2012)
    “…Take a closer look: Unexpectedly, a pair of enantiomeric ligands proved to have similar binding affinities for acetylcholinesterase. Further studies indicated…”
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  10. 10

    Discovery of Ligands for ADP-Ribosyltransferases via Docking-Based Virtual Screening by Andersson, C. David, Karlberg, Tobias, Ekblad, Torun, Lindgren, Anders E. G, Thorsell, Ann-Gerd, Spjut, Sara, Uciechowska, Urszula, Niemiec, Moritz S, Wittung-Stafshede, Pernilla, Weigelt, Johan, Elofsson, Mikael, Schüler, Herwig, Linusson, Anna

    Published in Journal of medicinal chemistry (13-09-2012)
    “…The diphtheria toxin-like ADP-ribosyltransferases (ARTDs) are an enzyme family that catalyzes the transfer of ADP-ribose units onto substrate proteins by using…”
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  11. 11

    Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase by Berg, Lotta, Niemiec, Moritz S., Qian, Weixing, Andersson, C. David, Wittung-Stafshede, Pernilla, Ekström, Fredrik, Linusson, Anna

    Published in Angewandte Chemie (14-12-2012)
    “…Schau genau hin: Ein Paar enantiomerer Liganden hatte unerwartet ähnliche Bindungsaffinitäten für Acetylcholinesterase. Die Enantiomeren wiesen verschiedene…”
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    Journal Article