(32P)Phosphoryl Transfer by Endogenous Protein Kinase at the Ehrlich Cell Surface into Extrinsic Acceptor Proteins
Author:
Publisher
Uppsala Medical Society
Subject
General Medicine
Link
http://www.tandfonline.com/doi/pdf/10.3109/03009737409178394
Reference14 articles.
1. Nucleoside diphosphate kinase at the cell surface of neoplastic human cells in culture
2. Isolation of32P-Labelled Phosphorylserine from Ehrlich Mouse-Ascites Tumour Cells Suspended in an Isotonic Medium Containing32P-Labelled Adenosine Triphosphate
3. Isolation of 32P-Labelled Phosphorylserine and Phosphorylthreonine from Ehrlich Mouse-ascites Tumour Cells, Suspended in an Isotonic Medium, Containing 32P-Labelled Nucleoside Triphosphates or Inorganic Pyrophosphates.
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1. ECTO- AND EXO-PROTEIN KINASES IN SCHISTOSOMA MANSONI: REGULATION OF SURFACE PHOSPHORYLATION BY ACETYLCHOLINE AND IDENTIFICATION OF THE ALPHA SUBUNIT OF CKII AS A MAJOR SECRETED PROTEIN KINASE;Journal of Parasitology;2005-08
2. Cell Responses Initiated by Ecto-Kinases;The P2 Nucleotide Receptors;1998
3. Chemotactic activity of histones for human polymorphonuclear leukocytes;Experimental Pathology;1990-01
4. Phosphorylation of extracellular carbohydrates by intact cells. Chicken hepatocytes specifically adhere to and phosphorylate immobilized N-acetylglucosamine.;Journal of Biological Chemistry;1985-10
5. Endogenous surface phosphorylation reactions and ectokinase activity in the guinea pig T lymphocyte;Cellular Immunology;1984-09
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