<p>The 5′-terminus of the ribozyme (green) is in close contact with the primer (red) and template (orange). The P2 oligo (dark blue) is base paired to a complementary region on the ribozyme (light blue), forming the P2 helix. (<b>A</b>) Secondary structure of the polymerase ribozyme <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0025030#pone.0025030-Johnston1" target="_blank">[7]</a> with the 5′-duplexes and the P2 duplex that were used to attach arginine or amino cofactors. The length of the 5′-duplex is indicated. “X” denotes the position of the chemical modification. The P2 oligo is truncated, and the internal mismatch was removed <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0025030#pone.00...
<p>(<b>A</b>) Autoradiogram of PAGE separated polymerization products, with RNA/RNA duplexes at the ...
grantor: University of TorontoThe discovery of catalytic RNAs, or ribozymes, indicated tha...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, February 2003.Includes bib...
At the heart of the “RNA World” hypothesis is the requirement for an RNA polymerase ribozyme capable...
<p><b>Copyright information:</b></p><p>Taken from "The genomic HDV ribozyme utilizes a previously un...
Ribozyme-catalyzed RNA synthesis is central to the RNA world hypothesis. No natural RNA polymerase r...
AbstractBackground: Many new ribozymes, including sequence-specific nucleases, ligases and kinases, ...
ABSTRACT: The complex between the hairpin ribozyme and its substrate consists of two domains that mu...
We determined the x-ray structure of the RNA polymerase (Pol) II subcomplex Rpb4/7 at 2.3 Å resoluti...
Ribozyme (catalytic RNA) evolution by in vitro selection is one of the powerful evolutionary systems...
We determined the X−ray structure of the RNA polymerase II (Pol II) subcomplex Rpb4/7 at 2.3 A resol...
Ribonuclease P (RNase P) is a class of enzymes involved in the processing of precursor tRNAs to remo...
Early life presumably required polymerase ribozymes capable of replicating RNA. Known polymerase rib...
The TS ribozyme (originally called twister-sister) is a nucleolytic catalytic RNA. We present a crys...
<p><b>Copyright information:</b></p><p>Taken from "Searching genomes for ribozymes and riboswitches"...
<p>(<b>A</b>) Autoradiogram of PAGE separated polymerization products, with RNA/RNA duplexes at the ...
grantor: University of TorontoThe discovery of catalytic RNAs, or ribozymes, indicated tha...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, February 2003.Includes bib...
At the heart of the “RNA World” hypothesis is the requirement for an RNA polymerase ribozyme capable...
<p><b>Copyright information:</b></p><p>Taken from "The genomic HDV ribozyme utilizes a previously un...
Ribozyme-catalyzed RNA synthesis is central to the RNA world hypothesis. No natural RNA polymerase r...
AbstractBackground: Many new ribozymes, including sequence-specific nucleases, ligases and kinases, ...
ABSTRACT: The complex between the hairpin ribozyme and its substrate consists of two domains that mu...
We determined the x-ray structure of the RNA polymerase (Pol) II subcomplex Rpb4/7 at 2.3 Å resoluti...
Ribozyme (catalytic RNA) evolution by in vitro selection is one of the powerful evolutionary systems...
We determined the X−ray structure of the RNA polymerase II (Pol II) subcomplex Rpb4/7 at 2.3 A resol...
Ribonuclease P (RNase P) is a class of enzymes involved in the processing of precursor tRNAs to remo...
Early life presumably required polymerase ribozymes capable of replicating RNA. Known polymerase rib...
The TS ribozyme (originally called twister-sister) is a nucleolytic catalytic RNA. We present a crys...
<p><b>Copyright information:</b></p><p>Taken from "Searching genomes for ribozymes and riboswitches"...
<p>(<b>A</b>) Autoradiogram of PAGE separated polymerization products, with RNA/RNA duplexes at the ...
grantor: University of TorontoThe discovery of catalytic RNAs, or ribozymes, indicated tha...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, February 2003.Includes bib...