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Michael P. Schlunegger

Observed names: M SCHLUNEGGER, M. P. Schlunegger, M. Schlunegger, M.P. Schlunegger
OpenAlex ID: A5068436282
3D domain swapping: A mechanism for oligomer assembly
1995 · Melanie J. Bennett, Michael P. Schlunegger, et al. · Protein Science · 765
An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth fact or-β2
1992 · Michael P. Schlunegger, Markus G. Grütter · Nature · 332
Oligomer Formation By 3D Domain Swapping: A Model For Protein Assembly And Misassembly
1997 · M SCHLUNEGGER, M BENNETT, et al. · Advances in protein chemistry · 287
The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-Å resolution
1998 · Yanshun Liu, P. John Hart, et al. · Proceedings of the National Academy of Sciences · 186
Refined Crystal Structure of Human Transforming Growth Factor β2 at 1·5 Å Resolution
1993 · M.P. Schlunegger, M.G. Grütter · Journal of Molecular Biology · 63
Comparison of two crystal structures of TGF-β2: the accuracy of refined protein structures
1994 · S. Daopin, D. R. Davies, et al. · Acta Crystallographica Section D Biological Crystallography · 29
Crystallization and preliminary X‐ray analysis of recombinant human transforming growth factor β2
1992 · Michael P. Schlunegger, Nico Cerletti, et al. · FEBS Letters · 19
Crystallization and preliminary X-ray analysis of the β-isoform of glutamate decarboxylase from Escherichia coli
1998 · V. N. Malashkevich, D. De Biase, et al. · Acta Crystallographica Section D Biological Crystallography · 5
Crystallization and Preliminary Crystallographic Investigations of the Soluble Glucose Dehydrogenase from Acinetobacter calcoaceticus
1993 · M.P. Schlunegger, M.G. Grütter, et al. · Journal of Molecular Biology · 4
A Structure-Based Model of Diphtheria Toxin Action
1996 · David Eisenberg, Charles E. Bell, et al. · Molecular biology intelligence unit · 2
Crystal Structure of a 3d Domain-swapped Dimer of Bovine Pancreatic Ribonuclease a
1998 · Y. Liu, P.J. Hart, et al. · Worldwide Protein Data Bank
Works count: 12
Citation count: 1,693
H-index: 7
I10-index: 7
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