A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec 1-related Vps33p

The gene product of the Saccharomyces cerevisiae open reading frame YDR229w (named IVY1 for: Interacting with Vps33p and Ypt7p) was found to interact with both the GTPase Ypt7p and the Sec1-related Vps33 protein. While deletion of IVY1 does not lead to any recognized change in phenotype, overexpression of Ivy1p leads to fragmentation of the vacuole, missorting of the vacuolar enzyme carboxypeptidase Y (CPY) to the exterior of the cell, and an accumulation of multivesicular bodies inside the cell. All effects caused by the overexpression of Ivy1p can be reset by simultaneously raising the amount of Vps33p. This suppression activity of Vps33p suggests that Ivv1p and Vps33p at least partially counteract the action of each other in the cell. The intracellular level of Ivy1p increases in cells approaching stationary growth phase at which part of the protein is located at the rim of the vacuole. In addition to its specific interactions with members of two regulatory protein families, Ivy1p in vitro shows a marked propensity for binding phospholipids with high affinity

Types from Data: Making Structured Data First-class Citizens in F#

Most modern applications interact with external services and access data in structured formats such as XML, JSON and CSV. Static type systems do not understand such formats, often making data access more cumbersome. Should we give up and leave the messy world of external data to dynamic typing and runtime checks? Of course, not! We present F# Data, a library that integrates external structured data into F#. As most real-world data does not come with an explicit schema, we develop a shape inference algorithm that infers a shape from representative sample documents. We then integrate the inferred shape into the F# type system using type providers. We formalize the process and prove a relative type soundness theorem. Our library significantly reduces the amount of data access code and it provides additional safety guarantees when contrasted with the widely used weakly typed techniques

A novel phospholipid-binding protein from the yeast Saccharomyces cerevisiae with dual binding specificities for the transport GTPase Ypt7p and the Sec 1-related Vps33p

The gene product of the Saccharomyces cerevisiae open reading frame YDR229w (named IVY1 for: Interacting with Vps33p and Ypt7p) was found to interact with both the GTPase Ypt7p and the Sec1-related Vps33 protein. While deletion of IVY1 does not lead to any recognized change in phenotype, overexpression of Ivy1p leads to fragmentation of the vacuole, missorting of the vacuolar enzyme carboxypeptidase Y (CPY) to the exterior of the cell, and an accumulation of multivesicular bodies inside the cell. All effects caused by the overexpression of Ivy1p can be reset by simultaneously raising the amount of Vps33p. This suppression activity of Vps33p suggests that Ivv1p and Vps33p at least partially counteract the action of each other in the cell. The intracellular level of Ivy1p increases in cells approaching stationary growth phase at which part of the protein is located at the rim of the vacuole. In addition to its specific interactions with members of two regulatory protein families, Ivy1p in vitro shows a marked propensity for binding phospholipids with high affinity

Chemical modification of temoporfin - A second generation photosensitizer activated using upconverting nanoparticles for singlet oxygen generation

LiYF4:Tm3+/Yb3+ upconverting nanoparticles (UCNPs) were functionalized with the second generation photosensitizer 5,10,15,20-tetra(m-hydroxyphenyl)chlorin (m-THPC, Temoporfin, Foscan®). m-THPC was modified using 4-(bromomethyl)benzoic acid, which induced a bathochromic shift of the m-THPC blue absorption peak. The nanoconstruct causes up to 70% cell death under 980 nm irradiationJ.A.C. is a Concordia University Research Chair in Nanoscience and is grateful to Concordia University for financial support. J.A.C., P.F., G.L. and R.N. are grateful for the support from (NSERC) Canada