Search Results - "Kretschmar, Michael"

Efficient Intracellular Delivery of a Protein and a Low Molecular Weight Substance via Recombinant Polyomavirus-like Particles by Abbing, Andrea, Blaschke, Ulrich K., Grein, Swen, Kretschmar, Michael, Stark, Christoph M.B., Thies, Michael J.W., Walter, Jürgen, Weigand, Martina, Woith, Diemuth C., Hess, Jürgen, Reiser, Christian O.A.

“…Efficient encapsulation of foreign molecules like proteins and low molecular weight drugs into polyoma virus-like particles (capsoids) was achieved by the…”
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Crystal Structure of the Calcium-Loaded Spherulin 3a Dimer Sheds Light on the Evolution Of the Eye Lens βγ-Crystallin Domain Fold by Clout, Naomi J., Kretschmar, Michael, Jaenicke, Rainer, Slingsby, Christine

“…Background: The βγ-crystallins belong to a superfamily of two-domain proteins found in vertebrate eye lenses, with distant relatives occurring in…”
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Effective virus inactivation and removal by steps of Biotest Pharmaceuticals IGIV production process by Dichtelmüller, Herbert O., Flechsig, Eckhard, Sananes, Frank, Kretschmar, Michael, Dougherty, Christopher J.

“…The virus validation of three steps of Biotest Pharmaceuticals IGIV production process is described here. The steps validated are precipitation and removal of…”
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Stability of a homo-dimeric Ca2+-binding member of the βγ-crystallin superfamily: DSC measurements on spherulin 3a from Physarum polycephalum by Kretschmar, Michael, Jaenicke, Rainer

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Kinetic and Thermodynamic Stabilization of the βγ-Crystallin Homolog Spherulin 3a from Physarum polycephalum by Calcium Binding by Kretschmar, Michael, Mayr, Eva-Maria, Jaenicke, Rainer

“…Globular proteins may be stabilized, either intrinsically, at the various levels of the structural hierarchy, or extrinsically, by ligand binding. In the case…”
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Stability of a homo-dimeric Ca 2+-binding member of the βγ-crystallin superfamily: DSC measurements on spherulin 3a from Physarum polycephalum by Kretschmar, Michael, Jaenicke, Rainer

“…Spherulin 3a (S3a) from Physarum polycephalum represents the only known single-domain member of the superfamily of βγ eye-lens crystallins. It shares the…”
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Gamma S-crystallin of bovine and human eye lens: solution structure, stability and folding of the intact two-domain protein and its separate domains by Wenk, Martina, Herbst, Ruth, Hoeger, Dagmar, Kretschmar, Michael, Lubsen, Nicolette H., Jaenicke, Rainer

“…Human and bovine γS-crystallin (HγS and BγS) and their isolated N- and C-terminal domains were cloned and expressed as recombinant proteins in E. coli. HγS and…”
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