Sentences with word «ribonuclease»

Analysis of crosslinked complexes of M1 RNA, the catalytic RNA subunit of ribonuclease P from Escherichia coli, and transfer RNA precursor substrates has led to the identification of regions in the enzyme and in the substrate that are in close physical proximity to each other.

The RNA moiety M1 RNA of ribonuclease P from Escherichia coli and the unprocessed transcript prepared in vitro of the gene for M1 RNA can both perform the cleavage reactions of the canonical enzyme in the absence of the protein moiety.

A fluorescence - based high - throughput screening assay for inhibitors of human immunodeficiency virus - 1 reverse transcriptase - associated ribonuclease H activity

The most efficient EGSs form transfer RNA precursor - like structures with the target RNA, in which the analog of the anticodon stem has been disrupted, an indication that selection for the optimal substrate for ribonuclease P yields an RNA structure different from that of present - day transfer RNA precursors.

Crystal structures of the reverse transcriptase - associated ribonuclease H domain of xenotropic murine leukemia - virus related virus

Specific ribonuclease activities in spinach chloroplasts promote mRNA maturation and degradation

M1 RNA, the catalytic RNA subunit of Escherichia coli ribonuclease P, can cleave novel transfer RNA (tRNA) precursors that lack specific domains of the normal tRNA sequence.

Working with Samuel Danishefsky, who solved the difficult problem of synthesizing Globo H at the Memorial Sloan - Kettering Cancer Center in New York, Raines found that reducing the Globo H display on the surface made breast cancer cells less vulnerable to ribonucleases like those that Quintessence is testing.

The new understanding could help both approaches, says UW - Madison professor of biochemistry Ronald Raines, who has long studied ribonucleases — enzymes that break apart RNA, a messenger with multiple roles inside the cell.

Using standard techniques, she copied the DNA into RNA, which can be readily cleaved by an enzyme called ribonuclease H.

The picture that emerges from the work is of ribonucleases patrolling our bodies, looking for telltales of cancer cells, Raines says.

Soon thereafter, he found that the engineered ribonuclease was more toxic to cancer cells than to others.

Bernstein et al. «Role for A Bidentate Ribonuclease in the Initiation Step of RNA Interference», Nature, 409: 363 - 366, 2001.

Ribonuclease P (RNase P) from Escherichia coli or its catalytic RNA subunit can efficiently cleave small RNA substrates that lack the conserved features of natural substrates of RNase P if an additional small RNA is also present.

Standard laboratory DNA isolation methods, such as sonication, ribonuclease (RNase) treatment, and ethanol precipitation may reduce the available pool of DNA enough to prevent recovering usable sequences from the oldest samples.

Any RNA, when in a complex with another oligoribonucleotide known as an external guide sequence (EGS), can become a substrate for ribonuclease P. Simulation of evolution in vitro was used to select EGSs that bind tightly to a target substrate messenger RNA and that increase the efficiency of cleavage of the target by human ribonuclease P to a level equal to that achieved with natural substrates.

Monomeric ribonuclease A has very low activity toward typically double - stranded RNA's; the dimeric form of ribonuclease A obtained by cross linking the enzyme by dimethyl suberimidate has more than 78 times the activity of the monomer toward polyadenylate · polyuridylate and 440 times the activity of the monomer toward the double - stranded RNA of a virus from Penicillium chrysogenum.

Ribonuclease P is a ribonucleoprotein that cleaves precursors to transfer RNA (tRNA) molecules to yield the correct 5» terminal sequences of the mature tRNA's.

In 1998, he discovered how to alter one ribonuclease to avoid its deactivation in the body.

They remain shareholders in the firm, which has licensed the patent from WARF and begun early - phase human trials with the ribonuclease at the UW Carbone Cancer Center and MD Anderson Cancer Center in Houston.

The current study began as an effort to figure out why the ribonuclease was selective for cancer cells.

Ribonuclease II preserves chloroplast RNA homeostasis by increasing mRNA decay rates, and cooperates with polynucleotide phosphorylase in 3 «end maturation

Areas of emphasis include the roles of ribonucleases and RNA - binding proteins and assembly of the carbon - fixing enzyme Rubisco.

Germline Mutations in the Ribonuclease L (RNase L) Gene in Hereditary Prostate Cancer 1 (HPC1)- Linked Families.