Isolation of a 54 kDa tyrosyl-phosphorylated protein from the integument of the Medfly Ceratitis capitata: Possible physiological substrate for integumental phosphatase activity
Author:
Publisher
Elsevier BV
Subject
Insect Science,Molecular Biology,Biochemistry
Reference22 articles.
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3. Phosphorylation of endogenous proteins by a cyclic AMP-dependent protein kinase in the wing epidermis of Manduca sexta;Bishoff;Insect Biochem.,1991
4. Integumental phosphatase iso-enzymes from white puparia of Ceratitis capitata: isolation and characterization;Bourtzis;Biochem. cell Biol.,1991
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Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Changes of protein tyrosine phosphorylation in third instar larval integument of the Mediterranean fruit fly,Ceratitis capitata;Archives of Insect Biochemistry and Physiology;2002-04-10
2. Expression of the major tyrosyl phosphoprotein of 54 KDa in the integument of the medfly Ceratitis capitata;Roux's archives of developmental biology;1994-10
3. Expression and visualization during cell cycle progression of alkaline phosphatase in B lymphocytes from C3H/HeJ mice;Journal of Leukocyte Biology;1994-05
4. Expression of the major tyrosyl phosphoprotein of 54 KDa in the integument of the medflyCeratitis capitata;Roux's Archives of Developmental Biology;1994
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