Jianhua Jia

Dr. Jianhua Jia


Research Focus & Metrics

Academic Career Length

11Years (2016-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 April 2016 in Journal of Theoretical Biology
Verified
Journal Article
Closed access
JJJianhua Jia
Jianhua Jia
ZLZi Liu
Zi Liu
XXXuan Xiao
Xuan Xiao
BLBingxiang Liu
Bingxiang Liu
KCKuo-Chen Chou
Kuo-Chen Chou

26 June 2016 in Bioinformatics
Verified
Journal Article
Open access
PDF file
JJJianhua Jia
Jianhua Jia
LZLiuxia Zhang
Liuxia Zhang
ZLZi Liu
Zi Liu
XXXuan Xiao
Xuan Xiao
KCKuo-Chen Chou
Kuo-Chen Chou
Motivation: Sumoylation is a posttranslational modification (PTM) process, in which small ubiquitin-related modifier (SUMO) is attaching by covalent bonds to substrate protein. It is critical to many different biological processes such as replicating genome, expressing gene, localizing and stabilizing proteins; unfortunately, it is also involved with many major disorders including Alzheimer’s and Parkinson’s diseases. Therefore, for both basic research and drug development, it is important to identify the sumoylation sites in proteins.

3 May 2016 in Oncotarget
Verified
Journal Article
Open access
PDF file
JJJianhua Jia
Jianhua Jia
ZLZi Liu
Zi Liu
XXXuan Xiao
Xuan Xiao
BLBingxiang Liu
Bingxiang Liu
KCKuo-Chen Chou
Kuo-Chen Chou
ICar-PseCp: identify carbonylation sites in proteins by Monto Carlo sampling and incorporating sequence coupled effects into general PseAAC

19 January 2016 in Molecules
Verified
Journal Article
Open access
PDF file
JJJianhua Jia
Jianhua Jia
ZLZi Liu
Zi Liu
XXXuan Xiao
Xuan Xiao
BLBingxiang Liu
Bingxiang Liu
KCKuo-Chen Chou
Kuo-Chen Chou
Knowledge of protein-protein interactions and their binding sites is indispensable for in-depth understanding of the networks in living cells. With the avalanche of protein sequences generated in the postgenomic age, it is critical to develop computational methods for identifying in a timely fashion the protein-protein binding sites (PPBSs) based on the sequence information alone because the information obtained by this way can be used for both biomedical research and drug development. To address such a challenge, we have proposed a new predictor, called iPPBS-Opt, in which we have used: (1) the K-Nearest Neighbors Cleaning (KNNC) and Inserting Hypothetical Training Samples (IHTS) treatments to optimize the training dataset; (2) the ensemble voting approach to select the most relevant features; and (3) the stationary wavelet transform to formulate the statistical samples. Cross-validation tests by targeting the experiment-confirmed results have demonstrated that the new predictor is very promising, implying that the aforementioned practices are indeed very effective. Particularly, the approach of using the wavelets to express protein/peptide sequences might be the key in grasping the problem’s essence, fully consistent with the findings that many important biological functions of proteins can be elucidated with their low-frequency internal motions. To maximize the convenience of most experimental scientists, we have provided a step-by-step guide on how to use the predictor’s web server (http://www.jci-bioinfo.cn/iPPBS-Opt) to get the desired results without the need to go through the complicated mathematical equations involved.

1 January 2019 in Journal of Theoretical Biology
Verified
Journal Article
Closed access
JJJianhua Jia
Jianhua Jia
XLXiaoyan Li
Xiaoyan Li
WQWangren Qiu
Wangren Qiu
XXXuan Xiao
Xuan Xiao
KCKuo-Chen Chou
Kuo-Chen Chou