{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Martin-Fernandez ML"],"funding":["Science and Technology Facilities Council","Medical Research Council","Biotechnology and Biological Sciences Research Council"],"pagination":["73-91"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10952613"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["291(1)"],"pubmed_abstract":["The epidermal growth factor receptor (EGFR) is a poster child for the understanding of receptor behaviour, and of paramount importance to cell function and human health. Cloned almost forty years ago, the interest in EGFR's structure/function relationships remains unabated, not least because changes in oncogenic EGFR mutants are key drivers of the formation of lung and brain tumours. The structure of the assemblies formed by EGFR have been comprehensibly investigated by techniques such as high-resolution X-ray crystallography, NMR and all-atom molecular dynamics (MD) simulations. However, the complexity embedded in the portfolio of EGFR states that are only possible in the physiological environment of cells has often proved refractory to cell-free structural methods. Conversely, some key i"],"journal":["Journal of microscopy"],"pubmed_title":["A perspective of fluorescence microscopy for cellular structural biology with EGFR as witness."],"pmcid":["PMC10952613"],"funding_grant_id":["BB/S019553/1","BB/G006911/1","MR/K015591/1","ST/S000682/1","BB/E000215/1","BB/C51464X/1","BB/L014327/1"],"pubmed_authors":["Martin-Fernandez ML"],"additional_accession":[]},"is_claimable":false,"name":"A perspective of fluorescence microscopy for cellular structural biology with EGFR as witness.","description":"The epidermal growth factor receptor (EGFR) is a poster child for the understanding of receptor behaviour, and of paramount importance to cell function and human health. Cloned almost forty years ago, the interest in EGFR's structure/function relationships remains unabated, not least because changes in oncogenic EGFR mutants are key drivers of the formation of lung and brain tumours. The structure of the assemblies formed by EGFR have been comprehensibly investigated by techniques such as high-resolution X-ray crystallography, NMR and all-atom molecular dynamics (MD) simulations. However, the complexity embedded in the portfolio of EGFR states that are only possible in the physiological environment of cells has often proved refractory to cell-free structural methods. Conversely, some key i","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jul","modification":"2025-04-05T07:20:54.705Z","creation":"2024-11-19T23:31:13.901Z"},"accession":"S-EPMC10952613","cross_references":{"pubmed":["36282005"],"doi":["10.1111/jmi.13151"]}}