Results 211 to 220 of about 34,862 (253)
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Ribonuclease revisited: structural insights into ribonuclease III family enzymes
Current Opinion in Structural Biology, 2007Ribonuclease III (RNase III) enzymes occur ubiquitously in biology and are responsible for processing RNA precursors into functional RNAs that participate in protein synthesis, RNA interference and a range of other cellular activities. Members of the RNase III enzyme family, including Escherichia coli RNase III, Rnt1, Dicer and Drosha, share the ...
Jennifer Doudna, Ian Macrae
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Ribonuclease III: new sense from nuisance
International Journal of Biochemistry and Cell Biology, 2002RNases play an important role in the processing of precursor RNAs, creating the mature, functional RNAs. The ribonuclease III family currently is one of the most interesting families of endoribonucleases. Surprisingly, RNase III is involved in the maturation of almost every class of prokaryotic and eukaryotic RNA.
Christian, Conrad, Reinhard, Rauhut
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Mutational analysis of a ribonuclease III processing signal
Biochemistry, 1993A mutational approach was employed to identify sequence and structural elements in a ribonuclease III processing signal that are important for in vitro enzymatic cleavage reactivity and selectivity. The substrate analyzed was the bacteriophage T7 R1.1 processing signal, a 60 nucleotide irregular RNA hairpin exhibiting an upper and lower dsRNA stem ...
Allen W Nicholson
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Structural basis for non-catalytic and catalytic activities of ribonuclease III
Acta Crystallographica Section D: Biological Crystallography, 2006Ribonuclease III (RNase III) represents a highly conserved family of double-stranded (ds) RNA-specific endoribonucleases, exemplified by bacterial RNase III and eukaryotic Rnt1p, Drosha and Dicer. Bacterial RNase III, containing an endonuclease domain followed by a dsRNA-binding domain, is the most extensively studied member of the family.
Xinhua Ji, Ji X
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Specificity of cleavage by ribonuclease III
Biochemical and Biophysical Research Communications, 1976Abstract The specificity of RNase III for various synthetic homopolymeric doublestranded RNA substrates have been examined. Although RNase III appears to cleave all homopolymeric RNA duplex structures, with Poly (U)·Poly (A) as the substrate, the enzyme cleaves the Poly (U) strand much faster than it cleaves the Poly (A) strand.
S, Bishayee, U, Maitra
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Review: Non-canonical role of Drosha ribonuclease III
International Journal of Biological Macromolecules, 2023The typical function of Drosha is participating in cleaving pri-miRNA, the initial step of miRNA biogenesis, in the nucleus. Since Drosha has a double-stranded RNA-binding domain and two RNase III domains, when it binds and/or cleaves other RNA species other than pri-miRNA, Drosha is able to induce a variety of novel biological effects.
Xuanshuo, Wei +3 more
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Characterization of ribonuclease III from Brucella
Gene, 2016Bacterial ribonuclease III (RNase III) is a highly conserved endonuclease, which plays pivotal roles in RNA maturation and decay pathways by cleaving double-stranded structure of RNAs. Here we cloned rncS gene from the genomic DNA of Brucella melitensis, and analyzed the cleavage properties of RNase III from Brucella.
Chang-Xian, Wu +7 more
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III. THE RIBONUCLEASES OF HUMAN EPIDERMIS
British Journal of Dermatology, 1977Sodium acetate and sulphuric acid extracts of human epidermis can each be separated by chromatographic techniques into three or more fractions with ribonuclease activity. Eight of these fractions were compared with respect to molecular weight, pH activity profile, polyribonucleotide hydrolysis, and activity in the presence of low levels of spermidine ...
SUSANNE W. MELBYE +2 more
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