Decoding the Signals of Membrane Protein Sequences

1994 ◽  
pp. 27-40 ◽  
Author(s):  
Gunnar von Heijne
Virology ◽  
2001 ◽  
Vol 290 (1) ◽  
pp. 74-82 ◽  
Author(s):  
Kanakatte Raviprakash ◽  
Ernesto Marques ◽  
Dan Ewing ◽  
Yang Lu ◽  
Irving Phillips ◽  
...  

Author(s):  
Pranav Dutt Upadhayay ◽  
Rupaansh Chandra Agarwal ◽  
Ranjeet Kumar Rout ◽  
Arun Prakash Agrawal

2012 ◽  
Vol 13 (6) ◽  
pp. 160 ◽  
Author(s):  
Tilman Flock ◽  
AJ Venkatakrishnan ◽  
KR Vinothkumar ◽  
M Madan Babu

2020 ◽  
Vol 82 ◽  
pp. 104320 ◽  
Author(s):  
Manojit Bhattacharya ◽  
Ashish Ranjan Sharma ◽  
Garima Sharma ◽  
Prasanta Patra ◽  
Niladri Mondal ◽  
...  

Author(s):  
Glenda Anak Kaya ◽  
Nor Ashikin Mohamad Kamal

<span lang="EN-US">As the number of protein sequences in the database is increasing, effective and efficient techniques are needed to make these data meaningful.  These protein sequences contain redundant and irrelevant features that cause lower classification accuracy and increase the running time of the computational algorithm. In this paper, we select the best features using Minimum Redundancy Maximum Relevance(mRMR) and Correlation-based feature selection(CFS) methods. Two datasets of human membrane protein are used, S1 and S2.  After the features have been selected by mRMR and CFS, K-Nearest Neighbor(KNN) and Support Vector Machine(SVM) classifiers are used to classify these membrane proteins. The performance of these techniques is measured using accuracy, specificity and sensitivity. and F-measure. The proposed algorithm managed to achieve 76% accuracy for S1 and 73% accuracy for S2. Finally, our proposed methods present competitive results when compared with the previous works on membrane protein classification</span><span>.</span>


PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e57731 ◽  
Author(s):  
Marcus Stamm ◽  
René Staritzbichler ◽  
Kamil Khafizov ◽  
Lucy R. Forrest

2019 ◽  
Vol 476 (21) ◽  
pp. 3241-3260
Author(s):  
Sindhu Wisesa ◽  
Yasunori Yamamoto ◽  
Toshiaki Sakisaka

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.


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