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Locating Large, Flexible Ligands on Proteins

Autor: Ludwig Ohl, Jean-Noël Grad, Carsten Schmuck, Christoph Wilms, Christian Ottmann, Daniel Hoffmann, Jan Nikolaj Dybowski, Alba Gigante

Publikováno v: Journal of Chemical Information and Modeling, 58(2), 315-327. American Chemical Society

Many biologically important ligands of proteins are large, flexible, and in many cases charged molecules that bind to extended regions on the protein surface. It is infeasible or expensive to locate such ligands on proteins with standard methods such

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::698c047f2706bb7a5f9316b901eeae27
https://doi.org/10.1021/acs.jcim.7b00413

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Rational design, binding studies and crystal structure evaluation of the first ligand targeting the dimerization Interface of the 14-3-3ζ adapter protein

Autor: Carsten Schmuck, Marcel Mertel, Daniel Hoffmann, David Bier, Martin Ehlers, Elsa Sanchez-Garcia, Christian Ottmann, Ludwig Ohl, Sumit Mittal, Maria Bartel, Marius Heimann, Jean-Noël Grad, Jeroen Briels

Publikováno v: ChemBioChem, 19(6), 591-595. Wiley-VCH Verlag

14-3-3 Proteins play a central role in signalling pathways in cells: they interact as gatekeeper proteins with a huge number of binding partners. Their function as hub for intracellular communication can explain why these adapter proteins are associa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28097f11b52786a72db04f4474ff5984
https://research.tue.nl/nl/publications/aec4505e-5496-44f7-a580-7c843a3b951d

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Using dynamic model averaging in state space representation with dynamic Occam's window and applications to the stock and gold market

Autor: Ludwig Ohl, Marian Risse

We combine the Onorante and Raftery (2016) dynamic Occam’s window approach with the Raftery et al. (2010) DMA estimator in state space representation to create forecasts using a data-rich forecasting environment. Our approach is mainly related to e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d82285320a2552acb847e42ca80baef6
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=85032035181

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