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Two P-Thrs in SF3B1 are required for interaction with SNIP1s FHA domain Given that SNIP1 harbors a candidate P-Thr-binding FHA domain at its C-terminus, we tested whether this domain is necessary for interaction with P-SF3B1 (Fig

Standard glutathione is often broken down into its individual amino acids by stomach enzymes before it can ever be absorbed

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The tritium water content was 30.1% (female) and 29.3% (male), and the content of [ 3 H]proline (M1) was higher, accounting for 20.7% (female) and 30.2% (male) of the total radioactivity (Figure 5D)