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The recent discovery of binary neutron star mergers has opened a new and exciting venue of research into hot and dense strongly interacting matter. For the first time, this elusive state of matter, described by the theory of quantum chromo dynamics, can be studied in two very different environments. On the macroscopic scale, in the collisions of neutron stars; and on the microscopic scale, in collisions of heavy ions at particle collider facilities. We will discuss the conditions that are created in these mergers and the corresponding high energy nuclear collisions. This includes the properties of quantum chromo dynamics matter, that is, the expected equation of state as well as expected chemical and thermodynamic properties of this exotic matter. To explore this matter in the laboratory, a new research prospect is available at the Facility for Antiproton and Ion Research, FAIR. The new facility is being constructed adjacent to the existing accelerator complex of the GSI Helmholtz Centre for Heavy Ion Research at Darmstadt/Germany, expanding the research goals and technical possibilities substantially. The worldwide unique accelerator and experimental facilities of FAIR will open the way for a broad spectrum of unprecedented research supplying a variety of experiments in hadron, nuclear, atomic, and plasma physics as well as biomedical and material science, which will be briefly described.
Complexome profiling is an emerging ‘omics’ approach that systematically interrogates the composition of protein complexes (the complexome) of a sample, by combining biochemical separation of native protein complexes with mass-spectrometry based quantitation proteomics. The resulting fractionation profiles hold comprehensive information on the abundance and composition of the complexome, and have a high potential for reuse by experimental and computational researchers. However, the lack of a central resource that provides access to these data, reported with adequate descriptions and an analysis tool, has limited their reuse. Therefore, we established the ComplexomE profiling DAta Resource (CEDAR, www3.cmbi.umcn.nl/cedar/), an openly accessible database for depositing and exploring mass spectrometry data from complexome profiling studies. Compatibility and reusability of the data is ensured by a standardized data and reporting format containing the “minimum information required for a complexome profiling experiment” (MIACE). The data can be accessed through a user-friendly web interface, as well as programmatically using the REST API portal. Additionally, all complexome profiles available on CEDAR can be inspected directly on the website with the profile viewer tool that allows the detection of correlated profiles and inference of potential complexes. In conclusion, CEDAR is a unique, growing and invaluable resource for the study of protein complex composition and dynamics across biological systems.