2024 : 11 : 21
Rojiar Pir mohammadiani

Rojiar Pir mohammadiani

Academic rank: Assistant Professor
ORCID:
Education: PhD.
ScopusId: 3216
HIndex:
Faculty: Faculty of Engineering
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Phone:

Research

Title
Spectral clustering on protein-protein interaction networks via constructing affinity matrix using attributed graph embedding
Type
JournalPaper
Keywords
Protein-protein interaction network Protein complexes identification Spectral clustering Graph embedding Affinity matrix
Year
2021
Journal COMPUTERS IN BIOLOGY AND MEDICINE
DOI
Researchers Kamal Berahmand ، Elahe Nasiri ، Rojiar Pir mohammadiani ، yuefeng Li

Abstract

The identification of protein complexes in protein-protein interaction networks is the most fundamental and essential problem for revealing the underlying mechanism of biological processes. However, most existing protein complexes identification methods only consider a network’s topology structures, and in doing so, these methods miss the advantage of using nodes’ feature information. In protein-protein interaction, both topological structure and node features are essential ingredients for protein complexes. The spectral clustering method utilizes the eigenvalues of the affinity matrix of the data to map to a low-dimensional space. It has attracted much attention in recent years as one of the most efficient algorithms in the subcategory of dimensionality reduction. In this paper, a new version of spectral clustering, named text-associated DeepWalk-Spectral Clustering (TADWSC), is proposed for attributed networks in which the identified protein complexes have structural cohesiveness and attribute homogeneity. Since the performance of spectral clustering heavily depends on the effectiveness of the affinity matrix, our proposed method will use the text-associated DeepWalk (TADW) to calculate the embedding vectors of proteins. In the following, the affinity matrix will be computed by utilizing the cosine similarity between the two low dimensional vectors, which will be considerable to improve the accuracy of the affinity matrix. Experimental results show that our method performs unexpectedly well in comparison to existing state-of-the-art methods in both real protein network datasets and synthetic networks.