PAX3-FOXO1 dictates myogenic reprogramming and rhabdomyosarcoma identity in endothelial progenitors.

Fusion-positive rhabdomyosarcoma (FP-RMS) driven by the expression of the PAX3-FOXO1 (P3F) fusion oncoprotein is an aggressive subtype of pediatric rhabdomyosarcoma. FP-RMS histologically resembles developing muscle yet occurs throughout the body in areas devoid of skeletal muscle highlighting that FP-RMS is not derived from an exclusively myogenic cell of origin. Here we demonstrate that P3F reprograms mouse and human endothelial progenitors to FP-RMS.

Recoil Corrections to the Energy Levels of Hydrogenic Atoms.

We have completed the calculation of pure-recoil corrections of order (Zα)^{6} to Coulombic bound states of two spin-1/2 fermions without approximation in the particle masses. Our result applies to systems of arbitrary mass ratio such as muonium and positronium, as well as hydrogen and muonic hydrogen (with the neglect of proton structure effects). We have shown how the two-loop master integrals that occur in the relativistic region can be computed in analytic form and suggest that the same method can be applied to the three-loop integrals that would be present in a calculation of order (Zα)^{7} corrections.

Gut Microbiome Composition and Metabolic Capacity Differ by Secretor Status in Exclusively Breastfed Infants.

A major polymorphism in the fucosyltransferase2 (FUT2) gene influences risk of multiple gut diseases, but its impact on the microbiome of breastfed infants was unknown. In individuals with an active FUT2 enzyme (“secretors”), the intestinal mucosa is abundantly fucosylated, providing mutualist bacteria with a rich endogenous source of fucose. Non-secretors comprise approximately one-fifth of the population, and they lack the ability to create this enzyme.

Identifying Interaction Partners of Yeast Protein Disulfide Isomerases Using a Small Thiol-Reactive Cross-Linker: Implications for Secretory Pathway Proteostasis.

Protein disulfide isomerases (PDIs) function in forming the correct disulfide bonds in client proteins, thereby aiding the folding of proteins that enter the secretory pathway. Recently, several PDIs have been identified as targets of organic electrophiles, yet the client proteins of specific PDIs remain largely undefined. Here, we report that PDIs expressed in are targets of divinyl sulfone (DVSF) and other thiol-reactive protein cross-linkers.