Characterizing the Functional Similarity of Enzymes with High Co-Citation in Interaction Networks

2013 ◽  
Vol 20 (10) ◽  
pp. 1181-1187 ◽  
Author(s):  
Lilla Tothmeresz ◽  
Vince Grolmusz
2020 ◽  
Author(s):  
Bihai Zhao ◽  
Zhihong Zhang ◽  
Meiping Jiang ◽  
Sai Hu ◽  
Yingchun Luo ◽  
...  

Abstract Background: The accurate annotation of protein functions is of great significance in elucidating the phenomena of life, disease treatment and new drug development. Various methods have been developed to facilitate the prediction of functions by combining protein interaction networks (PINs) with multi-omics data. However, how to make full use of multiple biological data to improve the performance of functions annotation is still a dilemma. Results We presented NPF (Network Propagation for Functions prediction), an integrative protein function predicting framework assisted by network propagation and functional module detection, for discovering interacting partners with similar functions to target proteins. NPF leverages knowledge of the protein interaction network architecture and multi-omics data, such as domain annotation and protein complex information, to augment protein-protein functional similarity in a propagation manner. We have verified the great potential of NPF for accurately inferring protein functions. Comprehensive evaluation of NPF indicates that NPF archived higher performance than competing methods in terms of leave-one-out cross-validation and ten-fold cross validation. Conclusions: We demonstrated that network propagation combined with multi-omics data can not only discover more partners with similar function, but also effectively free from the constraints of the "small-world" feature of protein interaction networks. We conclude that the performance of function prediction depends greatly on whether we can extract and exploit proper functional similarity information from protein correlations.


2020 ◽  
Author(s):  
bihai zhao ◽  
Zhihong Zhang ◽  
Meiping Jiang ◽  
Sai Hu ◽  
Yingchun Luo ◽  
...  

Abstract Background: The accurate annotation of protein functions is of great significance in elucidating the phenomena of life, disease treatment and new drug development. Various methods have been developed to facilitate the prediction of functions by combining protein interaction networks (PINs) with multi-omics data. However, how to make full use of multiple biological data to improve the performance of functions annotation is still a dilemma.Results: We presented NPF (Network Propagation for Functions prediction), an integrative protein function predicting framework assisted by network propagation and functional module detection, for discovering interacting partners with similar functions to target proteins. NPF leverages knowledge of the protein interaction network architecture and multi-omics data, such as domain annotation and protein complex information, to augment protein-protein functional similarity in a propagation manner. We have verified the great potential of NPF for accurately inferring protein functions. Comprehensive evaluation of NPF indicates that NPF archived higher performance than competing methods in terms of leave-one-out cross-validation and ten-fold cross validation.Conclusions: We demonstrated that network propagation combined with multi-omics data can not only discover more partners with similar function, but also effectively free from the constraints of the "small-world" feature of protein interaction networks. We conclude that the performance of function prediction depends greatly on whether we can extract and exploit proper functional similarity information from protein correlations.


2017 ◽  
Vol 18 (S16) ◽  
Author(s):  
Zhen Tian ◽  
Maozu Guo ◽  
Chunyu Wang ◽  
Xiaoyan Liu ◽  
Shiming Wang

1979 ◽  
Author(s):  
C Cierniewski ◽  
T Krajewski ◽  
E Janiak

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.


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