SFRS17B inhibitors are a class of chemical compounds that specifically target and inhibit the activity of the SFRS17B protein, a member of the serine/arginine-rich splicing factor family. These proteins play a crucial role in the regulation of alternative splicing, a process by which precursor messenger RNA (pre-mRNA) is differentially spliced to generate multiple mRNA variants from a single gene. SFRS17B is known for its involvement in recognizing specific splice sites and influencing spliceosome assembly, thereby controlling the production of various protein isoforms. By inhibiting SFRS17B, these compounds can disrupt its regulatory functions in splicing, leading to changes in the splicing patterns of target genes. This modulation can result in alterations to gene expression, impacting cellular processes that rely on specific protein isoforms.
The structural design of SFRS17B inhibitors typically involves a deep understanding of the RNA-binding domains and the splicing-regulatory motifs of the SFRS17B protein. These inhibitors often bind to critical regions of the protein, such as its RNA recognition motifs (RRMs) or arginine/serine-rich (RS) domains, which are responsible for interacting with RNA and other splicing factors. The specificity of these inhibitors for SFRS17B is important to avoid unintended effects on other members of the serine/arginine-rich family, which share similar structural features. Researchers design these compounds to selectively interact with SFRS17B's unique domains, thereby preventing its normal function in the splicing machinery. SFRS17B inhibitors provide valuable tools for studying the mechanisms of alternative splicing regulation, enabling a deeper understanding of how splicing factors control gene expression and contribute to the complexity of cellular function.
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