J
Jan P. Erzberger
Researcher at ETH Zurich
Publications - 27
Citations - 4283
Jan P. Erzberger is an academic researcher from ETH Zurich. The author has contributed to research in topics: DnaA & dnaB helicase. The author has an hindex of 22, co-authored 24 publications receiving 3948 citations. Previous affiliations of Jan P. Erzberger include Lawrence Livermore National Laboratory & Lawrence Berkeley National Laboratory.
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Journal ArticleDOI
Evolutionary relationships and structural mechanisms of AAA+ proteins.
Jan P. Erzberger,James M. Berger +1 more
TL;DR: The critical features of theAAA+ domain are described, current knowledge of how this versatile element is incorporated into larger assemblies is summarized, and specific adaptations of the AAA+ fold are discussed that allow complex molecular manipulations to be carried out for a highly diverse set of macromolecular targets.
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Formation of MacroH2A-Containing Senescence-Associated Heterochromatin Foci and Senescence Driven by ASF1a and HIRA
Rugang Zhang,Maxim Poustovoitov,Maxim Poustovoitov,Xiaofen Ye,Hidelita Santos,Wei Chen,Sally M. Daganzo,Sally M. Daganzo,Jan P. Erzberger,Ilya G. Serebriiskii,Adrian A. Canutescu,Roland L. Dunbrack,John R. Pehrson,James M. Berger,Paul D. Kaufman,Paul D. Kaufman,Peter D. Adams +16 more
TL;DR: Analysis of composition and mode of assembly of SAHF indicates that HIRA and ASF1a drive formation of macroH2A-containing SAHF and senescence-associated cell cycle exit, via a pathway that appears to depend on flux of heterochromatic proteins through PML bodies.
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The septin family of GTPases: architecture and dynamics.
TL;DR: The first detailed structural views of the septin core have emerged and these, along with studies of septin dynamics in vivo, have provided new insight into septin-complex assembly and septin function in vivo.
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Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
TL;DR: This model clarifies how DnaA engages and unwinds bacterial origins and suggests that additional, regulatory AAA+ proteins engage DnaB at filament ends, indicating that a spiral, open-ring AAA+ assembly forms the core element of initiators in all domains of life.
Journal ArticleDOI
Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export.
Christine S. Weirich,Jan P. Erzberger,Jeffrey S. Flick,Jeffrey S. Flick,James M. Berger,Jeremy Thorner,Karsten Weis +6 more
TL;DR: The results define specific functions for Gle1 and InsP6 in mRNA export and suggest that local activation of Dbp5 at the nuclear pore is critical for mRNA export.