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dc.creatorTekos, A.en
dc.creatorStathopoulos, C.en
dc.creatorTsambaos, D.en
dc.creatorDrainas, D.en
dc.date.accessioned2015-11-23T10:49:39Z
dc.date.available2015-11-23T10:49:39Z
dc.date.issued2004
dc.identifier.issn9298673
dc.identifier.urihttp://hdl.handle.net/11615/33593
dc.description.abstractRNase P is an ubiquitous and essential endonuclease in tRNA biogenesis, which generates the mature 5′-termini of tRNAs. RNase P activities have been identified in all three kingdoms of life (Bacteria, Archaea, Eukarya). Most forms of RNase P are ribonucleoproteins, i.e., they consist of an essential RNA and protein subunits. In bacteria and in some archaea, the catalytic function of this enzyme resides entirely in its RNA subunit, which is one of firstly identified ribozymes. Its high structural and functional diversity among representatives of a vast variety of phylogenetic domains indicates that RNase P could also serve as a molecular target of and a useful screening system for the biological activity of different compounds and give more insight into the molecular mechanisms of their action inside the cell. The emerged information from recent studies on the mechanism and structural idiosyncrasies of RNase P provides a convenient platform for designing specific inhibitors for this ribozyme and potential areas of its application in gene therapy. This review summarises the current information on the effect of several protein synthesis inhibitors, retinoids and arotinoids, vitamin D analogues and anthalin on the activity of RNase P. © 2004 Bentham Science Publishers Ltd.en
dc.source.urihttp://www.scopus.com/inward/record.url?eid=2-s2.0-5644279189&partnerID=40&md5=d6c39c2259a89f18ad791bb17e7e3bfe
dc.subjectAminoglycosidesen
dc.subjectAnthralinen
dc.subjectCalcipotriolen
dc.subjectPeptidyl transferaseen
dc.subjectPsoriasisen
dc.subjectRetinoidsen
dc.subjectRibozymeen
dc.subjecttRNAen
dc.subject4 [2 (5,6,7,8 tetrahydro 5,5,8,8 tetramethyl 2 naphthyl) 1 propenyl]benzoic aciden
dc.subject4 [2 (5,6,7,8 tetrahydro 5,5,8,8 tetramethyl 2 naphthyl) 1 propenyl]benzoic acid ethyl esteren
dc.subjectaminoglycoside antibiotic agenten
dc.subjectarotinoiden
dc.subjectblasticidin Sen
dc.subjectdithranolen
dc.subjectetaroteneen
dc.subjectetretinen
dc.subjectframycetinen
dc.subjectgentamicinen
dc.subjectisotretinoinen
dc.subjectkanamycinen
dc.subjectparomomycinen
dc.subjectpolypeptide antibiotic agenten
dc.subjectprotein subuniten
dc.subjectprotein synthesis inhibitoren
dc.subjectpuromycinen
dc.subjectretinoic aciden
dc.subjectretinoid derivativeen
dc.subjectretinolen
dc.subjectribonuclease Pen
dc.subjectribonucleoproteinen
dc.subjectribosome RNAen
dc.subjecttemaroteneen
dc.subjecttetracyclineen
dc.subjecttobramycinen
dc.subjecttransfer RNAen
dc.subjectunindexed drugen
dc.subjectvitamin D derivativeen
dc.subjectArchaebacteriumen
dc.subjectbiogenesisen
dc.subjectcatalysisen
dc.subjectdrug structureen
dc.subjectdrug targetingen
dc.subjectenzyme activationen
dc.subjectenzyme activityen
dc.subjectenzyme inhibitionen
dc.subjecteukaryoteen
dc.subjectgene therapyen
dc.subjecthumanen
dc.subjectnonhumanen
dc.subjectphylogenyen
dc.subjectprotein analysisen
dc.subjectprotein domainen
dc.subjectprotein targetingen
dc.subjectreviewen
dc.subjectstructure activity relationen
dc.subjectstructure analysisen
dc.subjectAnimalsen
dc.subjectAnti-Bacterial Agentsen
dc.subjectCalcitriolen
dc.subjectClinical Trialsen
dc.subjectHumansen
dc.subjectPeptidyl Transferasesen
dc.titleRNase P: A promising molecular target for the development of new drugsen
dc.typejournalArticleen


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