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1 CF-7 cells that overexpressed the transgenic HMGA1a protein.
2 hook was evaluated by monitoring full-length HMGA1a protein binding using fluorescence anisotropy.
3 r in MCF-7 cells overexpressing HMGA1a; (ii) HMGA1a protein binds to AT-rich regions of the KL promot
4 d that, from a reversed-phase C4 column, the HMGA1a protein eluted in two different fractions with di
6 h lysine and arginine residues were found on HMGA1a proteins from metastatic cells compared to protei
7 f PTMs identified in this study suggest that HMGA1a proteins, like the histones, exhibit a biochemica
8 cates that one likely mechanism by which the HMGA1a protein promotes malignant changes in cells is th
9 and Ser102 were completely phosphorylated in HMGA1a protein, whereas only a portion of the protein wa
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