Modulation of p36 phosphorylation in human cells: studies using anti-p36 monoclonal antibodies.
We have characterized two monoclonal antibodies which recognize human p36. These have been used to examine the sites and extent of serine and tyrosine phosphorylation of p36 in human cells treated with epidermal growth factor and platelet-derived growth factor and in human cells transformed with viruses whose oncogenes encode protein-tyrosine kinases.
D017302:Annexins; D000911:Antibodies, Monoclonal; D002472:Cell Transformation, Viral; D004815:Epidermal Growth Factor / Q000494:pharmacology; D006801:Humans; D008565:Membrane Proteins / Q000276:immunology / Q000378:metabolism*; D015688:Oncogene Protein pp60(v-src); D009857:Oncogenes; D010766:Phosphorylation; D010982:Platelet-Derived Growth Factor / Q000494:pharmacology; D011505:Protein-Tyrosine Kinases / Q000235:genetics; D012191:Retroviridae Proteins / Q000378:metabolism; D012694:Serine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D017302:Annexins; D000911:Antibodies, Monoclonal; D008565:Membrane Proteins; D010982:Platelet-Derived Growth Factor; D012191:Retroviridae Proteins; D014443:Tyrosine; D012694:Serine; D004815:Epidermal Growth Factor; D011505:Protein-Tyrosine Kinases; D015688:Oncogene Protein pp60(v-src)