Geometric protean graphs

We study the link structure of on-line social networks (OSNs), and introduce a new model for such networks which may help infer their hidden underlying reality. In the geo-protean (GEO-P) model for OSNs nodes are identified with points in Euclidean space, and edges are stochastically generated by a mixture of the relative distance of nodes and a ranking function. With high probability, the GEO-P model generates graphs satisfying many observed properties of OSNs, such as power law degree distributions, the small world property, densification power law, and bad spectral expansion. We introduce the dimension of an OSN based on our model, and examine this new parameter using actual OSN data. We discuss how the geo-protean model may eventually be used as a tool to group users with similar attributes using only the link structure of the network

Dimensionality of social networks using motifs and eigenvalues

We consider the dimensionality of social networks, and develop experiments aimed at predicting that dimension. We find that a social network model with nodes and links sampled from an $m$-dimensional metric space with power-law distributed influence regions best fits samples from real-world networks when $m$ scales logarithmically with the number of nodes of the network. This supports a logarithmic dimension hypothesis, and we provide evidence with two different social networks, Facebook and LinkedIn. Further, we employ two different methods for confirming the hypothesis: the first uses the distribution of motif counts, and the second exploits the eigenvalue distribution.Comment: 26 page

Heterozygous mis-sense mutations in Prkcb as a critical determinant of anti-polysaccharide antibody formation

To identify rate-limiting steps in T cell-independent type 2 (TI-2) antibody production against polysaccharide antigens, we performed a genome-wide screen by immunizing several hundred pedigrees of C57BL/6 mice segregating ENU-induced mis-sense mutations. Two independent mutations, Tilcara and Untied, were isolated that semi-dominantly diminished antibody against polysaccharide but not protein antigens. Both mutations resulted from single amino acid substitutions within the kinase domain of Protein Kinase C Beta (PKCβ). In Tilcara, a Ser552>Pro mutation occurred in helix G, in close proximity to a docking site for the inhibitory N-terminal pseudosubstrate domain of the enzyme, resulting in almost complete loss of active, autophosphorylated PKCβI whereas the amount of alternatively spliced PKCβII protein was not markedly reduced. Circulating B cell subsets were normal and acute responses to BCR-stimulation such as CD25 induction and initiation of DNA synthesis were only measurably diminished in Tilcara homozygotes, whereas the fraction of cells that had divided multiple times was decreased to an intermediate degree in heterozygotes. These results, coupled with evidence of numerous mis-sense PRKCB mutations in the human genome, identify Prkcb as a genetically sensitive step likely to contribute substantially to population variability in anti-polysaccharide antibody levels