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November 1, 1985Molecular and Cellular Biology

Detection of c-abl tyrosine kinase activity in vitro permits direct comparison of normal and altered abl gene products.

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Authors

JKJames B. KonopkaStony Brook SchoolOwen N. WitteOwen N. WitteUniversity of California, Riverside

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Cite This Study

Konopka et al. (1985) studied this question.

synapsesocial.com/papers/6a16d7e92fcf950e00055af4https://doi.org/10.1128/mcb.5.11.3116
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Only site-directed antibodies reactive with the highly conserved src-homologous region of the v-abl protein neutralize kinase activity1984 · 117 citations
  2. 2Low Level of Cellular Protein Phosphorylation by Nontransforming Overproduced p60 c- src1985 · 171 citations
  3. 3A membrane-associated, carbohydrate-modified form of the v-abl protein that cannot be phosphorylated in vivo or in vitro1984 · 21 citations
  4. 4Two structurally and functionally different forms of the transforming protein of PRC II avian sarcoma virus.1982 · 21 citations
  5. 5Phosphorylation of synthetic peptides by a tyrosine protein kinase from the particulate fraction of a lymphoma cell line.1982 · 192 citations