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Following protein sequencing of the isolated ∼ 45 kDa imidazoline binding protein, we identified it to be brain creatine kinase (B-CK).
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In screens for VAB-19 binding proteins we identified the signaling adaptor EPS-8.
The RNA binding proteins we identified as crucial, are predominantly involved in RNA processing and include a CAF1 family ribonuclease (MAL8P1.104), a DEAD-box helicase (MAL8P1.19), a forkhead-associated domain (FHA) containing RNA binding protein (PF11_0347), a pre-mRNA splicing protein (PFD0180c) and an RNA recognition motif (RRM) domain containing protein (PF13_0318) (Table 3).
In a pilot mass spectrometry screen for Tld binding proteins we identified Collagen IV, an extracellular matrix protein that we have previously shown to be required for Dpp gradient formation (Wang et al., 2008).
Using a novel two-hybrid screen for rapamycin-dependent TOR-binding proteins, we identified the C. neoformans FKBP12 homolog, encoded by the FRR1 gene.
Interestingly, two of the RNA binding proteins we have identified as vital for intraerythrocytic growth, PF13_0318 and PF08_0086, were previously identified as important interacting partners in an early computational model of the P. falciparum interactome [7].
This reassured us that the eluates from the GST-14-3-3-affinity GST-14-3-3-affinity GST-14-3-3-affinity GST-14-3-3-affinity GST-14-3-3-affinityteins we identified were not artifactual results generated by the use of the GST-14-3-3-affinity purificationstechnique.
Indeed, among the top 30 RNA-binding proteins that we identified in mouse brain extracts to bind to biotinylated (GGGGCC 30 RNA in vitro, 8 are hnRNP proteins.
In order to identify specifically binding proteins, we generated biotinylated LTSM-positive probes from RPL36 and performed a protein pull-down from nuclear extracts in the presence of the unlabeled LTSM-negative RPS6 25mer competitor.
In a unique genome-wide unbiased screen for cell surface proteins binding Aβo, we identified PrPC[ 1].
At the time of its identification, no RNA binding protein was identified as a partner of the HP1 protein family.
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