Ca2+-CaM activation of AMP deaminase contributes to adenine nucleotide dysregulation and phosphatidylserine externalization in human sickle erythrocytes-Reference-Cited by-同舟云学术

Ca2+-CaM activation of AMP deaminase contributes to adenine nucleotide dysregulation and phosphatidylserine externalization in human sickle erythrocytes

Published:2009-02 Issue:3 Volume:144 Page:434-445
ISSN:0007-1048
Container-title:British Journal of Haematology
language:en
Short-container-title:

Author:

Sabina Richard L.,Wandersee Nancy J.,Hillery Cheryl A.

Publisher

Wiley

Subject

Hematology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2141.2008.07473.x/fullpdf

Reference58 articles.

1. Activation by calcium of AMP deaminase from the human red cell;Almarez;FEBS Letters,1989

2. Calcium-induced conversion of adenine nucleotides to inosine monophosphate in human red cells;Almarez;Journal of Physiology,1988

3. Modifying effects of anions on the alkali-cation-activated AMP deaminase of human erythrocytes;Askari;Molecular Pharmacology,1966

4. Regulation of AMP deaminase by 2,3-diphosphoglyceric acid: a possible mechanism for the control of adenine nucleotide metabolism in human erythrocytes;Askari;Biochimica et Biophysica Acta,1968

5. The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers;Atkinson;Biochemistry,1968

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