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Protonation- and substrate-regulated dimer opening couples brain-type creatine kinase to vesicular and actin-remodeling membranes

2026-08-09

Abstract excerpt

Brain-type creatine kinase (CK-BB) buffers local ATP demand through reversible phosphotransfer between ATP and phosphocreatine, yet how this soluble metabolic enzyme couples to dynamic membrane compartments remains unclear. Here, we integrate immunofluorescence microscopy, DEER spectroscopy, hydrogen-deuterium exchange and native mass spectrometry, DEER- and AlphaFold-guided modeling, and long-timescale molecular...

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Literature Corpus work
36bca908-da7d-52b2-b29a-62c158c3032b
DOI
10.64898/2026.08.04.742861
Open publication

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Protonation- and substrate-regulated dimer opening couples brain-type creatine kinase to vesicular and actin-remodeling membranesDOI 10.64898/2026.08.04.742861
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