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After his seminal 1972 discovery of the role of complement in the induction of antibody production and related work, Pepys has mostly worked on amyloid and acute phase proteins. He has illuminated the pathogenesis and natural history of systemic amyloidosis, transforming diagnosis of this fatal disease, and improving management and survival. He has also elucidated the structural properties, function and clinical significance of serum amyloid P component (SAP) and C-reactive protein (CRP). He first identified these proteins as therapeutic targets, and has designed and is developing new drugs aimed at them.
His invention of in vivo scintigraphy with radiolabelled SAP enabled systemic amyloidosis for the first time to be safely, non-invasively diagnosed and quantitatively monitored. This revolutionised understanding of the natural history of amyloidosis and its response to therapy, and has guided radical therapeutic developments, focusing attention on the crucial importance of reducing the abundance of amyloid fibril precursor proteins. Pepys has discovered many of the mutations responsible for hereditary amyloidosis, including the first human lysozyme mutation, leading to demonstration that amyloidogenic lysozyme variants are less stable than wild type lysozyme and construction of a widely accepted general model of amyloid fibrillogenesis.
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Open Biologyno. 12 (2023): 230253-230253
medRxiv : the preprint server for health sciences (2023)
JOURNAL OF INTERNAL MEDICINEno. 6 (2021): 933-935
Oxford University Press eBookspp.C12.12.3-2234, (2020)
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Oxford Textbook of Medicinepp.2199-2207, (2020)
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