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Our DeepPhospho-empowered workflow substantially expands the phosphoproteome coverage while maintaining high quantification performance, which leads to the discovery of more signaling pathways and regulated kinases in an EGF signaling study than the DDA library-based approach

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The VPS subcomplex consists of VPS26-VPS29-VPS35, where VPS35 interacts with VPS26 and VPS29 through its N-terminal and C-terminal domains, respectively, forming a horseshoe-shaped -helix 28