scholarly journals Protein tyrosine sulfation: A critical posttranslation modification in plants and animals

2009 ◽  
Vol 106 (35) ◽  
pp. 14741-14742 ◽  
Author(s):  
K. L. Moore
2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Song Guo ◽  
Chunhua Liu ◽  
Peng Zhou ◽  
Yanling Li

Tyrosine sulfation is one of the ubiquitous protein posttranslational modifications, where some sulfate groups are added to the tyrosine residues. It plays significant roles in various physiological processes in eukaryotic cells. To explore the molecular mechanism of tyrosine sulfation, one of the prerequisites is to correctly identify possible protein tyrosine sulfation residues. In this paper, a novel method was presented to predict protein tyrosine sulfation residues from primary sequences. By means of informative feature construction and elaborate feature selection and parameter optimization scheme, the proposed predictor achieved promising results and outperformed many other state-of-the-art predictors. Using the optimal features subset, the proposed method achieved mean MCC of 94.41% on the benchmark dataset, and a MCC of 90.09% on the independent dataset. The experimental performance indicated that our new proposed method could be effective in identifying the important protein posttranslational modifications and the feature selection scheme would be powerful in protein functional residues prediction research fields.


1993 ◽  
Vol 2 (2) ◽  
pp. 215-222 ◽  
Author(s):  
Grace L. Rosenquist ◽  
Hugh B. Nicholas

2009 ◽  
Vol 30 (15) ◽  
pp. 2526-2537 ◽  
Author(s):  
Wen-Chi Chang ◽  
Tzong-Yi Lee ◽  
Dray-Ming Shien ◽  
Justin Bo-Kai Hsu ◽  
Jorng-Tzong Horng ◽  
...  

1987 ◽  
Vol 12 ◽  
pp. 361-363 ◽  
Author(s):  
Wieland B. Huttner

2006 ◽  
Vol 20 (5) ◽  
Author(s):  
Andrew D. Westmuckett ◽  
Adam J. Hoffhines ◽  
Kevin L. Moore

2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Takamasa Teramoto ◽  
Yukari Fujikawa ◽  
Yoshirou Kawaguchi ◽  
Katsuhisa Kurogi ◽  
Masayuki Soejima ◽  
...  

1994 ◽  
Vol 92 (1-3) ◽  
pp. 257-271 ◽  
Author(s):  
Christof Niehrs ◽  
Roland Beißwanger ◽  
Wieland B. Huttner

2018 ◽  
Vol 475 (19) ◽  
pp. 3035-3037 ◽  
Author(s):  
Sharon Yeoh ◽  
Richard Bayliss

Sulfation is a common modification of extracelluar glycans and tyrosine residues on proteins, which is important in many signalling pathways and interactions. Existing methods for studying sulfotransferases, the enzymes that catalyse sulfation, are cumbersome and low-throughput. Recent studies published in the Biochemical Journal have repurposed established biochemical assays from the kinase field and applied them to the characterisation of sulfotransferases. Biochemical screening of a library of kinase inhibitors revealed that compounds that target RAF kinases may also be repurposed to inhibit sulfotransferases. Together with the available structures of sulfotransferases, these studies open the door to the development of chemical tools to probe the biological functions of these important enzymes.


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