Results 11 to 20 of about 34,904 (304)

Ribocentre: a database of ribozymes

open access: yesNucleic Acids Research, 2022
Abstract Ribozymes are excellent systems in which to study ‘sequence - structure - function’ relationships in RNA molecules. Understanding these relationships may greatly help structural modeling and design of functional RNA structures and some functional structural modules could be repurposed in molecular design. At present, there is no
Jie Deng   +12 more
openaire   +4 more sources

Ligand‐dependent ribozymes [PDF]

open access: yesWIREs RNA, 2016
The discovery of catalytic RNA (ribozymes) more than 30 years ago significantly widened the horizon of RNA‐based functions in natural systems. Similarly to the activity of protein enzymes that are often modulated by the presence of an interaction partner, some examples of naturally occurring ribozymes are influenced by ligands that can either act as ...
Felletti, Michele, Hartig, Jörg S.
openaire   +4 more sources

Structural and Biochemical Properties of Novel Self-Cleaving Ribozymes

open access: yesMolecules, 2017
Fourteen well-defined ribozyme classes have been identified to date, among which nine are site-specific self-cleaving ribozymes. Very recently, small self-cleaving ribozymes have attracted renewed interest in their structure, biochemistry, and biological
Ki-Young Lee, Bong-Jin Lee
doaj   +2 more sources

Twister ribozymes as highly versatile expression platforms for artificial riboswitches

open access: yesNature Communications, 2016
Twister ribozymes are small endonucleolytic RNA motifs. Here the authors develop twister ribozymes into RNA logic gates and cross-species synthetic genetic regulators.
Michele Felletti   +4 more
doaj   +2 more sources

Classification of the nucleolytic ribozymes based upon catalytic mechanism [version 1; peer review: 3 approved]

open access: yesF1000Research, 2019
The nucleolytic ribozymes carry out site-specific RNA cleavage reactions by nucleophilic attack of the 2′-oxygen atom on the adjacent phosphorus with an acceleration of a million-fold or greater.
David M.J. Lilley
doaj   +2 more sources

How RNA acts as a nuclease:some mechanistic comparisons in the nucleolytic ribozymes [PDF]

open access: yesBiochemical Society Transactions, 2017
Recent structural and mechanistic studies have shed considerable light on the catalytic mechanisms of nucleolytic ribozymes. The discovery of several new ribozymes in this class has now allowed comparisons to be made, and the beginnings of mechanistic ...
Lilley, David M. J.
core   +3 more sources

A Faster Triphosphorylation Ribozyme. [PDF]

open access: yesPLOS ONE, 2015
In support of the RNA world hypothesis, previous studies identified trimetaphosphate (Tmp) as a plausible energy source for RNA world organisms. In one of these studies, catalytic RNAs (ribozymes) that catalyze the triphosphorylation of RNA 5'-hydroxyl ...
Akoopie, Arvin   +2 more
core   +11 more sources

Complete RNA inverse folding: computational design of functional hammerhead ribozymes [PDF]

open access: yesNucleic Acids Research, 2014
Nanotechnology and synthetic biology currently constitute one of the most innovative, interdisciplinary fields of research, poised to radically transform society in the 21st century. This paper concerns the synthetic design of ribonucleic acid molecules,
Clote, Peter   +5 more
core   +2 more sources

Self-cleaving ribozymes: substrate specificity and synthetic biology applications

open access: yesRSC Chemical Biology, 2021
Various self-cleaving ribozymes appearing in nature catalyze the sequence-specific intramolecular cleavage of RNA and can be engineered to catalyze cleavage of appropriate substrates in an intermolecular fashion, thus acting as true catalysts.
Huan Peng   +4 more
semanticscholar   +1 more source

Imaginary Ribozymes.

open access: yesACS Chemical Biology, 2020
Biocatalysis is dominated by protein enzymes, and only a few classes of ribozymes are known to contribute to the task of promoting biochemical transformations.
R. Breaker
semanticscholar   +1 more source

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