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- Bookedited by Luc Ponchon.Contents:
Method to predict the 3D structure of an RNA scaffold / Xiaojun Xu and Shi-Jie Chen
Post-crystallization improvement of RNA crystal diffraction quality / Jinwei Zhang and Adrian R. Ferré-D'Amaré
Expression and purification of RNA-protein complexes in Escherichia coli / Margueritte El Khouri and others
Production of homogeneous recombinant RNA using a tRNA scaffold and hammerhead ribozymes / Frank H.T. Nelissen, Hans A. Heus, and Sybren S. Wijmenga
In vivo production of small recombinant RNAs embedded in a 5S rRNA-derived protective scaffold / Victor G. Stepanov and George E. Fox
Detection of RNA-protein interactions using tethered RNA affinity capture / Hidekazu Iioka and Ian G. Macara
Universal method for labeling native RNA in live bacterial cells / Irina Smolina and Natalia Broude
Live cell imaging using riboswitch-spinach tRNA fusions as metabolite-sensing fluorescent biosensors / Colleen A. Kellenberger, Zachary F. Hallberg, and Ming C. Hammond
RNA scaffold : designed to co-localize enzymes / ZJU_China Team (iGEM 2012) and Ming Chen
Artificial ligase ribozymes isolated by a "Design and Selection" strategy / Shigeyoshi Matsumura and Yoshiya Ikawa
Engineering aptazyme switches for conditional gene expression in mammalian cells utilizing an in vivo screening approach / Charlotte Rehm, Benedikt Klauser, and Jörg S. Hartig
Aptazyme-based riboswitches and logic gates in mammalian cells / Yoko Nomura and Yohei Yokobayashi
Design and characterization of topological small RNAs / Jack Hassall and others
Folding RNA-protein complex into designed nanostructures / Tomonori Shibata and others
Simple method for constructing RNA triangle, square, pentagon by tuning interior RNA 3WJ angle from 60° to 90° or 108° / Emil F. Khisamutdinov and others
RNA-mediated CdS-based nanostructures / Vinit Kumar and Anil Kumar
Effective method for specific gene silencing in Escherichia coli using artificial small RNA / Geunu Bak and others.Digital Access Springer 2015 - ArticleBusby WH, Travis JC.Comp Biochem Physiol B. 1978;60(4):389-96.1. Artiodactyla haptoglobins (Hps), goat, sheep and cattle (family Bovidae), and pig (family Suidae) were structurally characterized. 2. The polymeric Hp systems of goat, sheep and cattle were similar to the polymeric human Hp system, while the monomeric system of pig was more comparable to the monomeric human form. 3. All members of the Artiodactyla (family Bovidae) examined exhibited a large polypeptide subunit, comparable to that of the beta subunit of human Hp. 4. In addition, a small subunit, similar in molecular weight to the human alpha 2 subunit, was demonstrated. Pig Hp was shown to have two subunits, one slightly larger than the human beta subunit and the other intermediate in size to the human alpha 1 and alpha 2 subunits. 5. Immunoelectrophoretic and immunodiffusion studies indicated complete cross reactivity among the polymeric Artiodactyla Hps. 6. The polymeric Hps do not, however, cross react with the monomeric pig Hp.