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February 15, 1992Proceedings of the National Academy of SciencesOpen Access

Characterization of a guanine nucleotide-releasing factor and a GTPase-activating protein that are specific for the ras-related protein p25rab3A.

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Authors

EBEthan S. BursteinAcadia Pharmaceuticals (United States)IMIan G. MacaraVanderbilt University

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Burstein et al. (1992) studied this question.

synapsesocial.com/papers/6a8712c652b690c5299eb698https://doi.org/10.1073/pnas.89.4.1154
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Also Consider

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

  1. 1Regulation of reversible binding of smg p25A, a ras p21-like GTP-binding protein, to synaptic plasma membranes and vesicles by its specific regulatory protein, GDP dissociation inhibitor.1990 · 268 citations
  2. 2The <i>ras</i>-Like Protein p25<i><sup>rab3A</sup></i> Is Partially Cytosolic and Is Expressed Only in Neural Tissue1989 · 7 citations
  3. 3Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein.1990 · 306 citations
  4. 4The Cellular Functions of Small GTP-Binding Proteins1990 · 877 citations
  5. 5Evidence for Multiple, ras-like, Guanine Nucleotide-binding Proteins in Swiss 3T3 Plasma Membranes1989 · 19 citations