FEBS Press Awards
The FEBS Letters Award 2020
FEBS Letters is pleased to announce that the FEBS Letters Award 2020 will be presented to Dr Tim Bartels (UK Dementia Research Institute at UCL) for his outstanding paper:
Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces
Matteo Rovere, John B. Sanderson, Luis Fonseca-Ornelas, Dushyant S. Patel and Tim Bartels. FEBS Lett, 2018, 592: 1464–1472. doi:10.1002/1873-3468.13047
α-Synuclein is a neuronal protein of unknown physiological function. Pathological aggregates of a-synuclein are a hallmark of Dementia with Lewy Bodies (DLB), Parkinson’s disease (PD) and Multiple System Atrophy.
The lab of Tim Bartels found that a soluble form of α-synuclein exists as an α-helically folded tetramer. This soluble form of α-synuclein is not prone to aggregation and its folding is favored by interaction with lipid bilayers, which appear to act as molecular chaperones modulating the conformational space of the folding protein. The authors propose a scenario whereby α-synuclein is present in two conformational pools: one of them aggregation‐prone, soluble and unfolded, and the other α‐helical and aggregation‐resistant. Imbalances in the relative amounts of protein in these two pools could favor nucleation events and subsequent aggregation.
The award-winning article is selected by a special committee, formed by appointed members of the Editorial Board, plus one external member. The Award Committee members were: Laszlo Nagy (Orlando), Britta Brügger (Heidelberg), Nicola Gray (Edinburgh), Daniela Ruffell (Editorial Office) and Michael Brunner (Associate Managing Editor), Chair.
Dr Bartels will present a plenary lecture about this work at the 45th FEBS Congress in Ljubljana, Slovenia, 3–8 July 2021, where he will be officially presented with the prize.
The FEBS Journal Richard Perham Prize 2020
The prize was awarded for the below outstanding paper published by Kazunori Mori and co-authors in The FEBS Journal in 2019. The senior author, Dr Motoko Shibanuma (Showa University School of Pharmacy, Tokyo, Japan), will present a plenary lecture about this work at the 45th FEBS Congress in Ljubljana, Slovenia in July 2021.
A mitochondrial ROS pathway controls matrix metalloproteinase 9 levels and invasive properties in RAS‐activated cancer cells
Kazunori Mori, Tetsu Uchida, Toshihiko Yoshie, Yuko Mizote. Fumihiro Ishikawa, Masato Katsuyama and Motoko Shibanuma
FEBS J, 2019, 286: 459–478. doi:10.1111/febs.14671
Matrix metalloproteinases (MMPs) are a group of tissue‐remodeling enzymes that have been linked to a variety of pathophysiological processes, including cancer metastasis. In this study, the authors provided new insights into the regulation of MMP9. They showed that the molecular adaptor protein HIC‐5 suppresses the activation of NADPH oxidase 4 (NOX4), leading to downregulation of mitochondrial ROS levels, which in turn destabilizes MMP9 mRNA. They further demonstrated that this regulatory axis operates specifically in cancer cells harboring oncogenic mutations in H‐ or K‐ras, potentially unveiling a new therapeutic avenue for cancer therapy based on inhibition of MMPs.
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