Promoter‐specific expression of the imprinted IGF2 gene in bovine oocytes and pre‐implantation embryos

2021 ◽  
Author(s):  
Bruna Rodrigues Willhelm ◽  
Elvis Ticiani ◽  
Karine Campagnolo ◽  
Gabriella Borba Oliveira ◽  
Karine Mattos ◽  
...  
Keyword(s):  
Specific Expression ◽  
Igf2 Gene ◽  
Bovine Oocytes

scholarly journals Promoter-Specific Expression of the Imprinted IGF2 Gene in Cattle (Bos taurus)1

2005 ◽  
Vol 73 (6) ◽  
pp. 1275-1281 ◽  
Author(s):  
Carol Curchoe ◽  
Shouquan Zhang ◽  
Yanfang Bin ◽  
Xiquan Zhang ◽  
Lan Yang ◽  
...  
Keyword(s):  
Bos Taurus ◽  
Specific Expression ◽  
Igf2 Gene

Tissue-specific expression patterns of nuclear receptors

2013 ◽  
Author(s):  
AL Bookout ◽  
Y Jeong ◽  
M Downes ◽  
RT Yu ◽  
RM Evans ◽  
...  
Keyword(s):  
Nuclear Receptors ◽  
Expression Patterns ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression

Studies on the Low Developmental Ability of Parthenogenetic Aged Bovine Oocytes

1996 ◽  
Vol 67 (11) ◽  
pp. 991-995
Author(s):  
Hiroshi TAKANO ◽  
Chiaki KOZAI ◽  
Satoru SHIMIZU ◽  
Yoko KATO ◽  
Yukio TSUNODA
Keyword(s):  
Bovine Oocytes

Probing the 14-3-3 Isoform-Specificity Profile of Interactions Stabilized by Fusicoccin A

2020 ◽  
Author(s):  
James Frederich ◽  
Ananya Sengupta ◽  
Josue Liriano ◽  
Ewa A. Bienkiewicz ◽  
Brian G. Miller
Keyword(s):  
Protein Interactions ◽  
Neurological Diseases ◽  
Adapter Proteins ◽  
Protein Protein Interactions ◽  
Specific Expression ◽  
Individual Client ◽  
Isoform Specificity ◽  
Fusicoccin A

Fusicoccin A (FC) is a fungal phytotoxin that stabilizes protein–protein interactions (PPIs) between 14-3-3 adapter proteins and their phosphoprotein interaction partners. In recent years, FC has emerged as an important chemical probe of human 14-3-3 PPIs implicated in cancer and neurological diseases. These previous studies have established the structural requirements for FC-induced stabilization of 14-3-3·client phosphoprotein complexes; however, the effect of different 14-3-3 isoforms on FC activity has not been systematically explored. This is a relevant question for the continued development of FC variants because there are seven distinct isoforms of 14-3-3 in humans. Despite their remarkable sequence and structural similarities, a growing body of experimental evidence supports both tissue-specific expression of 14-3-3 isoforms and isoform-specific functions <i>in vivo</i>. Herein, we report the isoform-specificity profile of FC <i>in vitro</i>using recombinant human 14-3-3 isoforms and a focused library of fluorescein-labeled hexaphosphopeptides mimicking the C-terminal 14-3-3 recognition domains of client phosphoproteins targeted by FC in cell culture. Our results reveal modest isoform preferences for individual client phospholigands and demonstrate that FC differentially stabilizes PPIs involving 14-3-3s. Together, these data provide strong motivation for the development of non-natural FC variants with enhanced selectivity for individual 14-3-3 isoforms.

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