Title : Purification and characterization of a higher-molecular-mass form of protein phosphotyrosine phosphatase (PTP 1B) from placental membranes.

Pub. Date : 1991 Jun 1

PMID : 1646596






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The p56lck can be dephosphorylated by PTP-I at two tyrosine residues (Tyr-394 and Tyr-505), which are differentially phosphorylated in vitro and in vivo and have been suggested to modulate kinase activity. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens
2 The p56lck can be dephosphorylated by PTP-I at two tyrosine residues (Tyr-394 and Tyr-505), which are differentially phosphorylated in vitro and in vivo and have been suggested to modulate kinase activity. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens
3 The p56lck can be dephosphorylated by PTP-I at two tyrosine residues (Tyr-394 and Tyr-505), which are differentially phosphorylated in vitro and in vivo and have been suggested to modulate kinase activity. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens