Heat-shock protein-27, -70 and peroxiredoxin–II show molecular chaperone function in sickle red cells: Evidence from transgenic sickle cell mouse model-Reference-Cited by-同舟云学术

Heat-shock protein-27, -70 and peroxiredoxin–II show molecular chaperone function in sickle red cells: Evidence from transgenic sickle cell mouse model

Published:2008-05 Issue:5 Volume:2 Page:706-719
ISSN:1862-8346
Container-title:PROTEOMICS – CLINICAL APPLICATIONS
language:en
Short-container-title:Prot. Clin. Appl.

Author:

Biondani Andrea,Turrini Franco,Carta Franco,Matté Alessandro,Filippini Alida,Siciliano Angela,Beuzard Yves,De Franceschi Lucia

Publisher

Wiley

Subject

Clinical Biochemistry

Reference58 articles.

1. , in: , (Eds.), Disorders of Haemoglobin: Genetics, Pathophysiology, Clinical Managment, Cambridge University Press, Cambridge 2001, pp. 494–526.

2. , in: , , (Eds.), Sickle Cell Disease: Basic Principles and Clinical Practice. Raven, New York 1994. pp. 423–435.

3. Hemoglobin S gelation and sickle cell disease

4. Sickle Cell Hemoglobin Polymerization

5. Red blood cell changes during the evolution of the sickle cell painful crisis

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