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P-Rex1 adopts an inactive, compact conformation that is stabilized by an abundant intracellular molecule and undergoes dynamic changes to extend upon encountering signaling phospholipids in membranes.

Studies of Lowe syndrome patient cells, which lack the inositol 5-phosphatase OCRL, suggest that a defect in endocytosis plays a role in the pathological manifestations of the disease.

Dimerization promotes nonlinear kinetics in PIP5K-dependent lipid phosphorylation reactions.

The Sac1 phosphatase domain, rather than the proline-rich domain, plays an essential role in synaptojanin activity during endocytosis.

A subtle mutation in the ATP-binding site of inositol hexakisphosphate kinases increases their conformational flexibility and thereby makes them susceptible to isozyme-selective, allosteric inhibition.

Using barcoded mutagenesis and a high-throughput genetic screen results in the identification of 150 genes that affect lipid accumulation in a non-model yeast system.

eMags is an engineered photodimerizer pair for optogenetic modulation in mammalian cells that is especially suited for the manipulation of intracellular processes occurring in small volumes or subcellular organelles.

A key B-cell tyrosine kinase that adopts an autoinhibited conformation, and can be activated by either membrane recruitment or soluble inositol hexakisphosphates in solution.

SAC1 is unable to adopt an efficient "trans" mode of action in living cells.

Simulations reveal where phosphoinositide lipids bind to voltage-gated sodium channels and how they reduce channel activity.