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Phosphorylation of membrane proteins in erythrocytes treated with lead
Luisa Belloni-Olivi
, Madhu Annadata
,
Gary W. Goldstein
,
Joseph P. Bressler
School of Medicine
Bloomberg School of Public Health
Research output
:
Contribution to journal
›
Article
›
peer-review
31
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Keyphrases
Phosphorylation
100%
Membrane Protein
100%
Erythrocytes
100%
Lead Acetate
83%
Protein Kinase C
83%
Cytoskeletal Proteins
33%
Phorbol 12-myristate 13-acetate
33%
Diacylglycerol
33%
Human Erythrocytes
33%
CAMP-dependent Protein Kinase
16%
Molecular Mass
16%
Cell-to-cell
16%
Endothelial Cells
16%
Protein Phosphatase
16%
Immature Rats
16%
Direct Interaction
16%
Cell Exposure
16%
Microvessels
16%
Casein Kinase 2
16%
Phorbol 12
16%
Glioma Cells
16%
Kinase Protein
16%
Biochemistry, Genetics and Molecular Biology
Protein Kinase C
100%
Membrane Protein
100%
phosphorylation
100%
Myristic Acid
40%
Cytoskeletal Proteins
40%
Enzyme
20%
Protein Kinases
20%
Molecular Weight
20%
Cyclic Adenosine Monophosphate
20%
Phosphoprotein Phosphatase
20%
Casein Kinase
20%
Diacylglycerol
20%
Diglyceride
20%
Rat
20%
Pharmacology, Toxicology and Pharmaceutical Science
Protein Kinase C
100%
Membrane Protein
100%
Lead Acetate
100%
Cytoskeleton Protein
40%
12-O-Tetradecanoylphorbol-13-Acetate
40%
Protein Kinases
20%
Casein Kinase
20%
Phorbol 12,13-dibutyrate
20%
Phosphoprotein Phosphatase
20%
Diacylglycerol
20%
Enzymes
20%
Rat
20%
Glioma
20%
Neuroscience
Acetate
100%
phosphorylation
100%
Protein Kinase C
71%
Phorbol
42%
Myristic Acid
28%
Cytoskeleton Protein
28%
Cyclic Adenosine Monophosphate
14%
Microvessel
14%
Protein Kinases
14%
Phosphoprotein Phosphatase
14%
Enzymes
14%
Casein Kinase
14%
Diglyceride
14%
Glioma
14%