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Philipp D. Pollheimer

Researcher at Johannes Kepler University of Linz

Publications -  9
Citations -  536

Philipp D. Pollheimer is an academic researcher from Johannes Kepler University of Linz. The author has contributed to research in topics: Receptor & Avidin. The author has an hindex of 8, co-authored 9 publications receiving 499 citations. Previous affiliations of Philipp D. Pollheimer include Hong Kong University of Science and Technology & Medical University of Vienna.

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Linking of Sensor Molecules with Amino Groups to Amino-Functionalized AFM Tips

TL;DR: A uncompromising solution to the problem of undesired bivalent reaction of bifunctional linkers with adjacent NH2 groups on the tip surface was found with the help of a new cross-linker (“acetal-PEG-NHS”) which possesses one activated carboxyl group and one acetal-protected benzaldehyde function.
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Single-molecule force spectroscopy and imaging of the vancomycin/D-Ala-D-Ala interaction.

TL;DR: The ability of single-molecule atomic force microscopy with antibiotic-modified tips to measure the specific binding forces of vancomycin and to map individual ligands on living bacteria is demonstrated.
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Antibody linking to atomic force microscope tips via disulfide bond formation.

TL;DR: The coupling scheme was well-reproduced on amino-functionalized silicon nitride chips, and the number of covalently bound biotin-IgG per microm2 was estimated by the amount of specifically bound ExtrAvidin-peroxidase conjugate.
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Molecular Determinants within N Terminus of Orai3 Protein That Control Channel Activation and Gating

TL;DR: In aggregate, the N-terminal conserved region plays a multifaceted role in Orai3 current gating with distinct structural requirements for STIM1- and 2-APB-stimulated activation.
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Nanoscale DNA Tetrahedra Improve Biomolecular Recognition on Patterned Surfaces

TL;DR: In assays testing the molecular accessibility via DNA hybridization and protein capturing, tetrahedron-tethered receptors outperformed conventional immobilization approaches with regard to specificity and amount of captured polypeptide by a factor of up to seven.