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Matches in Nanopublications for { ?s ?p " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " ?g. }

• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.
• _5 value " Here, as a first step toward pinpointing this role, we have employed two-dimensional tryptic mapping to directly identify the major sites of Src-induced p120 phosphorylation. Eight sites were identified by direct mutation of candidate tyrosines to phenylalanine and elimination of the accompanying spots on the two-dimensional maps. Identical sites were observed in vitro and in vivo, strongly suggesting that the physiologically important sites have been correctly identified. (Next section taken from Results - Fig 4) Mutation of tyrosines 112, 228, and 280 to phenylalanine resulted in elimination of phosphopeptide spots 6, 7, and 8, respectively. Mutation of tyrosine 96 eliminated spots 9 and 10, whereas mutation of tyrosine 257 eliminated spots 4 and 5...These results suggest that peptides 1, 2, and 3 represent singly, doubly, and triply phosphorylated variants, respectively, of the same peptide, containing Tyr291, Tyr296, and Tyr302. " provenance.