RNA interference and receptors

@article{,

title = {Comments on the paper by kumagai, hibino, kawano and sugiyama (1999) FEBS lett. 450, 227-230},

author = { P. Dumas and M. Bergdoll and J. Masson},

year  = {1999},

date = {1999-01-01},

journal = {FEBS Lett},

volume = {459},

number = {2},

pages = {282-3;discussion 284},

note = {0014-5793 

Comment 

Journal Article},

keywords = {*Acetyltransferases, Antibiotics, Bacterial, Bleomycin/*metabolism/pharmacology, effects/genetics/*metabolism, Glycopeptide/metabolism/pharmacology, Mutation, Proline/*genetics/pharmacology, Proteins/genetics/*metabolism, Streptomyces/drug},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering},

author = { P. Dumas and M. Bergdoll and C. Cagnon and J. M. Masson},

year  = {1994},

date = {1994-01-01},

journal = {EMBO J},

volume = {13},

number = {11},

pages = {2483-92},

abstract = {The antibiotic bleomycin, a strong DNA cutting agent, is naturally produced by actinomycetes which have developed a resistance mechanism against such a lethal compound. The crystal structure, at 2.3 A resolution, of a bleomycin resistance protein of 14 kDa reveals a structure in two halves with the same alpha/beta fold despite no sequence similarity. The crystal packing shows compact dimers with a hydrophobic interface and involved in mutual chain exchange. Two independent solution studies (analytical centrifugation and light scattering) showed that this dimeric form is not a packing artefact but is indeed the functional one. Furthermore, light scattering also showed that one dimer binds two antibiotic molecules as expected. A crevice located at the dimer interface, as well as the results of a site-directed mutagenesis study, led to a model wherein two bleomycin molecules are completely sequestered by one dimer. This provides a novel insight into antibiotic resistance due to drug sequestering, and probably also into drug transport and excretion.},

note = {0261-4189 

Journal Article},

keywords = {*Acetyltransferases, &, Acid, Amino, Bacterial, Bacterial/*genetics, Base, Binding, Bleomycin/*metabolism/pharmacology, Conformation, Crystallization, Crystallography, Data, Drug, Fusion, Genes, Gov't, Microbial/genetics, Models, Molecular, Mutagenesis, Non-U.S., Protein, Proteins/*chemistry/genetics/isolation, Proteins/isolation, purification, purification/metabolism, Recombinant, Relationship, Resistance, Secondary, Sequence, Site-Directed, Sites, Structural, structure, Structure-Activity, Support, X-Ray},

pubstate = {published},

tppubtype = {article}

}