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Proteomics in protein misfolding diseases.

STOPPINI, MONICA;LAVATELLI, FRANCESCA;GIORGETTI, SOFIA;MORATTI, REMIGIO;BELLOTTI, VITTORIO;MERLINI, GIAMPAOLO
2009-01-01
2009
The Biotechnology & Applied Microbiology category includes resources on a number of subjects that relate to the exploitation of living organisms or their components. In CC/AB&ES, the emphasis is on applied biology, including industrial microbiology. Applications include industrial chemicals and enzymes, biosensors, bioelectronics, pesticide development, food, flavor and fragrance industry applications, waste treatment, and pollution bioremediation.
CLINICAL CHEMISTRY AND LABORATORY MEDICINE
sì
WOS:000267978700002
2-s2.0-67650585848
Sì, ma tipo non specificato
Inglese
Internazionale
STAMPA
47
627
635
9
19527136
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. Clin Chem Lab Med 2009;47:627-35.
Proteomica; misfolding diseases
8
info:eu-repo/semantics/article
262
Stoppini, Monica; Laura, Obici; Lavatelli, Francesca; Giorgetti, Sofia; Loredana, Marchese; Moratti, Remigio; Bellotti, Vittorio; Merlini, Giampaolo...espandi
1 Contributo su Rivista::1.1 Articolo in rivista
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1.1 Articolo in rivista
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/150959
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