https://www.selleckchem.com/JAK.html The tumor suppressor phosphatase and tensin homologue (PTEN) is a redox-sensitive dual specificity phosphatase with an essential role in the negative regulation of the PI3K-AKT signaling pathway, affecting metabolic and cell survival processes. PTEN is commonly mutated in cancer, and dysregulation in the metabolism of PIP3 is implicated in other diseases such as diabetes. PTEN interactors are responsible for some functional roles of PTEN beyond the negative regulation of the PI3K pathway and are thus of great importance in cell biology. Both high-data content proteomics-based approaches and low-data content PPI approaches have been used to investigate the interactome of PTEN and elucidate further functions of PTEN. While low-data content approaches rely on co-immunoprecipitation and Western blotting, and as such require previously generated hypotheses, high-data content approaches such as affinity pull-down proteomic assays or the yeast 2-hybrid system are hypothesis generating. This review provides an overview of the PTEN interactome, including redox effects, and critically appraises the methods and results of high-data content investigations into the global interactome of PTEN. The biological significance of findings from recent studies is discussed and illustrates the breadth of cellular functions of PTEN that can be discovered by these approaches.We present a computational scheme for restricted-active-space configuration interaction (RASCI) calculations combined with second-order perturbation theory (RASCI-PT2) on a fragment of a periodic system embedded in the periodic Hartree-Fock (HF) wave function. This method allows one to calculate the electronic structure of localized strongly correlated features in crystals and surfaces. The scheme was implemented via an interface between the Cryscor and Q-Chem codes. To evaluate the performance of the embedding method, we explored dissociation of a fluorine atom from a lithium fluori