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IJMS | Free Full-Text | The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins
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Phosphorylation-regulated HMGA1a-P53 interaction unveils the function of HMGA1a acidic tail phosphorylations via synthetic proteins - ScienceDirect
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IJMS | Free Full-Text | The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins
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Mapping Unstructured Regions and Synergistic Folding in Intrinsically Disordered Proteins with Amide H/D Exchange Mass Spectrometry | Biochemistry
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Mapping Unstructured Regions and Synergistic Folding in Intrinsically Disordered Proteins with Amide H/D Exchange Mass Spectrometry | Biochemistry
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