@article{oai:yamanashi.repo.nii.ac.jp:00003145,
 author = {OZAKI, Yukio},
 issue = {2},
 journal = {山梨医科大学雑誌, 山梨医科大学雑誌},
 month = {},
 note = {Tyrosine protein kinases that phosphorylate substrate proteins at the tyrosine residues are abundant in human platelets. The major component of tyrosine kinase is attributed to pp60c-src which is a protooncogene product. Upon stimulation of platelets, several sets of tyrosine-phosphorylated proteins are expressed, the type and time course of which vary with different agonists employed. The tyrosine kinase activity may be closely associated with the activation of the fibrinogen-binding glycoprotein IIb/IIIa, intracellular Ca++ mobilization, and inositol phosphofipid metabolism.},
 pages = {35--41},
 title = {<Review> Tyrosine Kinase and Platelet Functions},
 volume = {7},
 year = {1992}
}