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Structural basis for binding of RILPL1 to TMEM55B reveals a lysosomal platform for adaptor assembly through a conserved TBM motif

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Zenodo2025-08-17 更新2026-05-26 收录
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We performed a DIA based mass spectrometry analysis using TMEM55B wild type and R151E mutant as bait in the presence of LRRK2 Y1699C (kinase active) and Rab8A Q67L (GTP bound active form) to explore the new interactors of TMEM55B. In another experiment, we used the wild type TMEM55B as bait in the presence of Rab8A Q67L (GTP bound active form) either with LRRK2 Y1699C (kinase active) or with LRRK2 Y1699C D2017A (kinase dead). Table of contents Table Number Description Corresponding Figures or section in manuscript Table 1 Search result of DIA MS data: TMEM55B WT IP vs R151E IP with LRRK2 Y1699C and Rab8A Q67L These data were used to generate Fig 3A. Table 2 Search result of DIA MS data: TMEM55B WT IP with LRRK2 Y1699C and Rab8A Q67L vs TMEM55B WT IP with LRRK2 Y1699C D2017A and Rab8A Q67L These data were used to generate Fig 3C. Table 3 Complete LC and DIA-MS Parameters This table corresponds to the LC-MS/MS analysis section.

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2025-08-17
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