JoJo Benn
@benn_jojo
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Postdoc with @w_mcewan at @ukdri Cambridge. Developing targeted protein degradation strategies against neurodegenerative protein aggregates.
Cambridge, England
Joined September 2018
Very happy to share our paper describing the selective degradation of aggregated tau protein via clustering activated RING-Nanobody (R-Nb) constructs. Intracellular R-Nb expression prevented tau aggregation and rapidly removed preformed aggregates. https://t.co/ufbwMB1kqA
science.org
Selective degradation of pathological protein aggregates while sparing monomeric forms is of major therapeutic interest. The E3 ligase tripartite motif–containing protein 21 (TRIM21) degrades...
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Check out episode 9 of The ParAqua Podcast featuring @jo_mauch from @LeibnizIGB We discuss his PhD research into the effects of climate change and changing lake ecology on the invasive Quagga Mussel https://t.co/NTo91Fvlfd
@ParAqua_CA20125
linktr.ee
View paraquapodcast’s Linktree to discover and stream music from top platforms like YouTube, Spotify here. Your next favorite track is just a click away!
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Our review is out now in @NeuroCellPress! We provide an updated overview of the links between autophagy, ageing, and age-related neurodegeneration. A collaboration between the Rubinsztein and @VIKorolchuk labs that was very enjoyable to work on 🤓 https://t.co/rygzwhhOfJ
cell.com
This review discusses the links between the autophagy pathway, aging, and age-associated neurodegeneration in Alzheimer’s, Parkinson’s, motor neuron, and Huntington’s diseases. The authors highlight...
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Episode 8 of the ParAqua podcast features Professor Claire Gachon from the Museum of Natural History in Paris. We discuss her research on parasitism and the impacts it can have on the emerging algal aquaculture industry https://t.co/NTo91Fvlfd
@ParAqua_CA20125 @AnaAgavrilster
linktr.ee
View paraquapodcast’s Linktree to discover and stream music from top platforms like YouTube, Spotify here. Your next favorite track is just a click away!
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Targeting intracellular tau tangles with the active domain of a ubiquitin ligase mopped them up rapidly in tauopathy mice. #alzheimersdisease @UKDRI, @MRC_LMB
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Exciting new research co-led by @w_mcewan harnesses the unique capabilities of the protein TRIM21 to selectively remove aggregated tau from the brains of mice The team say this approach could avoid any potential side-effects of eliminating normal tau👉 https://t.co/JDVYjtLTrE
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The UK DRI's @w_mcewan & @JamesLab9 (@MRC_LMB) have developed new therapies that selectively remove aggregated tau proteins - harnessing the unique capabilities of a protein called TRIM21. The treatment improved symptoms of neurodegeneration in mice👉 https://t.co/JDVYjtLTrE
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Researchers from @MRC_LMB in Cambridge, England and @UKDRI at @Cambridge_Uni have developed new potential therapies that selectively remove the aggregated tau tangles to treat #Alzheimersdisease. Learn more:
insideprecisionmedicine.com
The new therapies leverage a protein known as TRIM21, which has been re-engineered to selectively remove tau tangles.
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Super excited to share our latest paper on a novel targeted protein degradation technology, now out in @CellCellPress. We introduce RING-Bait technology, an innovative approach to selectively target and degrade intracellular protein aggregates (1/7)
cell.com
RING-Bait technology hijacks the process of templated aggregation to recruit ubiquitination machinery and selectively degrade pathogenic tau assemblies without generating a specific binder, thereby...
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It's been a long journey from TRIMinator to R-Nb, and wouldn't have been possible without the expertise of my co-first author Shi Cheng and the support of @w_mcewan and the many others involved in this project!
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We've focused on tau, but hope that the growing repertoire of nanobodies will allow for the creation of R-Nb's against the many other aggregating proteins implicated in neurodegenerative disease!
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The TRIM21 RING is activated by clustering, meaning R-Nb's should only induce degradation when target epitopes are densely packed. i.e. on protein aggregates! This allowed us to degrade aggregated tau whilst leaving monomer levels unaltered.
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R-Nb's are simple genetically encoded constructs consisting of a nanobody, to bind the tau aggregate, fused to the E3 ligase domain (RING) of TRIM21, to induce target degradation.
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