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Evgenij Fiskin
Researcher at Goethe University Frankfurt
Publications - 9
Citations - 492
Evgenij Fiskin is an academic researcher from Goethe University Frankfurt. The author has contributed to research in topics: Ubiquitin ligase & Effector. The author has an hindex of 7, co-authored 9 publications receiving 403 citations.
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Journal ArticleDOI
Fluorescence-Based Sensors to Monitor Localization and Functions of Linear and K63-Linked Ubiquitin Chains in Cells
Sjoerd J L van Wijk,Evgenij Fiskin,Mateusz Putyrski,Francesco Pampaloni,Jian Hou,Philipp Wild,Tobias Kensche,Hernán E. Grecco,Philippe I. H. Bastiaens,Ivan Dikic +9 more
TL;DR: It is proposed that UBD-based biosensors could serve as prototypes to track and trace other chain types and ubiquitin-like signals in vivo.
Journal ArticleDOI
Bacteria-host relationship: ubiquitin ligases as weapons of invasion
TL;DR: The roles played by different classes of bacterial Ub ligases in infection and pathogenicity are described and an overview of the different mechanisms by which bacteria mimic specific components of the host Ub system is provided.
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Global Analysis of Host and Bacterial Ubiquitinome in Response to Salmonella Typhimurium Infection
TL;DR: Dynamic changes in the global ubiquitinome of host epithelial cells and invading pathogen in response to Salmonella Typhimurium infection are reported and it is revealed that bacterial Ub-modifying enzymes modulate a unique subset of host targets, affecting different stages ofSalmonella infection.
Journal ArticleDOI
Structural basis for phosphorylation-triggered autophagic clearance of Salmonella.
Vladimir V. Rogov,Hironori Suzuki,Evgenij Fiskin,Philipp Wild,Andreas Kniss,Alexis Rozenknop,Ryuichi Kato,Masato Kawasaki,David G. McEwan,Frank Löhr,Peter Güntert,Ivan Dikic,Soichi Wakatsuki,Volker Dötsch +13 more
TL;DR: The NMR and crystal structures of the autophagy modifier LC3B in complex with the LC3 interaction region of optineurin either phosphorylated or bearing phospho-mimicking mutations show that the negative charge induced by phosphorylation is recognized by the side chains of Arg¹¹ and Lys⁵¹ inLC3B.
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Structural basis for the recognition and degradation of host TRIM proteins by Salmonella effector SopA.
TL;DR: It is demonstrated that SopA ubiquitinates TRIM56 and TRIM65, resulting in their proteasomal degradation during infection, and provides the basis for how a bacterial HECT ligase blocks host RING ligases and exemplifies the multivalent power of bacterial effectors during infection.