نتایج جستجو برای: catalytic

تعداد نتایج: 79040  

Journal: :Journal of Synthetic Organic Chemistry, Japan 1990

Journal: :Gold Bulletin 1983

Journal: :The Analyst 2015
Ya Wang Junying Zhang Linling Zhu Linlin Lu Chongchong Feng Fengyang Wang Zhiai Xu Wen Zhang

Based on melamine binding-triggered triplex formation and subsequent activation of Mg(2+)-dependent DNAzymes, a novel strategy for DNAzyme regulation was proposed and developed for melamine recognition.

Journal: :Chemical communications 2016
Anthony R Hesser Benjamin M Brandsen Shannon M Walsh Puzhou Wang Scott K Silverman

We report the identification by in vitro selection of Zn(2+)/Mn(2+)-dependent deoxyribozymes that glycosylate the 3'-OH of a DNA oligonucleotide. Both β and α anomers of aryl glycosides can be used as the glycosyl donors. Individual deoxyribozymes are each specific for a particular donor anomer.

Journal: :Science 1993
D P Bartel J W Szostak

An iterative in vitro selection procedure was used to isolate a new class of catalytic RNAs (ribozymes) from a large pool of random-sequence RNA molecules. These ribozymes ligate two RNA molecules that are aligned on a template by catalyzing the attack of a 3'-hydroxyl on an adjacent 5'-triphosphate--a reaction similar to that employed by the familiar protein enzymes that synthesize RNA. The co...

2013
Maria Anokhina Sergey Bessonov Zhichao Miao Eric Westhof Klaus Hartmuth Reinhard Lührmann

2000
Pamela A. Pavco Craig M. Flory Brown Tom J. Parry Denis J. Schrier Stephen W. Hunt Thale C. Jarvis Karyn S. Bouhana Mark E. Lesch Suzy A. Brown Craig M. Flory

Journal: :Science 2001
J Liphardt B Onoa S B Smith I Tinoco C Bustamante

Here we use mechanical force to induce the unfolding and refolding of single RNA molecules: a simple RNA hairpin, a molecule containing a three-helix junction, and the P5abc domain of the Tetrahymena thermophila ribozyme. All three molecules (P5abc only in the absence of Mg2+) can be mechanically unfolded at equilibrium, and when kept at constant force within a critical force range, are bi-stab...

Journal: :Current Biology 1998
Jennifer A Doudna

A new crystal structure of a modified hammerhead ribozyme reveals an intermediate conformation that may explain discrepancies between previous structures and the required orientation of the labile bond in the ribozyme's active site.

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