Results 201 to 210 of about 8,461 (225)
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The Hairpin Ribozyme

1994
RNA enzymes, or ribozymes, are fascinating molecules with novel biochemical properties. Since the discovery of ribozymes in 1981, biological catalysis by RNA has been found to be at the heart of critical steps in gene expression, including RNA splicing, endonucleolytic RNA processing, and possibly ribosomal peptide bond formation (Sheldon et al.
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Self-association of adenine-dependent hairpin ribozymes

European Biophysics Journal, 2007
Hairpin ribozymes are flexible molecules that catalyse reversible self-cleavage after the docking of two independently folded internal loops, A and B. The activities, self-association and structures in solution of two 85 base adenine-dependent hairpin ribozymes (ADHR1 and ADHR2) were studied by native gel electrophoresis, analytical centrifugation, and
Li, Yan-Li   +5 more
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Kinetics and Thermodynamics of Intermolecular Catalysis by Hairpin Ribozymes

Biochemistry, 1995
The hairpin ribozyme, derived from the negative strand of the satellite RNA of tobacco ringspot virus, belongs to the class of small catalytic RNAs that cleave RNA to generate 2',3'-cyclic phosphate and 5'hydroxyl termini and ligate these termini in the reverse reaction to form 3',5'-phosphodiesters.
Martha J. Fedor, Lisa A. Hegg
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Enhanced Folding of Hairpin Ribozymes with Replaced Domains

Biochemistry, 1996
Reversely joined ribozymes (Komatsu et al., 1995) have been proven to be active. Here we describe the construction of hairpin ribozymes with separated domains, but containing complementary arms for association of the two domains. Linker nucleotides were inserted between the arms and domains. These ribozymes were active under the standard conditions (12
Eiko Ohtsuka   +2 more
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Structural Basis for the Guanosine Requirement of the Hairpin Ribozyme

Biochemistry, 1999
To form a catalytically active complex, the essential nucleotides of the hairpin ribozyme, embedded within the internal loops of the two domains, must interact with one another. Little is known about the nature of these essential interdomain interactions.
Dominic Lambert   +5 more
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Hairpin and hammerhead ribozymes: how different are they?

Biochemical Society Transactions, 2002
Recent experimental work on the hairpin and hammerhead ribozymes suggests that they have more similarities than previously suspected. Notably, each is now known to function as a true RNA catalyst, not requiring metal ions for folding or catalytic function.
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Novel guanosine requirement for catalysis by the hairpin ribozyme

Nature, 1991
THERE is much interest in the development of 'designer ribozymes' to target destruction of RNAs in vitro and in vivo. Engineering of ribozymes with novel specificities requires detailed knowledge of the ribozyme-substrate interaction, and a rigorous evaluation of sequence specificity.
John M. Burke   +2 more
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A Mechanistic Comparison of the Varkud Satellite and Hairpin Ribozymes

2013
The hairpin and Varkud satellite ribozymes are two members of the class of nucleolytic ribozymes that catalyze cleavage and ligation reactions at a specific site. Cleavage occurs by a transesterification reaction whereby the 2'-O attacks the adjacent phosphorus with departure of the 5'-O to leave a 2',3'-cyclic phosphate.
Wilson, Timothy J., Lilley, David M. J.
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Design and Optimization of Sequence-Specific Hairpin Ribozymes

2004
The hairpin ribozyme belongs to a group of small catalytic RNAs that have been extensively used to trans-cleave RNA molecules. Many efforts have been made to elucidate its reaction mechanism, and there is great interest in designing hairpin ribozymes with improved catalytic activity for use in the development of agents that specifically inactivate RNA ...
Alicia Barroso-delJesus   +3 more
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The Hairpin and Varkud Satellite Ribozymes

2007
Nucleolytic ribozymes carry out cleavage at a specific site by transesterification reactions in which the 2′-oxygen attacks the 3′-phosphorus, with departure of the 5′-oxygen to leave a cyclic 2′-3′-phosphate. The reaction follows an SN2 mechanism, with inversion of configuration at the phosphorus.
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