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VAP A intrinsically disordered regions enable versatile tethering at membrane contact sites ScienceDirect Figure 2 from OSBP Related Protein Family in Lipid Transport Over Membrane Contact Sites Semantic Scholar Motor Neuron Disease Associated Mutant Vesicle Associated Membrane Protein Associated Protein (VAP) B Recruits Wild Type VAPs into Endoplasmic Reticulum Derived Tubular Aggregates Journal of Neuroscience Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7RILPp150Glued and late endosome positioning Journal of Cell Biology Rockefeller University Press A genetic screen to uncover mechanisms underlying lipid transfer protein function at membrane contact sites Life Science Alliance
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VAP-A intrinsically disordered regions enable versatile tethering at  membrane contact sites - ScienceDirect
Figure 2 from OSBP-Related Protein Family in Lipid Transport Over Membrane  Contact Sites | Semantic Scholar
Motor Neuron Disease-Associated Mutant Vesicle-Associated Membrane Protein-Associated  Protein (VAP) B Recruits Wild-Type VAPs into Endoplasmic Reticulum-Derived  Tubular Aggregates | Journal of Neuroscience
Cholesterol sensor ORP1L contacts the ER protein VAP to control  Rab7RILPp150Glued and late endosome positioning | Journal of Cell Biology  | Rockefeller University Press
A genetic screen to uncover mechanisms underlying lipid transfer protein  function at membrane contact sites | Life Science Alliance

vap protein VAPA

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