Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Dirk Windisch"'
Autor:
Marcel Zeitler, Peter L. Gor’kov, Jochen Bürck, Stephan L. Grage, Dirk Windisch, Anne S. Ulrich, Colin Ziegler
Publikováno v:
Biophysical Journal. 109(4):737-749
The oncogenic E5 protein from bovine papillomavirus is a short (44 amino acids long) integral membrane protein that forms homodimers. It activates platelet-derived growth factor receptor (PDGFR) β in a ligand-independent manner by transmembrane heli
Publikováno v:
Journal of Synchrotron Radiation
UV-CD12 at ANKA and its current end-station are described, with a standard module for vacuum-UV synchrotron radiation circular dichroism of bio-macromolecules in the liquid state, and a unique module for macroscopically oriented lipid membranes (orie
Publikováno v:
Biological Chemistry. 395:1443-1452
E5 is the major transforming oncoprotein of bovine papillomavirus, which activates the platelet-derived growth factor receptor β in a highly specific manner. The short transmembrane protein E5 with only 44 residues interacts directly with the transm
Autor:
Wolfgang Grosse, Barbara Mertins, Ulrich Koert, Lars-Oliver Essen, Dirk Windisch, Anne S. Ulrich, Georgios Psakis, Jochen Bürck, Felix Brademann, Philipp Reiss
Publikováno v:
Biochemistry. 53:4826-4838
Porins, like outer membrane protein G (OmpG) of Escherichia coli, are ideal templates among ion channels for protein and chemical engineering because of their robustness and simple architecture. OmpG shows fast transitions between open and closed sta
Autor:
Katharina Becker, Anne S. Ulrich, Torsten H. Walther, Ariadna Grau Campistany, Stephan L. Grage, Sergiy Afonin, Jochen Bürck, Erik Strandberg, Benjamin Zimpfer, Lena M. E. Steger, Dirk Windisch, Parvesh Wadhwani, Johannes Reichert
Publikováno v:
Biophysical Journal. 114:34a
Autor:
Marcel Zeitler, Sergii Afonin, Claudia Muhle-Goll, Silke Hoffmann, Dirk Windisch, Anton A. Polyansky, Anne S. Ulrich, Jochen Bürck, Stephan L. Grage
The platelet-derived growth factor receptor β is a member of the cell surface receptor tyrosine kinase family and dimerizes upon activation. We determined the structure of the transmembrane segment in dodecylphosphocholine micelles by liquid-state N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::685c072f6a58ca29c4512f4f358b4e69
https://europepmc.org/articles/PMC3406703/
https://europepmc.org/articles/PMC3406703/
Autor:
Soraya Benamira, Sergii Afonin, Silke Hoffmann, Birgid Langer, Dirk Windisch, Claudia Muhle-Goll, Jochen Bürck, Stefanie Vollmer, Anne S. Ulrich
Publikováno v:
Biophysical journal. 99(6)
The E5 oncoprotein is the major transforming protein of bovine papillomavirus type 1. This 44-residue transmembrane protein can interact with the platelet-derived growth factor receptor β, leading to ligand-independent activation and cell transforma