Survey of Surveys (SoS) ‐ Mapping The Landscape of Survey Papers in Information Visualization

Information visualization as a field is growing rapidly in popularity since the first information visualization conference in 1995.However, as a consequence of its growth, it is increasingly difficult to follow the growing body of literature within the field.Survey papers and literature reviews are valuable tools for managing the great volume of previously published research papers,and the quantity of survey papers in visualization has reached a critical mass. To this end, this survey paper takes a quantumstep forward by surveying and classifying literature survey papers in order to help researchers understand the current landscapeof Information Visualization. It is, to our knowledge, the first survey of survey papers (SoS) in Information Visualization. Thispaper classifies survey papers into natural topic clusters which enables readers to find relevant literature and develops thefirst classification of classifications. The paper also enables researchers to identify both mature and less developed researchdirections as well as identify future directions. It is a valuable resource for both newcomers and experienced researchers in andoutside the field of Information Visualization and Visual Analytic

Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains

Cyclic nucleotide-binding (CNB) domains allosterically regulate the activity of proteins with diverse functions, but the mechanisms that enable the cyclic nucleotide-binding signal to regulate distant domains are not well understood. Here we use optical tweezers and molecular dynamics to dissect changes in folding energy landscape associated with cAMP-binding signals transduced between the two CNB domains of protein kinase A (PKA). We find that the response of the energy landscape upon cAMP binding is domain specific, resulting in unique but mutually coordinated tasks: one CNB domain initiates cAMP binding and cooperativity, whereas the other triggers inter-domain interactions that promote the active conformation. Inter-domain interactions occur in a stepwise manner, beginning in intermediate-liganded states between apo and cAMP-bound domains. Moreover, we identify a cAMP-responsive switch, the N3A motif, whose conformation and stability depend on cAMP occupancy. This switch serves as a signaling hub, amplifying cAMP-binding signals during PKA activation