Myriad Genetics

About: Myriad Genetics is a company organization based out in Munich, Germany. It is known for research contribution in the topics: Cancer & Breast cancer. The organization has 562 authors who have published 586 publications receiving 56046 citations. The organization is also known as: Myriad Genetics, Inc..

Novel yeast two-hybrid system and use thereof

Abstract: A method for detecting protein-protein interactions is provided, in which two fusion proteins are prepared and allowed to interact with each other in yeast cells. The interaction between the two fusion proteins leads to protein trans-splicing, generating an active and detectable reporter.

Assessment of proteomic measures across serious psychiatric illness

Abstract: The diagnoses of serious psychiatric illnesses, such as schizophrenia, schizoaffective disorder, and bipolar disorder, rely on the subjective recall and interpretation of often overlapping...

Homologous recombination deficiency (HRD) in patients with pancreatic cancer (PC) and response to chemotherapy.

Abstract: 317Background: Mutations or copy number abnormalities of genes involved in homologous recombination occur in PC. DNA-based measures of HRD have been developed and may help identify tumors with better response to DNA damaging agents. This study aimed to describe the mutation and HRD status of PC and determine their association with treatment response and outcome. Methods: This was a retrospective analysis of tumor samples from patients treated at Indiana University for locally advanced or metastatic PC. Patients were included if they received gemcitabine/nab-paclitaxel or FOLFIRINOX and had adequate follow up to assess survival and response to therapy. Tumor analysis generated a 3-biomarker (LOH, TAI, LST) HRD score and mutation data for 45 genes. Results: Ninety-one samples met inclusion criteria, 78 (15 FFPE and 63 FNA) generated mutation data. HRD analysis was successful for 57; the primary cause of failure low tumor %. The final analysis set consisted of 78 samples with mutation status, including 57 wi...

In vitro translation and computational analyses of human profilin multimers.

Abstract: Profilin is an ubiquitous intracellular G-actin and PIP2-binding protein that is a pan-allergen. Functional native human profilin multimers have recently been described, implicating regulatory roles in cell morphology, signaling and allergies. Considering the potential importance of profilin self-association in nature, multimerization was examined using cDNAs to human profilin I (P1) and II (P2) by employing a plasmid (pCITE2a+) for in vitro transcription/radiolabeled translation. Autoradiography of affinity column purified 35S-met-P1 or -P2 revealed predominant -14.8, 30 and 58 kDa bands that corresponded to parallel immunoblots using rabbit anti-human profilin antibodies. Reducing agents had no significant effect on the ratios of cpm associated with gel slices corresponding to 14.8/30/58 kDa profilin bands. Computer-based molecular modeling was used to further analyze a hypothetical structure for profilin multimers resistant to reducing agents. The crystalline P1 structure was downloaded and analyzed for likely sulphydryl bonding via the three integral cysteines (C16, C70, C127). All possible combinations of SH-bonds were investigated. The energetically most favorable dimer involved C16 + C127. 3-Dimensional conformation also revealed a protective pocket around the S-S bonds. The data show that, similar to native human and plant profilins, P1 and P2 cDNAs encode proteins that form fastidious multimers. A structure is proposed with relatively protected disulfide bridges between individual profilin moieties consistent with existing biochemical data.