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Publication Date:
June 2009
ISSN:
1437-4331
DOI:
10.1515/CCLM.2009.164

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Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the International Federation of Clinical Chemistry and Laboratory Medicine and the European Federation of Clinical Chemistry and Laboratory Medicine

Editor-in-Chief: Plebani, Mario

Editorial Board Member: Lippi, Giuseppe / Gillery, Philippe / Kazmierczak, Steven / Lackner, Karl J. / Melichar, Bohuslav / Siest, Gérard / Whitfield, John B. / Abi Fadel, Marianne / Alvarez Menendez, Francisco V. / Azzazy, Hassan M.E. / Diamandis, Eleftherios P. / Eckardstein, Arnold / Favaloro, Emmanuel J. / Griesmacher, Andrea / Herrmann, Wolfgang / Hoffmann, Johannes J.M.L. / Hooijkaas, Herbert / Ichihara, Kiyoshi / Kaabachi, Naziha / Kim, Jeong-Ho / Korte, Wolfgang / Kroupis, Christos / Lai, Leslie Charles / Lam, Wai Kei Christopher / Marc, Janja / Miyoshi, Eiji / Özben, Tomris / Palicka, Vladimir / Panteghini, Mauro / Queralto, Jose M. / Scartezini, Marileia / Simundic, Ana-Maria / Tsongalis, Gregory J. / Wallemacq, Pierre E. / Yan, Shengkai / Young, Ian S. / Chiu, Rossa Wai Kwun / Ghosh, Debabrata / Kappelmayer, Janos / Lehmann, Sylvain / Sypniewska, Grazyna

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Increased IMPACT FACTOR 2011: 2.150
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Proteomics in protein misfolding diseases

Monica Stoppini1 / Laura Obici2 / Francesca Lavatelli2 / Sofia Giorgetti1 / Loredana Marchese1 / Remigio Moratti1, 3 / Vittorio Bellotti1 / Giampaolo Merlini1, 2

1Department of Biochemistry, University of Pavia, Pavia, Italy

2Amyloidosis Research and Treatment Center, Biotechnology Research Laboratories, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy

3Clinical Chemistry Central Laboratory, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy

Corresponding author: Giampaolo Merlini, Department of Biochemistry, University of Pavia, Amyloidosis Research and Treatment Center, Biotechnology Research Laboratories, Fondazione IRCCS Policlinico San Matteo, P.le Golgi 19, 27100 Pavia, Italy Phone: +39-0382-502995, Fax: +39-0382-502990,

Citation Information: Clinical Chemistry and Laboratory Medicine. Volume 47, Issue 6, Pages 627–635, ISSN (Online) 1437-4331, ISSN (Print) 1434-6621, DOI: 10.1515/CCLM.2009.164, June 2009

Publication History:
Received:
2009-02-15
Accepted:
2009-04-20
Published Online:
2009-06-15

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.

Keywords: amyloidosis; diagnosis; pathogenesis; protein misfolding diseases

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