Search Results - (Author, Cooperation:H. Stahlberg)
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1G. Hassaine ; C. Deluz ; L. Grasso ; R. Wyss ; M. B. Tol ; R. Hovius ; A. Graff ; H. Stahlberg ; T. Tomizaki ; A. Desmyter ; C. Moreau ; X. D. Li ; F. Poitevin ; H. Vogel ; H. Nury
Nature Publishing Group (NPG)
Published 2014Staff ViewPublication Date: 2014-08-15Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Amino Acid Sequence ; Animals ; Binding Sites ; Crystallography, X-Ray ; Mice ; Models, Molecular ; Molecular Sequence Data ; Neurotransmitter Agents/metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Receptors, Serotonin, 5-HT3/*chemistry/metabolismPublished by: -
2S. Cavadini ; E. S. Fischer ; R. D. Bunker ; A. Potenza ; G. M. Lingaraju ; K. N. Goldie ; W. I. Mohamed ; M. Faty ; G. Petzold ; R. E. Beckwith ; R. B. Tichkule ; U. Hassiepen ; W. Abdulrahman ; R. S. Pantelic ; S. Matsumoto ; K. Sugasawa ; H. Stahlberg ; N. H. Thoma
Nature Publishing Group (NPG)
Published 2016Staff ViewPublication Date: 2016-04-01Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Allosteric Regulation ; Apoproteins/chemistry/metabolism/ultrastructure ; Binding Sites ; *Biocatalysis ; Carrier Proteins/chemistry/metabolism/ultrastructure ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Cullin Proteins/chemistry/metabolism/ultrastructure ; DNA Damage ; DNA-Binding Proteins/chemistry/metabolism/ultrastructure ; Humans ; Kinetics ; Models, Molecular ; Multiprotein Complexes/chemistry/*metabolism/*ultrastructure ; Peptide Hydrolases/chemistry/*metabolism/*ultrastructure ; Protein Binding ; Ubiquitination ; Ubiquitins/metabolismPublished by: -
3N. M. Taylor ; N. S. Prokhorov ; R. C. Guerrero-Ferreira ; M. M. Shneider ; C. Browning ; K. N. Goldie ; H. Stahlberg ; P. G. Leiman
Nature Publishing Group (NPG)
Published 2016Staff ViewPublication Date: 2016-05-20Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsPublished by: -
4J. Liu ; L. Renault ; X. Veaute ; F. Fabre ; H. Stahlberg ; W. D. Heyer
Nature Publishing Group (NPG)
Published 2011Staff ViewPublication Date: 2011-10-25Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Adenosine Triphosphatases/genetics/*metabolism ; DNA Helicases/antagonists & inhibitors/*metabolism ; DNA Repair Enzymes/genetics/*metabolism ; DNA, Single-Stranded/chemistry/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Protein Binding ; Rad51 Recombinase/chemistry/*metabolism ; Saccharomyces cerevisiae/enzymology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/antagonists & ; inhibitors/chemistry/genetics/*metabolismPublished by: -
5Stahlberg, H. ; Kutejová, E. ; Muchová, K. ; Gregorini, M. ; Lustig, A. ; Müller, S. A. ; Olivieri, V. ; Engel, A. ; Wilkinson, A. J. ; Barák, I.
Oxford, UK : Blackwell Science Ltd
Published 2004Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: DivIVA from Bacillus subtilis is a bifunctional protein with distinct roles in cell division and sporulation. During vegetative growth, DivIVA regulates the activity of the MinCD complex, thus helping to direct cell division to the correct mid-cell position. DivIVA fulfils a quite different role during sporulation in B. subtilis when it directs the oriC region of the chromosome to the cell pole before asymmetric cell division. DivIVA is a 19.5 kDa protein with a large part of its structure predicted to form a tropomyosin-like α-helical coiled-coil. Here, we present a model for the quaternary structure of DivIVA, based on cryonegative stain transmission electron microscopy images. The purified protein appears as an elongated particle with lateral expansions at both ends producing a form that resembles a ‘doggy-bone’. The particle mass estimated from these images agrees with the value of 145 kDa measured by analytical ultracentrifugation suggesting 6- to 8-mers. These DivIVA oligomers serve as building blocks in the formation of higher order assemblies giving rise to strings, wires and, finally, two-dimensional lattices in a time-dependent manner.Type of Medium: Electronic ResourceURL: