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2017 ; 18
(5
): ä Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
PCVMZM: Using the Probabilistic Classification Vector Machines Model Combined
with a Zernike Moments Descriptor to Predict Protein-Protein Interactions from
Protein Sequences
#MMPMID28492483
Wang Y
; You Z
; Li X
; Chen X
; Jiang T
; Zhang J
Int J Mol Sci
2017[May]; 18
(5
): ä PMID28492483
show ga
Protein-protein interactions (PPIs) are essential for most living organisms'
process. Thus, detecting PPIs is extremely important to understand the molecular
mechanisms of biological systems. Although many PPIs data have been generated by
high-throughput technologies for a variety of organisms, the whole interatom is
still far from complete. In addition, the high-throughput technologies for
detecting PPIs has some unavoidable defects, including time consumption, high
cost, and high error rate. In recent years, with the development of machine
learning, computational methods have been broadly used to predict PPIs, and can
achieve good prediction rate. In this paper, we present here PCVMZM, a
computational method based on a Probabilistic Classification Vector Machines
(PCVM) model and Zernike moments (ZM) descriptor for predicting the PPIs from
protein amino acids sequences. Specifically, a Zernike moments (ZM) descriptor is
used to extract protein evolutionary information from Position-Specific Scoring
Matrix (PSSM) generated by Position-Specific Iterated Basic Local Alignment
Search Tool (PSI-BLAST). Then, PCVM classifier is used to infer the interactions
among protein. When performed on PPIs datasets of Yeast and H. Pylori, the
proposed method can achieve the average prediction accuracy of 94.48% and 91.25%,
respectively. In order to further evaluate the performance of the proposed
method, the state-of-the-art support vector machines (SVM) classifier is used and
compares with the PCVM model. Experimental results on the Yeast dataset show that
the performance of PCVM classifier is better than that of SVM classifier. The
experimental results indicate that our proposed method is robust, powerful and
feasible, which can be used as a helpful tool for proteomics research.