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D M Vigushin

Researcher at Hammersmith Hospital

Publications -  13
Citations -  1673

D M Vigushin is an academic researcher from Hammersmith Hospital. The author has contributed to research in topics: Amyloidosis & Amyloid. The author has an hindex of 9, co-authored 13 publications receiving 1593 citations.

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Metabolic and scintigraphic studies of radioiodinated human C-reactive protein in health and disease.

TL;DR: The synthesis rate of CRP is the only significant determinant of its plasma level, confirming the validity of serum CRP measurement as an objective index of disease activity in disorders associated with an acute-phase response.
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Human lysozyme gene mutations cause hereditary systemic amyloidosis

TL;DR: It is reported that in two unrelated English families under the authors' care, lysozyme is the amyloid fibril protein in these two families, the first report of naturally occurring variants of human ly sozyme and of lyso enzyme-associated disease.
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Scintigraphic quantification and serial monitoring of human visceral amyloid deposits provide evidence for turnover and regression

TL;DR: A simple reproducible method for quantifying the uptake of 123l-labelled serum amyloid P component into individual livers, spleens and kidneys was devised and evaluated in 22 patients with different types of systemic Amyloidosis as discussed by the authors.
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Histone deacetylase inhibitor, Trichostatin A induces ubiquitin-dependent cyclin D1 degradation in MCF-7 breast cancer cells

TL;DR: It is demonstrated that rapid TSA-induced cyclin D1 degradation in MCF-7 cells requires GSK3β-mediated Thr-286 phosphorylation and the ubiquitin-dependent 26S proteasome pathway, and the findings suggest that HDAC inhibitors may have therapeutic potential as small-molecule cycl in D1 ablative agents.
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A new apolipoprotein Al variant, Trp50Arg, causes hereditary amyloidosis

TL;DR: A man with hereditary non-neuropathic systemic amyloidosis hadAmyloid fibril protein subunits consisting of N-terminal fragments of a previously unknown variant of apolipoprotein Al, Trp50Arg, encoded by a thymine-cytosine transition, which should facilitate analysis of the molecular basis of fibrillogenesis and of factors that modulate amyloids deposition and its consequences in vivo.