(Altman, 1995; Guerrier-Takadaet al., 1997; Liu and Altman, 1995). The guide sequence base-pairs with the target RNA and provides a pseudo-substrate for the endogenous enzyme. While the original demonstrations of thisribozymeapproach employed the well-characterized bacterial RNase P, more recent...
synthesis of a labeled antisense RNA probe complementary to a several-hundred-base region of the target mRNA, isolation of RNA sample(s) to be examined for target expression, hybridization of the labeled probe to a total RNA sample, treatment of the sample ...
Functional genomics and target validation approaches using antisense oligonucleotide technology H is a class ofthat degrades thestrand of an RNA–DNA duplex, producing a 5′-phosphate and 3′-hydroxy terminus. The resulting cleavage products lack a 5′-cap and 3′-polyadenylation tail, respectively...
of the RNA base after primer hybridization to the target DNA. Because the primers can only be cleaved after they hybridize to the perfectly matched target sequence, primer-dimers are reduced. The requirement for high target complementarity reduces amplification of closely related sequences (Figure 1...
Mtb-RNase J exhibits β-lactamase and exonuclease activity, making it a potential target for clinical drug development (Fig. 1). Structural superimposition of Mtb-RNase J with S. coelicolor RNase J (PDB ID: 5A0T), S. epidermidis RNase J1 (PDB ID: 6K6S), and RNase J2 (PDB ID: 6K6W...
Target information above from: UniProt accession Q5TBB1 The UniProt ConsortiumThe Universal Protein Resource (UniProt) in 2010 Nucleic Acids Res. 38:D142-D148 (2010) . Information by UniProt Database links Entrez Gene: 79621 Human Omim: 610326 Human SwissProt: Q5TBB1 Human Unigene: 306291 Hum...
DNA primers containing a single RNA residue and a 3′ blocking moiety (rhPrimers) are activated when cleaved by RNase H2 enzyme. Cleavage occurs on the 5′ side of the RNA base after primer hybridization to the target DNA. Because the primers can only be cleaved after they hybridize to ...
Retroviral RNase H, a part of the viral reverse transcriptase enzyme, is an important pharmaceutical target, as it is absolutely necessary for the proliferation of retroviruses, such as HIV and murine leukemia virus[7][8]. Inhibitors of this enzyme could therefore provide new drugs against disease...
Briefly, 50 ng genomic DNA was used as an amplification target with 1 unit of Platinum Taq polymerase under standard conditions. Genomic DNAs, Taq proofreading polymerase, and gene-specific primers RN8F and RN8R primers were used to amplify a 688 bp genomic fragment encompassing the RNase ...
activated during UPR, inositol-requiring enzyme 1α (IRE1). The rationale is that the IRE1 pathway is associated with cell fate decisions and recognized as a promising target for cancer therapeutics. Here we discuss IRE1 inhibitors and how they might prove to be an effective cancer therapeutic...