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1 he structure and biochemical activity of the v-Abl protein.
3 ance those mediated via other regions of the v-Abl protein and facilitate transformation of primary,
4 te for that of v-Abl in the full-length P120 v-Abl protein and in P70 v-Abl, a protein that lacks the
5 ine kinase activities of oncogenic BCRABL or v-ABL protein and propose that AAP1 functions as a trans
8 at MA sequences within the Gag moiety of the v-Abl protein contribute to proper localization by playi
15 that one important transforming function of v-Abl proteins is overcoming the effects of a functional
16 ymphoid transformation, mutants expressing a v-Abl protein lacking portions of the COOH terminus were
17 e leukemia virus (Ab-MLV) mutants expressing v-Abl proteins lacking the carboxyl terminus are comprom
18 Immunofluorescence analysis revealed that a v-Abl protein retaining only the first 34 amino acids of
19 reflects a balance between signals from the v-Abl protein that drive transformation and those coming
20 reviously studied mutants encoding truncated v-Abl proteins that lack the extreme carboxyl terminus r
21 ag-derived myristoylation signal targets the v-Abl protein to the plasma membrane, the protein contai
22 monstrated previously that the activation of v-Abl protein tyrosine kinase (PTK) in IC.DP murine pre-
23 n murine leukemia virus (Ab-MLV) encodes the v-Abl protein tyrosine kinase and induces transformation
28 once cells are fully transformed, an active v-Abl protein tyrosine kinase is required to suppress ap
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