ARN

@article{,

title = {Molecular recognition of aminoglycoside antibiotics by ribosomal RNA and resistance enzymes: an analysis of x-ray crystal structures},

author = {Q Vicens and E Westhof},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12925992},

isbn = {12925992},

year  = {2003},

date = {2003-01-01},

journal = {Biopolymers},

volume = {70},

number = {1},

pages = {42-57},

abstract = {The potential of RNA molecules to be used as therapeutic targets by small inhibitors is now well established. In this fascinating wide-open field, aminoglycoside antibiotics constitute the most studied family of RNA binding drugs. Within the last three years, several x-ray crystal structures were solved for aminoglycosides complexed to one of their main natural targets in the bacterial cell, the decoding aminoacyl-tRNA site (A site). Other crystallographic structures have revealed the binding modes of aminoglycosides to the three existing types of resistance-associated enzymes. The present review summarizes the various aspects of the molecular recognition of aminoglycosides by these natural RNA or protein receptors. The analysis and the comparisons of the detailed interactions offer insights that are helpful in designing new generations of antibiotics.},

note = {0006-3525 

Journal Article 

Review 

Review, Tutorial},

keywords = {Aminoglycosides/*chemistry  Anti-Bacterial Agents/*chemistry  Binding Sites  Crystallography, Chemical  Models, Microbial  Enzymes/*chemistry  Models, Molecular  Protein Binding  RNA/chemistry  RNA, Ribosomal/*chemistry  Ribosomes/chemistry, Unité ARN, WESTHOF, X-Ray/*methods  *Drug Resistance},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {Dimerization of human immunodeficiency virus type 1 RNA involves sequences located upstream of the splice donor site},

author = {R Marquet and J C Paillart and E Skripkin and C Ehresmann and B Ehresmann},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8121797},

isbn = {8121797},

year  = {1994},

date = {1994-01-01},

journal = {Nucleic Acids Res},

volume = {22},

number = {2},

pages = {145-151},

abstract = {The retroviral genome consists of two homologous RNA molecules associated close to their 5' ends. We studied the spontaneous dimerization of four HIV-1 RNA fragments (RNAs 1-707, 1-615, 311-612, and 311-415) containing the previously defined dimerization domain, and a RNA fragment (RNA 1-311) corresponding to the upstream sequences. Significant dimerization of all RNAs is observed on agarose gels when magnesium is included in the electrophoresis buffer. In contrast to dimerization of RNAs 311-612 and 311-415, dimerization of RNAs 1-707, 1-615 and 1-311 strongly depends on the size of the monovalent cation present in the incubation buffer. Also, dimerization of RNAs 1-707, 1-615, and 1-311 is 10 times faster than that of RNAs 311-612 and 311-415. The dimers formed by the latter RNAs are substantially more stable than that of RNA 1-615, while RNA 1-311 dimer is 5-7 degrees C less stable than RNA 1-615 dimer. These results indicate that dimerization of HIV-1 genomic RNA involves elements located upstream of the splice donor site (position 305), i.e. outside of the previously defined dimerization domain.},

note = {0305-1048 

Journal Article},

keywords = {Base Sequence  Cations  HIV-1/*genetics  Kinetics  Macromolecular Systems  Magnesium  Models, Chemical  Models, Genetic  Molecular Sequence Data  RNA Splicing  RNA, MARQUET, Non-U.S. Gov't  Thermodynamics, PAILLART, Unité ARN, Viral/*chemistry  Support},

pubstate = {published},

tppubtype = {article}

}