Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Petra Wollmann"'
Publikováno v:
Current Opinion in Structural Biology. 22:225-233
Swi2/Snf2 (switch / sucrose non-fermentable) enzymes form a large and diverse class of proteins and multiprotein assemblies that remodel nucleic acid:protein complexes, using the energy of ATP hydrolysis. The core Swi2/Snf2 type ATPase domain belongs
Autor:
David T. Auble, A. Butryn, Ramya Viswanathan, Karl-Peter Hopfner, Melissa N. Wells, Petra Wollmann, Gregor Witte, Roland Beckmann, Manuela Moldt, Sheng Cui, Petra Wendler, Otto Berninghausen
Publikováno v:
Nature. 475:403-407
The Swi2/Snf2 family of proteins uses the energy of ATP hydrolysis to disrupt protein-DNA interactions, a process known as remodelling. In this study, Karl-Peter Hopfner and colleagues have solved the structure of the Mot1 ATPase in complex with the
Autor:
Kornelius Zeth, Petra Wollmann
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:895-898
Sensing external stress in the bacterial periplasm and signal transduction to the cytoplasm are important functions of the CpxAR, Bae and sigma(E) signalling pathways. In Escherichia coli, the sigma(E) pathway can be activated through degradation of
Publikováno v:
Nucleic Acids Research. 27:2126-2134
Entry into the cell cycle in budding yeast involves transcriptional activation of G1cyclin genes and DNA synthesis genes when cells reach a critical size in late G1. Expression of G1cyclins CLN1 and CLN2 is regulated by the transcription factor SBF (
Autor:
Kornelius Zeth, Petra Wollmann
Publikováno v:
Journal of molecular biology. 372(4)
An elegant network of signal transduction has evolved in the bacterial cell envelope to respond to environmental stress. It is initiated by sensing unfavourable and harmful changes in the periplasm. The stress signal is then transmitted by a controll
Publikováno v:
International journal of biological macromolecules. 39(1-3)
Non-fimbrial adhesins, such as Yersinia YadA, Moraxella UspA1 and A2, Haemophilus Hia and Hsf, or Bartonella BadA, represent an important class of molecules by which pathogenic proteobacteria adhere to their hosts. They form trimeric surface structur