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Proteomics in protein misfolding diseases.

Stoppini, M; Obici, L; Lavatelli, F; Giorgetti, S; Marchese, L; Moratti, R; Bellotti, V; (2009) Proteomics in protein misfolding diseases. Clin Chem Lab Med , 47 (6) pp. 627-635. 10.1515/CCLM.2009.164.

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Abstract

Protein misfolding and deposition as amyloid, with consequent tissue damage, plays a key role in the group of diseases generically termed amyloidoses. In the systemic forms, amyloid deposition is widespread and causes severe dysfunction of vital organs. Proteomic analysis, thanks to its versatility and the comprehensiveness of information obtained, is an ideal tool for the study of systemic amyloidoses. It has been successfully employed in the characterization of the circulating amyloidogenic precursors and the analysis of affected tissues, for the diagnostic identification of the fibril components and for characterizing disease-related changes in protein expression. We present the developments in the field of proteomics applied to systemic amyloidoses, and discuss the perspectives opened in the study of these diseases.

Type: Article
Title: Proteomics in protein misfolding diseases.
Location: Germany
DOI: 10.1515/CCLM.2009.164
Keywords: Amyloid, Amyloidosis, Brain, Humans, Protein Folding, Proteomics, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine > Inflammation
URI: http://discovery.ucl.ac.uk/id/eprint/1356159
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