Abstract: The study of proteomics reached unexpected levels of
interest, as a direct consequence of its discovered influence over some
complex biological phenomena, such as problematic diseases like
cancer. This paper presents the latest authors- achievements regarding
the analysis of the networks of proteins (interactome networks), by
computing more efficiently the betweenness centrality measure. The
paper introduces the concept of betweenness centrality, and then
describes how betweenness computation can help the interactome net-
work analysis. Current sequential implementations for the between-
ness computation do not perform satisfactory in terms of execution
times. The paper-s main contribution is centered towards introducing
a speedup technique for the betweenness computation, based on
modified shortest path algorithms for sparse graphs. Three optimized
generic algorithms for betweenness computation are described and
implemented, and their performance tested against real biological
data, which is part of the IntAct dataset.
Abstract: The study of proteomics reached unexpected levels of
interest, as a direct consequence of its discovered influence over
some complex biological phenomena, such as problematic diseases
like cancer. This paper presents a new technique that allows for an
accurate analysis of the human interactome network. It is basically
a two-step analysis process that involves, at first, the detection of
each protein-s absolute importance through the betweenness centrality
computation. Then, the second step determines the functionallyrelated
communities of proteins. For this purpose, we use a community
detection technique that is based on the edge betweenness
calculation. The new technique was thoroughly tested on real biological
data and the results prove some interesting properties of those proteins that are involved in the carcinogenesis process. Apart from its
experimental usefulness, the novel technique is also computationally
effective in terms of execution times. Based on the analysis- results, some topological features of cancer mutated proteins are presented
and a possible optimization solution for cancer drugs design is suggested.