U
Ulrike Holzgrabe
Researcher at University of Würzburg
Publications - 591
Citations - 11158
Ulrike Holzgrabe is an academic researcher from University of Würzburg. The author has contributed to research in topics: Allosteric regulation & Capillary electrophoresis. The author has an hindex of 45, co-authored 566 publications receiving 9806 citations. Previous affiliations of Ulrike Holzgrabe include Jagiellonian University & University of Illinois at Chicago.
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Effects of fluoroquinolones on HERG channels and on pancreatic β-cell ATP-sensitive K+ channels
TL;DR: The structural requirements for fluoroquinolones to inhibit I(Kr) currents and K(ATP) currents appear to differ, and the amino group at position C(5) seems to be primarily responsible for the strong HERG current blocking property of sparfloxacin.
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Influence of charged aerosol detector instrument settings on the ultra-high-performance liquid chromatography analysis of fatty acids in polysorbate 80.
TL;DR: Overall, this new UHPLC method method offers improved detection limits, as well as time savings of over 75% and eluent savings of more than 40% compared to the previously published HPLC-CAD method for polysorbate analysis.
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Impurity profiling of atropine sulfate by microemulsion electrokinetic chromatography.
Yaser Bitar,Ulrike Holzgrabe +1 more
TL;DR: Good agreement was obtained between the established MEEKC method and the traditional RP-HPLC method on the detection and determination of atropine sulfate related substances at impurity levels given in the European Pharmacopoeia.
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Search for the pharmacophore in kappa-agonistic diazabicyclo[3.3.1]nonan-9-one-1,5-diesters and arylacetamides
TL;DR: The purpose of this study was to unravel the active conformation of the bicyclononanones using well‐known k‐selective agonists such as ketocyclacocine, arylacetamides, several isoquinolines, CI‐977, and four stereoisomers of EMD‐61753 for comparison.
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Ligand-Specific Restriction of Extracellular Conformational Dynamics Constrains Signaling of the M2 Muscarinic Receptor.
Marcel Bermudez,Andreas Bock,Andreas Bock,Fabian Krebs,Ulrike Holzgrabe,Klaus Mohr,Martin J. Lohse,Martin J. Lohse,Gerhard Wolber +8 more
TL;DR: The extent of closure of the extracellular, allosteric binding site interferes with the activation of certain G proteins and is found to allow the rational design of Gi-biased agonists at the M2 receptor and delineate a simple principle which may be translated to other GPRCs.