IndraLab

Statements


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"IKK mediated CYLD activation is expected to remove K63 linked polyubiquitins from PSD proteins and thus regulate their trafficking."

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"Thus, CYLD and SPATA2 form a highly stable heterotetramer.43 Phosphorylation-mediated allosteric changes of a protein can reason to dimerization, which facilitates the binding of many response regulators to their partners.76 Therefore, homo-dimerized IKKϵ-mediated Ser418 phosphorylation could promote dimerization of CYLD and thus facilitate the interaction of CYLD with SPATA2."

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"Unexpectedly, our recent study revealed that NEMO is modified by SUMO-3, and this modification prevents the access of CYLD to the IKK complex, thus impairing the negative action of CYLD, a de-ubiquiti[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"