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The main focus of my research is to understand the molecular mechanisms that control the cellular response to ER stress. ER stress causes unfolded proteins to accumulate in the ER and this activates a cellular signaling network called the Unfolded Protein Response (UPR). The UPR aims to reduce the load of unfolded proteins in the ER and restore ER homeostasis by a number of mechanisms, however, if the stress is too severe or prolonged the UPR can induce cell death. There are three ER transmembrane proteins, PERK, ATF6 and IRE1, involved in the initiation of downstream UPR signaling. ER stress and UPR have been implicated in the development of conditions such as neurodegenerative diseases, inflammatory disorders, diabetes and cancer. Currently my lab are studying (1) UPR signaling in tumorogenesis, tumor metastasis and therapy resistance; (2) UPR drug discovery, in particular drugs targeting IRE1 or PERK; (3) biomarker discovery as companion diagnostics and for stratification of patients based on UPR activation in tumors.
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Cellular and molecular life sciences : CMLSno. 12 (2023): 1-14
EMBO MOLECULAR MEDICINEno. 2 (2023)
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