scholarly journals A novel approach for the identification of protein-protein interaction with integral membrane proteins

2001 ◽  
Vol 29 (4) ◽  
pp. 18e-18 ◽  
Author(s):  
M. Hubsman
Author(s):  
F N Gilmiyarova ◽  
N A Kolotyeva ◽  
V I Kuzmicheva ◽  
V V Remizov ◽  
O A Gusyakova

2019 ◽  
Author(s):  
Fen Yu ◽  
Zheng Zhang ◽  
Yuanqiang Zou ◽  
Ye Qiu ◽  
Aiping Wu ◽  
...  

AbstractMotivationReceptors on host cells play a critical role in viral infection. How phages select receptors is still unknown.ResultsHere, we manually curated a high-quality database named phageReceptor, including 355 pairs of phage-host receptor interactions, 280 unique viral species or sub-species and 64 bacterial species. Sugars and proteins were most widely used by phages as receptors. The receptor usage of phages in Gram-positive bacteria was different from that in Gram-negative bacteria. Most protein receptors were located on the outer membrane. The protein receptors were highly diverse in their structures, and had little homology with mammalian virus receptors. Further functional characterization of phage protein receptors in Escherichia coli showed that they had larger node degrees and betweennesses in the protein-protein interaction (PPI) network, and higher expression levels, than other outer membrane proteins, plasma membrane proteins, or other intracellular proteins. These findings were consistent with what observed for mammalian virus receptors, suggesting that viral protein receptors play a central role in the host’s PPI network. The study deepens our understanding of virus-host interactions.AvailabilityThe database of phageReceptor is publicly accessible at http://www.computationalbiology.cn/viralRecepetor/index.html.


PROTEOMICS ◽  
2011 ◽  
Vol 11 (10) ◽  
pp. 2124-2128 ◽  
Author(s):  
Volker S. Müller ◽  
Peter R. Jungblut ◽  
Thomas F. Meyer ◽  
Sabine Hunke

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Meijing Li ◽  
Tsendsuren Munkhdalai ◽  
Xiuming Yu ◽  
Keun Ho Ryu

Many researchers focus on developing protein-named entity recognition (Protein-NER) or PPI extraction systems. However, the studies about these two topics cannot be merged well; then existing PPI extraction systems’ Protein-NER still needs to improve. In this paper, we developed the protein-protein interaction extraction system named PPIMiner based on Support Vector Machine (SVM) and parsing tree. PPIMiner consists of three main models: natural language processing (NLP) model, Protein-NER model, and PPI discovery model. The Protein-NER model, which is named ProNER, identifies the protein names based on two methods: dictionary-based method and machine learning-based method. ProNER is capable of identifying more proteins than dictionary-based Protein-NER model in other existing systems. The final discovered PPIs extracted via PPI discovery model are represented in detail because we showed the protein interaction types and the occurrence frequency through two different methods. In the experiments, the result shows that the performances achieved by our ProNER and PPI discovery model are better than other existing tools. PPIMiner applied this protein-named entity recognition approach and parsing tree based PPI extraction method to improve the performance of PPI extraction. We also provide an easy-to-use interface to access PPIs database and an online system for PPIs extraction and Protein-NER.


Author(s):  
D.J. Benefiel ◽  
R.S. Weinstein

Intramembrane particles (IMP or MAP) are components of most biomembranes. They are visualized by freeze-fracture electron microscopy, and they probably represent replicas of integral membrane proteins. The presence of MAP in biomembranes has been extensively investigated but their detailed ultrastructure has been largely ignored. In this study, we have attempted to lay groundwork for a systematic evaluation of MAP ultrastructure. Using mathematical modeling methods, we have simulated the electron optical appearances of idealized globular proteins as they might be expected to appear in replicas under defined conditions. By comparing these images with the apearances of MAPs in replicas, we have attempted to evaluate dimensional and shape distortions that may be introduced by the freeze-fracture technique and further to deduce the actual shapes of integral membrane proteins from their freezefracture images.


Sign in / Sign up

Export Citation Format

Share Document