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sho c. takatori lipid membrane 2019

sho c. takatori lipid membrane 2019 PMP2/FABP8 induces PI(4,5)P2-dependent transbilayer reorganization of sphingomyelin in the plasma membrane: Cell Reports Lipid Interactions of a Ciliary

Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin 2 ScienceDirect Active Surface Flows Accelerate the Coarsening of Lipid Membrane Domains Phys. Rev. Lett. Frontiers Lipid Rafts, Sphingolipids, and Ergosterol in Yeast Vacuole Fusion and Maturation Nonequilibrium Dynamics at Cellular Interfaces: Insights From Simulation and Theory Jiao 2024 WIREs Computational Molecular Science Wiley Online Library

SKU: 60270981490 · From www.marsberger-treibhaus.de

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Description

Two calpain-sensitive hinge regions (H1 and H2) separate the 24 repeats in a rod-1 domain (repeats 115), rod-2 domain (repeats 1623), and repeat 24

sho c. takatori lipid membrane 2019 PMP2/FABP8 induces PI(4,5)P2-dependent transbilayer reorganization of sphingomyelin in the plasma membrane: Cell Reports Lipid Interactions of a Ciliary

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sho c. takatori lipid membrane 2019 PMP2/FABP8 induces PI(4,5)P2-dependent transbilayer reorganization of sphingomyelin in the plasma membrane: Cell Reports Lipid Interactions of a Ciliary

Markov, A

sho c. takatori lipid membrane 2019 PMP2/FABP8 induces PI(4,5)P2-dependent transbilayer reorganization of sphingomyelin in the plasma membrane: Cell Reports Lipid Interactions of a Ciliary

Lee SB, Kim JJ, Han SA, Fan Y, Guo LS, Aziz K, et al

sho c. takatori lipid membrane 2019 PMP2/FABP8 induces PI(4,5)P2-dependent transbilayer reorganization of sphingomyelin in the plasma membrane: Cell Reports Lipid Interactions of a Ciliary
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