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Status |
Public on Jul 13, 2017 |
Title |
Splicing activation by Rbfox requires self-aggregation through its tyrosine-rich domain |
Organism |
Homo sapiens |
Experiment type |
Expression profiling by high throughput sequencing
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Summary |
To determine how the higher order assembly of Rbfox proteins affect Rbfox-dependent splicing regulation, we expressed Rbfox wildtype and its mutant protein in Flp-In™ T-REx™ 293 Rbfox2-/- cells and extracted RNA from these cells to perform RASL-seq which profiles thousands of alternative splicing event.
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Overall design |
Flp-In™ T-REx™ 293 Cell Line (in triplicate) were transfected by Rbfox1 wildtype and its mutants, followed by Dox induction. Total RNAs were extracted and been analyzed by RASL-seq.
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Contributor(s) |
Ying Y, Black DL |
Citation(s) |
28708999 |
NIH grant(s) |
Grant ID |
Grant title |
Affiliation |
Name |
R01 GM114463 |
Mechanisms of Alternative Splicing Regulation by Rbfox Proteins |
UNIVERSITY OF CALIFORNIA LOS ANGELES |
Douglas L. Black |
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Submission date |
Nov 07, 2016 |
Last update date |
May 15, 2019 |
Contact name |
Douglas L. Black |
E-mail(s) |
dougb@microbio.ucla.edu
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Organization name |
UCLA
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Department |
MIMG
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Lab |
6-780 MacDonald Research Laboratories
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Street address |
675 Charles E. Young Drive South
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City |
Los Angeles |
State/province |
CA |
ZIP/Postal code |
90095 |
Country |
USA |
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Platforms (1) |
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Samples (12)
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Relations |
BioProject |
PRJNA352682 |
SRA |
SRP092755 |