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Norbert Sträter

Showing results (11-20 of 110) with videos related to

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Biochemistry|February 16, 2005
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidaseRobert Schultz-Heienbrok, Timm Maier, Norbert Sträter
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|November 30, 2012
Crystallization and preliminary X-ray analysis of the open form of human ecto-5'-nucleotidase (CD73)Karen Maree Knapp, Matthias Zebisch, Norbert Sträter
Protein Science : a Publication of the Protein Society|June 25, 2004
Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridgesRobert Schultz-Heienbrok, Timm Maier, Norbert Sträter
The Journal of Biological Chemistry|December 2, 2011
Structural insight into activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reductionUlrike Krug, Matthias Zebisch, Michel Krauss, et al.
Journal of Molecular Biology|November 22, 2011
Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1Matthias Zebisch, Michel Krauss, Petra Schäfer, et al.
Acta Crystallographica. Section D, Biological Crystallography|April 5, 2014
Structures of Legionella pneumophila NTPDase1 in complex with polyoxometallatesMatthias Zebisch, Michel Krauss, Petra Schäfer, et al.
Proteins|April 11, 2012
Crystal structure of a supercharged variant of the human enteropeptidase light chainPeter Simeonov, Michael Zahn, Norbert Sträter, et al.
Environment International|February 25, 2023
Structural basis of the activation of PPARγ by the plasticizer metabolites MEHP and MINCHAbibe Useini, Felipe Engelberger, Georg Künze, et al.
BMC Biotechnology|December 30, 2014
Protein surface charge of trypsinogen changes its activation patternKarin Buettner, Thomas Kreisig, Norbert Sträter, et al.
Chembiochem : a European Journal of Chemical Biology|October 12, 2013
The ATP/ADP substrate specificity switch between Toxoplasma gondii NTPDase1 and NTPDase3 is caused by an altered mode of binding of the substrate baseUlrike Krug, Robert Totzauer, Matthias Zebisch, et al.
Pageof 11

Showing results (11-20 of 110) with videos related to

Sort By:
Pageof 11
Biochemistry|February 16, 2005
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidaseRobert Schultz-Heienbrok, Timm Maier, Norbert Sträter
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|November 30, 2012
Crystallization and preliminary X-ray analysis of the open form of human ecto-5'-nucleotidase (CD73)Karen Maree Knapp, Matthias Zebisch, Norbert Sträter
Protein Science : a Publication of the Protein Society|June 25, 2004
Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridgesRobert Schultz-Heienbrok, Timm Maier, Norbert Sträter
The Journal of Biological Chemistry|December 2, 2011
Structural insight into activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reductionUlrike Krug, Matthias Zebisch, Michel Krauss, et al.
Journal of Molecular Biology|November 22, 2011
Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1Matthias Zebisch, Michel Krauss, Petra Schäfer, et al.
Acta Crystallographica. Section D, Biological Crystallography|April 5, 2014
Structures of Legionella pneumophila NTPDase1 in complex with polyoxometallatesMatthias Zebisch, Michel Krauss, Petra Schäfer, et al.
Proteins|April 11, 2012
Crystal structure of a supercharged variant of the human enteropeptidase light chainPeter Simeonov, Michael Zahn, Norbert Sträter, et al.
Environment International|February 25, 2023
Structural basis of the activation of PPARγ by the plasticizer metabolites MEHP and MINCHAbibe Useini, Felipe Engelberger, Georg Künze, et al.
BMC Biotechnology|December 30, 2014
Protein surface charge of trypsinogen changes its activation patternKarin Buettner, Thomas Kreisig, Norbert Sträter, et al.
Chembiochem : a European Journal of Chemical Biology|October 12, 2013
The ATP/ADP substrate specificity switch between Toxoplasma gondii NTPDase1 and NTPDase3 is caused by an altered mode of binding of the substrate baseUlrike Krug, Robert Totzauer, Matthias Zebisch, et al.
Pageof 11