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Benjamin Stieglitz

Researcher at Queen Mary University of London

Publications -  18
Citations -  1826

Benjamin Stieglitz is an academic researcher from Queen Mary University of London. The author has contributed to research in topics: Ubiquitin ligase & Ubiquitin. The author has an hindex of 11, co-authored 16 publications receiving 1588 citations. Previous affiliations of Benjamin Stieglitz include Francis Crick Institute & Medical Research Council.

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SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis.

TL;DR: It is reported that SHARPIN functions as a novel component of the linear ubiquitin chain assembly complex (LUBAC) and that the absence of SHARPin causes dysregulation of NF-κB and apoptotic signalling pathways, explaining the severe phenotypes displayed by chronic proliferative dermatitis (cpdm) in SHARPIn-deficient mice.
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An IL-9 fate reporter demonstrates the induction of an innate IL-9 response in lung inflammation

TL;DR: It was found that during papain-induced lung inflammation, IL-9 production was largely restricted to innate lymphoid cells (ILCs) and was rapidly lost in favor of other cytokines, such as IL-13 and IL-5, which suggested that ILCs provide the missing link between the well-established functions of IL-8 and type 2 helper T cell cytokines and responses.
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LUBAC synthesizes linear ubiquitin chains via a thioester intermediate

TL;DR: It is shown that the RING‐in‐between‐RING (RBR)‐containing region of HOIP—the catalytic subunit of LUBAC—is sufficient to generate linear ubiquitin chains, supporting the notion that RBR ligases act as RING/HECT hybrids.
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Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP

TL;DR: The crystal structure of the catalytic core of HOIP, which belongs to the RBR (RING-between-RING) family of E3 ligases, is reported, providing a unique snapshot of the ubiquitin transfer complex containing both donor and acceptor ubiquitIn.
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Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II

TL;DR: The crystal structure of Ras in complex with the Ras binding domain (RBD) of NORE1A/RAPL is described and it is demonstrated that the enlarged interface provides a rationale for an exceptionally long lifetime of the complex.