pr10 protein
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2017 ◽  
Vol 15 (1) ◽  
pp. 42-49 ◽  
Author(s):  
Niloofar Zandvakili ◽  
Mohammadreza Zamani ◽  
Mostafa Motallebi ◽  
Zahra Moghaddassi Jahromi

2013 ◽  
Vol 114 (2) ◽  
pp. 217-223 ◽  
Author(s):  
Jun-Jun Liu ◽  
Abul K. M. Ekramoddoullah ◽  
Barbara Hawkins ◽  
Saleh Shah

2012 ◽  
Vol 32 (6) ◽  
pp. 567-575 ◽  
Author(s):  
Christian Seutter von Loetzen ◽  
Kristian Schweimer ◽  
Wilfried Schwab ◽  
Paul Rösch ◽  
Olivia Hartl-Spiegelhauer

The PR10 family protein Fra a 1E from strawberry (Fragaria x ananassa) is down-regulated in white strawberry mutants, and transient RNAi (RNA interference)-mediated silencing experiments confirmed that Fra a 1 is involved in fruit pigment synthesis. In the present study, we determined the solution structure of Fra a 1E. The protein fold is identical with that of other members of the PR10 protein family and consists of a seven-stranded antiparallel β-sheet, two short V-shaped α-helices and a long C-terminal α-helix that encompass a hydrophobic pocket. Whereas Fra a 1E contains the glycine-rich loop that is highly conserved throughout the protein family, the volume of the hydrophobic pocket and the size of its entrance are much larger than expected. The three-dimensional structure may shed some light on its physiological function and may help to further understand the role of PR10 proteins in plants.


2008 ◽  
Vol 28 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Ashraf El-kereamy ◽  
S. Jayasankar ◽  
Ali Taheri ◽  
Deena Errampalli ◽  
Gopinadhan Paliyath

2004 ◽  
Vol 45 (9) ◽  
pp. 1320-1324 ◽  
Author(s):  
Sanjeeva Srivastava ◽  
Brian Fristensky ◽  
Nat N. V. Kav

2004 ◽  
Vol 45 (5) ◽  
pp. 550-559 ◽  
Author(s):  
Makoto Hashimoto ◽  
Larisa Kisseleva ◽  
Shinichiro Sawa ◽  
Toshiko Furukawa ◽  
Setsuko Komatsu ◽  
...  

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