Results 171 to 180 of about 3,495 (190)

A microsomal exoribonuclease from rat liver

Biochimica et Biophysica Acta (BBA) - Enzymology, 1979
A exoribonuclease has been purified from the microsomes of rat liver. The enzyme had an apparent molecular weight of 80 000-83 000 and produced, via a processive mechanism, 5'-AMP as the only product from poly(A). The degradation was found to proceed in the 3' to 5' direction.
H, Kumagai, K, Igarashi, K, Tanaka, H, Nakao, S, Hirose   +4 more
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RNA exoribonucleases in E. coli

Archives of Microbiology
Ribonucleases are associated with processing and degradation of diverse RNA substrates. These enzymes act on the substrate with high specificity, often in association with their interacting partners. Functionally redundant exoribonucleases are indispensable for maintaining the physiological homeostasis under normal and challenging conditions for growth.
Ashaq, Hussain, Malay, Kumar Ray
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An exoribonuclease in bovine brain

Brain Research, 1975
An exonuclease which degrades RNA to yield 3′-mononucleotides has been purified 300-fold from an acetone powder of bovine brain white matter. The enzyme preparation does not contain detectable quantities of RNase A, DNase, 2′,3′-cyclic phosphodiesterase, 5′-nucleotidase, and acid and alkaline phosphatase activities and requires sulfhydryl compounds for
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5′-Exoribonuclease 1: Xrn1

2001
Publisher Summary The detection, purification, and partial characterization of 5′-exoribonuclease 1 (Xrn1) from Saccharomyces cerevisiae as a 160-kDa RNase was reported in 1980 and 1985. The enzyme is a processive exonuclease hydrolyzing RNA from the 5′ end with the production of 5′-mononucleofides.
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A cytoplasmic exoribonuclease from HeLa cells

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1977
An exoribonuclease has been purified from the cytoplasm of HeLa cells. The enzyme produces 5'-AMP as the only product from poly(A). The degradation proceeds in a 3' to 5' direction, and a 3'-OH terminus is required. In addition to poly(A), the enzyme degrades other synthetic homopolymers as well as natural messenger, and ribosomal RNAs.
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Cooperation of Endo- and Exoribonucleases in Chloroplast mRNA Turnover

2004
Chloroplasts were acquired by eukaryotic cells through endosymbiosis and have retained their own gene expression machinery. One hallmark of chloroplast gene regulation is the predominance of posttranscriptional control, which is exerted both at the gene-specific and global levels.
Thomas J, Bollenbach, Gadi, Schuster, David B, Stern   +2 more
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Function and Characterization of Poly(A)-Specific 3´ Exoribonucleases

1997
Poly(A) tails are commonly found at the 3´ end of various classes of RNA (reviewed in Brawerman 1981; Manley 1995b). They are evolutionarily widespread and appear on RNAs of several different organisms. In mammalian cells almost all mRNAs end with an approximately 200-adenosine-residue-long poly(A) tail.
A, Virtanen, J, Aström
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Studying Exoribonuclease Activity Using Fluorescence Anisotropy Assay

Fluorescence anisotropy is a powerful technique, widely used for investigating ligand-macromolecule binding and high-throughput screens for drugs. Here, we employ fluorescence anisotropy to quantitatively study the activity of exoribonucleases exemplified by the Xrn2 enzyme.
Krzysztof, Kuś, Lidia, Vasiljeva
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Exoribonuclease II

1991
Dietmar Schomburg, Margit Salzmann
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Exoribonuclease H

1991
Dietmar Schomburg, Margit Salzmann
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