Zobrazeno 1 - 10
of 175
pro vyhledávání: '"Hermann J, Gruber"'
Autor:
Sandra Posch, Camilo Aponte-Santamaría, Richard Schwarzl, Andreas Karner, Matthias Radtke, Frauke Gräter, Tobias Obser, Gesa König, Maria A. Brehm, Hermann J. Gruber, Roland R. Netz, Carsten Baldauf, Reinhard Schneppenheim, Robert Tampé, Peter Hinterdorfer
Publikováno v:
Data in Brief, Vol 8, Iss , Pp 1080-1087 (2016)
We here give information for a deeper understanding of single molecule force spectroscopy (SMFS) data through the example of the blood protein von Willebrand factor (VWF). It is also shown, how fitting of rupture forces versus loading rate profiles i
Externí odkaz:
https://doaj.org/article/a6af907a1b04473db79970e4cbf3d20c
Publikováno v:
Methods and Protocols, Vol 2, Iss 1, p 6 (2019)
Ligand binding to receptors is one of the most important regulatory elements in biology as it is the initiating step in signaling pathways and cascades. Thus, precisely localizing binding sites and measuring interaction forces between cognate recepto
Externí odkaz:
https://doaj.org/article/eae16c5e285b4febbf02a946f660eb09
Autor:
Elke, Oberbichler, Maria, Wiesauer, Eva, Schlögl, Jessica, Stangl, Felix, Faschinger, Günther, Knör, Hermann J, Gruber, Vesa P, Hytönen
Publikováno v:
Methods in enzymology. 633
Biotinylated molecules are extensively employed in bioanalytics and biotechnology. The currently available assays for quantification of biotin groups suffer from low sensitivity, low accuracy, or provide highly variable responses for different biotin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d5bb0c02964163e6a28dcde3b4c9caee
https://pubmed.ncbi.nlm.nih.gov/32046840
https://pubmed.ncbi.nlm.nih.gov/32046840
Autor:
Felix Faschinger, Günther Knör, Maria Wiesauer, Vesa P. Hytönen, Hermann J. Gruber, Eva Schlögl, Elke Oberbichler, Jessica Stangl
Biotinylated molecules are extensively employed in bioanalytics and biotechnology. The currently available assays for quantification of biotin groups suffer from low sensitivity, low accuracy, or provide highly variable responses for different biotin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2079712ade430e854cb3cdb8d1f0f2ef
https://doi.org/10.1016/bs.mie.2019.10.028
https://doi.org/10.1016/bs.mie.2019.10.028
Autor:
Lukas Traxler, Felix Faschinger, Michael Stadlbauer, Hermann J. Gruber, Peter Hinterdorfer, Tatsiana Charnavets, Marc Fahrner, Christoph Romanin, Petr Rathner, Norbert Müller
Publikováno v:
Angewandte Chemie. 129:15962-15967
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2a7d00d7a1b76514b34436f9429733c
https://doi.org/10.1002/ange.201708667
https://doi.org/10.1002/ange.201708667
Autor:
Oliver Kudlacek, Peter Hinterdorfer, Harald H. Sitte, Walter Sandtner, Julia Gobl, Marion Holy, Amy Hauck Newman, Thomas Stockner, Rong Zhu, Michael Freissmuth, Hermann J. Gruber
Publikováno v:
Biophysical Journal. 118:618a-619a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::26a585298d9e8750f3c7fc57f18296f1
https://doi.org/10.1016/j.bpj.2019.11.3337
https://doi.org/10.1016/j.bpj.2019.11.3337
Publikováno v:
Methods in Molecular Biology ISBN: 9781493988938
Linking of sensor molecules (e.g., antibodies) to an AFM tip converts it into a biosensor by which single target molecules (e.g., antigens) can be detected and localized on the sample surface. Moreover, the mechanism of interaction can be studied by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0dfc9a32d202f6d03d68cebdd58201f5
https://doi.org/10.1007/978-1-4939-8894-5_7
https://doi.org/10.1007/978-1-4939-8894-5_7
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1814
The number of ligand binding sites in neurotransmitter-sodium symporters has been determined by crystal structure analysis and molecular pharmacology with controversial results. Here, we designed molecular tools to measure the interaction forces betw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d40ca11e0976c12bb1e4a7134fc2e53e
https://pubmed.ncbi.nlm.nih.gov/29956224
https://pubmed.ncbi.nlm.nih.gov/29956224
Autor:
Hermann J. Gruber, Peng Zhang, Michael Freissmuth, Thomas Stockner, Harald H. Sitte, Peter S. Hasenhuetl, Walter Sandtner, Oliver Kudlacek, Peter Hinterdorfer, Doris Sinwel, Kusumika Saha, Vivek Kumar, Marion Holy, Amy Hauck Newman, Christian Rankl, Rong Zhu, Sonja Sucic, Andreas Karner
Publikováno v:
Angewandte Chemie. 128:1751-1754
Controversy regarding the number and function of ligand binding sites in neurotransmitter/sodium symporters arose from conflicting data in crystal structures and molecular pharmacology. Here, we have designed novel tools for atomic force microscopy t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ff5c6bde5f93c7dbc96feb55e8547e0
https://doi.org/10.1002/ange.201508755
https://doi.org/10.1002/ange.201508755
Autor:
Lukas, Traxler, Petr, Rathner, Marc, Fahrner, Michael, Stadlbauer, Felix, Faschinger, Tatsiana, Charnavets, Norbert, Müller, Christoph, Romanin, Peter, Hinterdorfer, Hermann J, Gruber
Publikováno v:
Angewandte Chemie (International ed. in English). 56(49)
Calmodulin (CaM) binds most of its targets by wrapping around an amphipathic α-helix. The N-terminus of Orai proteins contains a conserved CaM-binding segment but the binding mechanism has been only partially characterized. Here, microscale thermoph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::746d824513db65132fbb592bbcb1a2ba
https://pubmed.ncbi.nlm.nih.gov/29024298
https://pubmed.ncbi.nlm.nih.gov/29024298