RNA interference and receptors

@article{,

title = {Anticodon-independent aminoacylation of an RNA minihelix with valine},

author = {M Frugier and C Florentz and R Giege},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1570324},

isbn = {1570324},

year  = {1992},

date = {1992-01-01},

journal = {Proc Natl Acad Sci U S A},

volume = {89},

number = {9},

pages = {3990-3994},

abstract = {Minihelices mimicking the amino acid acceptor and anticodon branches of yeast tRNA(Val) have been synthesized by in vitro transcription of synthetic templates. It is shown that a minihelix corresponding to the amino acid acceptor branch and containing solely a valine-specific identity nucleotide can be aminoacylated by yeast valyl-tRNA synthetase. Its charging ability is lost after mutating this nucleotide. This ability is stimulated somewhat by the addition of a second hairpin helix that mimicks the anticodon arm, which suggests that information originating from the anticodon stem-loop can be transmitted to the active site of the enzyme by the core of the protein.},

note = {0027-8424 

Journal Article},

keywords = {*Amino Acid Activation  Anticodon  Base Sequence  Hydrogen Bonding  In Vitro  Molecular Sequence Data  RNA, ERIANI, FLORENTZ, FRUGIER, Non-U.S. Gov't  Valine-tRNA Ligase/*metabolism, Transfer, Unité ARN, Val/chemistry/*metabolism  Saccharomyces cerevisiae  Structure-Activity Relationship  Support},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {Crystallization of aspartyl-tRNA synthetase-tRNA(Asp) complex from Escherichia coli and first crystallographic results},

author = {S Eiler and M Boeglin and F Martin and G Eriani and J Gangloff and J C Thierry and D Moras},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1569573},

isbn = {1569573},

year  = {1992},

date = {1992-01-01},

journal = {J Mol Biol},

volume = {224},

number = {4},

pages = {1171-1173},

abstract = {Crystals of the dimeric aspartyl-tRNA synthetase from Escherichia coli (molecular mass 132,000 Da) complexed with its cognate tRNA (molecular mass 25,000 Da) have been grown using ammonium sulfate as precipitant. The crystals belong to the orthorhombic space group C222(1) with unit cell parameters a = 102.75 A},

note = {0022-2836 

Journal Article},

keywords = {Asp/*ultrastructure  X-Ray Diffraction, Aspartate-tRNA Ligase/*ultrastructure  Crystallography  Escherichia coli/enzymology  RNA, ERIANI, Transfer, Unité ARN},

pubstate = {published},

tppubtype = {article}

}