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The dynamic configuration and phosphorylation of the C-terminal HEAT domain of huntingtin modulates its function

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NIAID Data Ecosystem2026-03-11 收录
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https://www.omicsdi.org/dataset/pride/PXD013907
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资源简介:
Chemical cross-linking coupled to mass spectrometry was used to study different forms of human huntingtin (HTT). The variants included wild-type protein with poly-Q tail lengths of 23 and 78 and Ser2116 > Ala mutation of Q23- and Q78-HTT. Cross-linking was performed using the homobifunctional, lysine-reactive disuccinimidyl suberate (DSS).
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2020-07-07
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