The Risks of Ranking: Revisiting Graphical Perception to Model Individual Differences in Visualization Performance.

Graphical perception studies typically measure visualization encoding effectiveness using the error of an "average observer", leading to canonical rankings of encodings for numerical attributes: e.g., position area angle volume. Yet different people may vary in their ability to read different visualization types, leading to variance in this ranking across individuals not captured by population-level metrics using "average observer" models. One way we can bridge this gap is by recasting classic visual perception tasks as tools for assessing individual performance, in addition to overall visualization performance. In this paper we replicate and extend Cleveland and McGill's graphical comparison experiment using Bayesian multilevel regression, using these models to explore individual differences in visualization skill from multiple perspectives. The results from experiments and modeling indicate that some people show patterns of accuracy that credibly deviate from the canonical rankings of visualization effectiveness. We discuss implications of these findings, such as a need for new ways to communicate visualization effectiveness to designers, how patterns in individuals' responses may show systematic biases and strategies in visualization judgment, and how recasting classic visual perception tasks as tools for assessing individual performance may offer new ways to quantify aspects of visualization literacy. Experiment data, source code, and analysis scripts are available at the following repository: https://osf.io/8ub7t/?view_only=9be4798797404a4397be3c6fc2a68cc0.

Mutation of lysine 1370 in full-length human alpha2-macroglobulin blocks binding to the low density lipoprotein receptor-related protein-1.

alpha2-Macroglobulin (alpha2M) regulates cell physiology by binding to cellular receptors; however, residues that contribute to receptor-binding have not been elucidated in the full-length protein. In alpha2M fragments, expressed in bacteria, Lys(1370) and Lys(1374) are critical for binding to the low density lipoprotein receptor-related protein-1 (LRP-1) and a distinct alpha2M-signaling receptor. We expressed full-length recombinant human alpha2M (r(alpha)2M) and mutants in which Lys(1370) or Lys(1374) was converted to alanine in K-562 cells. The r(alpha)2M species demonstrated intact structure and function, as determined by subunit size, intersubunit disulfide bonds, reaction with trypsin or methylamine, and ability to undergo conformational change. Binding of transforming growth factor-beta1 was unaltered. Mutation of Lys(1370) almost entirely inhibited specific binding of methylamine-activated r(alpha)2M to RAW 264.7 cells. Mutation of Lys(1374) had no effect. Binding of r(alpha)2M to RAW 264.7 cells was blocked by receptor-associated protein, indicating an essential role for LRP-1. These studies demonstrate that a single mutation in full-length r(alpha)2M is sufficient to block binding to LRP-1.