𝔖 Bobbio Scriptorium
✦   LIBER   ✦

RNA Interference: A New Way to Analyze Protein Function

✍ Scribed by Ute Schepers; Thomas Kolter

Publisher
John Wiley and Sons
Year
2001
Tongue
English
Weight
72 KB
Volume
40
Category
Article
ISSN
0044-8249

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

From Structure to Function: A New Approa
From Structure to Function: A New Approach to Detect Functional Similarity among Proteins Independent from Sequence and Fold Homology
✍ Stefan Schmitt; Manfred Hendlich; Gerhard Klebe πŸ“‚ Article πŸ“… 2001 πŸ› John Wiley and Sons 🌐 English βš– 199 KB πŸ‘ 1 views

Protein function is almost invariably linked with the specific recognition of substrates or endogenous ligands in particular binding pockets; proteins of related function should, therefore, share comparable recognition pockets. On the basis of this idea a new computer method has been developed to de

A new soft-core potential function for m
A new soft-core potential function for molecular dynamics applied to the prediction of protein loop conformations
✍ Tappura, K.; Lahtela-Kakkonen, M.; Teleman, O. πŸ“‚ Article πŸ“… 2000 πŸ› John Wiley and Sons 🌐 English βš– 262 KB πŸ‘ 1 views

We have developed a new soft-core potential function for the conformational search of complex systems with molecular dynamics. The potential function was designed to maintain the main equilibrium properties of the original force field, which means that the soft-core potential gives physically realis

A new way to construct luminescent funct
A new way to construct luminescent functionalized polysiloxane based on ternary lanthanide complexes of 1, 10-phenanthroline
✍ Haifeng Lu; Lei Liu; Shengyu Feng πŸ“‚ Article πŸ“… 2011 πŸ› John Wiley and Sons 🌐 English βš– 335 KB πŸ‘ 1 views

## Abstract A kind of polysiloxane with ester group as the functional side chain was prepared via hydrosilylation reaction in this article. Then the functionalized polysiloxane was submitted to complex with 1, 10‐phenanthroline and lanthanide ions (Tb^3+^ and Eu^3+^ ions, respectively) to obtain tw

Search for aCaenorhabditis elegans FMR1
Search for aCaenorhabditis elegans FMR1 homologue: Identification of a new putative RNA-binding protein (PRP-1) that hybridizes to the mouse FMR1 double K homology domain
✍ Shtang, Sharon; Perry, Marc D.; Percy, Maire E. πŸ“‚ Article πŸ“… 1999 πŸ› John Wiley and Sons 🌐 English βš– 19 KB πŸ‘ 1 views

A mixed stage gt10 Caenorhabditis elegans cDNA library was screened with a probe derived by polymerase chain reaction from the double K homology (KH) domain of mouse FMR1 cDNA, a region that is highly conserved in the human, mouse, chicken, and frog FMR1 proteins. Four positively hybridizing cDNAs w