How does the ER send misfolded proteins to destruction?
Our new Communications Biology study uncovers a 6:6 Derlin-1/p97 complex, a dynamic channel that bridges ER quality control with cytoplasmic degradation.
rdcu.be/eLMSx
20.10.2025 01:06
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The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation - Nature Communications
This study reveals the structural basis of collagen processing by the KOGG complex, revealing how it catalyzes lysine hydroxylation and dual-glycosylation, essential for collagen folding and stability...
Our latest cryo-EM study reveals the architecture of the KOGG complex, a key player in collagen lysine O-link glycosylation. This LH3/ColGalT1 enzyme machinery ensures proper collagen maturation and may even form fiber-like supercomplexes! #Glycosylation #Collagen
doi.org/10.1038/s41467-025-57768-9
15.03.2025 04:47
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