Selected article for: "ATP dependent helicase domain and helicase domain"

Author: Asiedu Ebenezer
Title: Designing Effective small interfering RNA for Post-Transcriptional Silencing of Human GREM1: A Comprehensive Bioinformatics Approach
  • Document date: 2020_1_24
  • ID: j99qg2a0_6
    Snippet: The processing of dsRNA to siRNAs is done by a complex protein, Dicer, together with double stranded RNA binding proteins [18] . The dicer mediated processing is followed by an integration of the siRNAs to RNA-induced silencing complex (RISC) by RISC-loading complex (RLC). RISC has an ATP-dependent RNA helicase domain that separates the two strands of the siRNA. The strand whose 5' end has the lower free energy of binding, the guide strand, is bo.....
    Document: The processing of dsRNA to siRNAs is done by a complex protein, Dicer, together with double stranded RNA binding proteins [18] . The dicer mediated processing is followed by an integration of the siRNAs to RNA-induced silencing complex (RISC) by RISC-loading complex (RLC). RISC has an ATP-dependent RNA helicase domain that separates the two strands of the siRNA. The strand whose 5' end has the lower free energy of binding, the guide strand, is bound by the RISC whereas its complementary strand, the passenger strand, is cleaved and removed. The active siRNA-RISC (si-RISC) complex recognizes its target mRNA. An RNase III component of RISC known as Argonaute-2 cleaves the mRNA opposite the bound guide strand, thereby preventing its translation.

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