Kinase Identification with Supervised Laplacian Regularized Least Squares.

Phosphorylation is catalyzed by protein kinases and is irreplaceable in regulating biological processes. Identification of phosphorylation sites with their corresponding kinases contributes to the understanding of molecular mechanisms. Mass spectrometry analysis of phosphor-proteomes generates a lar...

Full description

Bibliographic Details
Main Authors: Ao Li, Xiaoyi Xu, He Zhang, Minghui Wang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4598036?pdf=render
id doaj-34459e0ffa6c47e79d782f5bfa62db86
record_format Article
spelling doaj-34459e0ffa6c47e79d782f5bfa62db862020-11-25T01:50:35ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-011010e013967610.1371/journal.pone.0139676Kinase Identification with Supervised Laplacian Regularized Least Squares.Ao LiXiaoyi XuHe ZhangMinghui WangPhosphorylation is catalyzed by protein kinases and is irreplaceable in regulating biological processes. Identification of phosphorylation sites with their corresponding kinases contributes to the understanding of molecular mechanisms. Mass spectrometry analysis of phosphor-proteomes generates a large number of phosphorylated sites. However, experimental methods are costly and time-consuming, and most phosphorylation sites determined by experimental methods lack kinase information. Therefore, computational methods are urgently needed to address the kinase identification problem. To this end, we propose a new kernel-based machine learning method called Supervised Laplacian Regularized Least Squares (SLapRLS), which adopts a new method to construct kernels based on the similarity matrix and minimizes both structure risk and overall inconsistency between labels and similarities. The results predicted using both Phospho.ELM and an additional independent test dataset indicate that SLapRLS can more effectively identify kinases compared to other existing algorithms.http://europepmc.org/articles/PMC4598036?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Ao Li
Xiaoyi Xu
He Zhang
Minghui Wang
spellingShingle Ao Li
Xiaoyi Xu
He Zhang
Minghui Wang
Kinase Identification with Supervised Laplacian Regularized Least Squares.
PLoS ONE
author_facet Ao Li
Xiaoyi Xu
He Zhang
Minghui Wang
author_sort Ao Li
title Kinase Identification with Supervised Laplacian Regularized Least Squares.
title_short Kinase Identification with Supervised Laplacian Regularized Least Squares.
title_full Kinase Identification with Supervised Laplacian Regularized Least Squares.
title_fullStr Kinase Identification with Supervised Laplacian Regularized Least Squares.
title_full_unstemmed Kinase Identification with Supervised Laplacian Regularized Least Squares.
title_sort kinase identification with supervised laplacian regularized least squares.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2015-01-01
description Phosphorylation is catalyzed by protein kinases and is irreplaceable in regulating biological processes. Identification of phosphorylation sites with their corresponding kinases contributes to the understanding of molecular mechanisms. Mass spectrometry analysis of phosphor-proteomes generates a large number of phosphorylated sites. However, experimental methods are costly and time-consuming, and most phosphorylation sites determined by experimental methods lack kinase information. Therefore, computational methods are urgently needed to address the kinase identification problem. To this end, we propose a new kernel-based machine learning method called Supervised Laplacian Regularized Least Squares (SLapRLS), which adopts a new method to construct kernels based on the similarity matrix and minimizes both structure risk and overall inconsistency between labels and similarities. The results predicted using both Phospho.ELM and an additional independent test dataset indicate that SLapRLS can more effectively identify kinases compared to other existing algorithms.
url http://europepmc.org/articles/PMC4598036?pdf=render
work_keys_str_mv AT aoli kinaseidentificationwithsupervisedlaplacianregularizedleastsquares
AT xiaoyixu kinaseidentificationwithsupervisedlaplacianregularizedleastsquares
AT hezhang kinaseidentificationwithsupervisedlaplacianregularizedleastsquares
AT minghuiwang kinaseidentificationwithsupervisedlaplacianregularizedleastsquares
_version_ 1725001005846757376