Beate Voss
Max Planck Society
5 Papers
10 Citations
Beate Voss is an academic researcher from Max Planck Society. The author has contributed to research in topics: Chemical biology & Electroporation. The author has an hindex of 3, co-authored 5 publications.
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Papers
The pseudo GTPase CENP-M drives human kinetochore assembly
Federica Basilico,Stefano Maffini,John R. Weir,Daniel Prumbaum,Ana M. Rojas,Tomasz Zimniak,Anna De Antoni,Sadasivam Jeganathan,Beate Voss,Suzan van Gerwen,Veronica Krenn,Lucia Massimiliano,Alfonso Valencia,Ingrid R. Vetter,Franz Herzog,Stefan Raunser,Sebastiano Pasqualato,Andrea Musacchio +17 more
TL;DR: It is reported that a protein at the kinetochore–centromere interface, CENP-M, is structurally and evolutionarily related to small GTPases but is incapable of GTP-binding and conformational switching.
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Electroporated recombinant proteins as tools for in vivo functional complementation, imaging and chemical biology
Amal Alex,Valentina Piano,Soumitra Polley,Marchel Stuiver,Stephanie Voss,Giuseppe Ciossani,Katharina Overlack,Beate Voss,Sabine Wohlgemuth,Arsen Petrovic,Yao-Wen Wu,Yao-Wen Wu,Philipp Selenko,Philipp Selenko,Andrea Musacchio,Andrea Musacchio,Stefano Maffini +16 more
TL;DR: The data show that electroporation is well-suited to deliver synthetic and chemically modified versions of functional proteins, and, therefore, constitutes a promising tool for applications in chemical and synthetic biology.
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Electroporated recombinant proteins as tools for in vivo functional complementation, imaging, and chemical biology
Amal Alex,Valentina Piano,Soumitra Polley,Marchel Stuiver,Marchel Stuiver,Stephanie Voss,Giuseppe Ciossani,Katharina Overlack,Beate Voss,Sabine Wohlgemuth,Arsen Petrovic,Arsen Petrovic,Yao-Wen Wu,Yao-Wen Wu,Philipp Selenko,Philipp Selenko,Andrea Musacchio,Andrea Musacchio,Stefano Maffini +18 more
TL;DR: B batch electroporation is surveyed as a delivery tool for single polypeptides and multi-subunit protein assemblies of kinetochores, a spatially confined and well-studied subcellular structures and is therefore a promising tool for chemical and synthetic biology.
10
Nucleotide binding and filament assembly of recombinant yeast septin complexes
TL;DR: It is shown here that the nucleotide-binding sites of the septins show drastic changes on formation of higher oligomers, and the binary core Cdc3p-Cdc12p complex does not form filaments, but the ternary and quaternary complexes form bundles of paired filaments.
Author response: The pseudo GTPase CENP-M drives human kinetochore assembly
Federica Basilico,Federica Basilico,Stefano Maffini,John R. Weir,Daniel Prumbaum,Ana M. Rojas,Tomasz Zimniak,Anna De Antoni,Sadasivam Jeganathan,Beate Voss,Suzan van Gerwen,Veronica Krenn,Veronica Krenn,Lucia Massimiliano,Alfonso Valencia,Ingrid R. Vetter,Franz Herzog,Stefan Raunser,Sebastiano Pasqualato,Andrea Musacchio,Andrea Musacchio +20 more