A Quasi-Clique Mining Algorithm for Analysis of the Human Protein-Protein Interaction Network

2017 ◽  
pp. 411-417 ◽  
Author(s):  
Brijesh Kumar Sriwastava ◽  
Subhadip Basu ◽  
Ujjwal Maulik
Keyword(s):  
Protein Interaction ◽  
Protein Interaction Network ◽  
Interaction Network ◽  
Human Protein ◽  
Protein Protein Interaction ◽  
Mining Algorithm ◽  
Protein Protein Interaction Network

scholarly journals Alpha influenza virus infiltration prediction using virus-human protein–protein interaction network

2020 ◽  
Vol 17 (4) ◽  
pp. 3109-3129 ◽  
Author(s):  
Babak Khorsand ◽  
◽  
Abdorreza Savadi ◽  
Javad Zahiri ◽  
Mahmoud Naghibzadeh ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Protein Interaction ◽  
Protein Interaction Network ◽  
Interaction Network ◽  
Human Protein ◽  
Protein Protein Interaction ◽  
Protein Protein Interaction Network

scholarly journals Insight into Bacterial Virulence Mechanisms against Host Immune Response via the Yersinia pestis-Human Protein-Protein Interaction Network

2011 ◽  
Vol 79 (11) ◽  
pp. 4413-4424 ◽  
Author(s):  
Huiying Yang ◽  
Yuehua Ke ◽  
Jian Wang ◽  
Yafang Tan ◽  
Sebenzile K. Myeni ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Protein Interaction ◽  
Protein Interaction Network ◽  
Interaction Network ◽  
Mapk Signaling ◽  
Human Protein ◽  
Content Type ◽  
Protein Protein Interaction ◽  
Human Proteins ◽  
Protein Protein Interaction Network

ABSTRACTAYersinia pestis-human protein interaction network is reported here to improve our understanding of its pathogenesis. Up to 204 interactions between 66Y. pestisbait proteins and 109 human proteins were identified by yeast two-hybrid assay and then combined with 23 previously published interactions to construct a protein-protein interaction network. Topological analysis of the interaction network revealed that human proteins targeted byY. pestiswere significantly enriched in the proteins that are central in the human protein-protein interaction network. Analysis of this network showed that signaling pathways important for host immune responses were preferentially targeted byY. pestis, including the pathways involved in focal adhesion, regulation of cytoskeleton, leukocyte transendoepithelial migration, and Toll-like receptor (TLR) and mitogen-activated protein kinase (MAPK) signaling. Cellular pathways targeted byY. pestisare highly relevant to its pathogenesis. Interactions with host proteins involved in focal adhesion and cytoskeketon regulation pathways could account for resistance ofY. pestisto phagocytosis. Interference with TLR and MAPK signaling pathways byY. pestisreflects common characteristics of pathogen-host interaction that bacterial pathogens have evolved to evade host innate immune response by interacting with proteins in those signaling pathways. Interestingly, a large portion of human proteins interacting withY. pestis(16/109) also interacted with viral proteins (Epstein-Barr virus [EBV] and hepatitis C virus [HCV]), suggesting that viral and bacterial pathogens attack common cellular functions to facilitate infections. In addition, we identified vasodilator-stimulated phosphoprotein (VASP) as a novel interaction partner of YpkA and showed that YpkA could inhibitin vitroactin assembly mediated by VASP.

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