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000056130 0247_ $$2pmid$$apmid:16773394
000056130 0247_ $$2DOI$$a10.1007/s00249-006-0076-4
000056130 0247_ $$2WOS$$aWOS:000240899300005
000056130 037__ $$aPreJuSER-56130
000056130 041__ $$aeng
000056130 082__ $$a570
000056130 084__ $$2WoS$$aBiophysics
000056130 1001_ $$0P:(DE-HGF)0$$aPapadopoulos, G.$$b0
000056130 245__ $$aChanges in the level of poly(Phe) synthesis in Escherichia coli ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus can be explained by structural changes in the peptidyltransferase center: a molecular dynamics simulation anal.
000056130 260__ $$aBerlin$$bSpringer$$c2006
000056130 300__ $$a675 - 683
000056130 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000056130 3367_ $$2DataCite$$aOutput Types/Journal article
000056130 3367_ $$00$$2EndNote$$aJournal Article
000056130 3367_ $$2BibTeX$$aARTICLE
000056130 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000056130 3367_ $$2DRIVER$$aarticle
000056130 440_0 $$010441$$aEuropean Biophysics Journal : with Biophysics Letters$$v35$$x0175-7571$$y8
000056130 500__ $$aRecord converted from VDB: 12.11.2012
000056130 520__ $$aData from polyphenylalanine [poly(Phe)] synthesis determination in the presence and in the absence of erythromycin have been used in conjunction with Molecular Dynamics Simulation analysis, in order to localize the functional sites affected by mutations of Thermus thermophilus ribosomal protein L4 incorporated in Escherichia coli ribosomes. We observed that alterations in ribosome capability to synthesize poly(Phe) in the absence of erythromycin were mainly correlated to shifts of A2062 and C2612 of 23S rRNA, while in the presence of erythromycin they were correlated to shifts of A2060 and U2584 of 23S rRNA. Our results suggest a means of understanding the role of the extended loop of L4 ribosomal protein in ribosomal peptidyltransferase center.
000056130 536__ $$0G:(DE-Juel1)FUEK414$$2G:(DE-HGF)$$aKondensierte Materie$$cP54$$x0
000056130 588__ $$aDataset connected to Web of Science, Pubmed
000056130 650_2 $$2MeSH$$aAmino Acid Sequence
000056130 650_2 $$2MeSH$$aAnti-Bacterial Agents: pharmacology
000056130 650_2 $$2MeSH$$aErythromycin: pharmacology
000056130 650_2 $$2MeSH$$aEscherichia coli: drug effects
000056130 650_2 $$2MeSH$$aEscherichia coli: genetics
000056130 650_2 $$2MeSH$$aEscherichia coli: metabolism
000056130 650_2 $$2MeSH$$aModels, Molecular
000056130 650_2 $$2MeSH$$aMolecular Sequence Data
000056130 650_2 $$2MeSH$$aMutation
000056130 650_2 $$2MeSH$$aNucleic Acid Conformation
000056130 650_2 $$2MeSH$$aPeptides: metabolism
000056130 650_2 $$2MeSH$$aPeptidyl Transferases: chemistry
000056130 650_2 $$2MeSH$$aPeptidyl Transferases: metabolism
000056130 650_2 $$2MeSH$$aProtein Conformation
000056130 650_2 $$2MeSH$$aRNA, Bacterial: genetics
000056130 650_2 $$2MeSH$$aRNA, Ribosomal, 23S: genetics
000056130 650_2 $$2MeSH$$aRibosomal Proteins: chemistry
000056130 650_2 $$2MeSH$$aRibosomal Proteins: genetics
000056130 650_2 $$2MeSH$$aRibosomal Proteins: metabolism
000056130 650_2 $$2MeSH$$aRibosomes: genetics
000056130 650_2 $$2MeSH$$aRibosomes: metabolism
000056130 650_2 $$2MeSH$$aThermus thermophilus: metabolism
000056130 650_7 $$00$$2NLM Chemicals$$aAnti-Bacterial Agents
000056130 650_7 $$00$$2NLM Chemicals$$aPeptides
000056130 650_7 $$00$$2NLM Chemicals$$aRNA, Bacterial
000056130 650_7 $$00$$2NLM Chemicals$$aRNA, Ribosomal, 23S
000056130 650_7 $$00$$2NLM Chemicals$$aRibosomal Proteins
000056130 650_7 $$00$$2NLM Chemicals$$aribosomal protein L4
000056130 650_7 $$0114-07-8$$2NLM Chemicals$$aErythromycin
000056130 650_7 $$030394-07-1$$2NLM Chemicals$$apolyphenylalanine
000056130 650_7 $$0EC 2.3.2.12$$2NLM Chemicals$$aPeptidyl Transferases
000056130 650_7 $$2WoSType$$aJ
000056130 65320 $$2Author$$amolecular dynamics
000056130 65320 $$2Author$$aribosomal function
000056130 65320 $$2Author$$aerythromycin
000056130 7001_ $$0P:(DE-Juel1)VDB10417$$aGrudinin, S.$$b1$$uFZJ
000056130 7001_ $$0P:(DE-HGF)0$$aKalpaxis, D.$$b2
000056130 7001_ $$0P:(DE-HGF)0$$aCholi-Papadopoulou, T.$$b3
000056130 773__ $$0PERI:(DE-600)1398349-0$$a10.1007/s00249-006-0076-4$$gVol. 35, p. 675 - 683$$p675 - 683$$q35<675 - 683$$tEuropean biophysics journal$$v35$$x0175-7571$$y2006
000056130 8567_ $$uhttp://dx.doi.org/10.1007/s00249-006-0076-4
000056130 909CO $$ooai:juser.fz-juelich.de:56130$$pVDB
000056130 9131_ $$0G:(DE-Juel1)FUEK414$$bMaterie$$kP54$$lKondensierte Materie$$vKondensierte Materie$$x0$$zentfällt   bis 2009
000056130 9141_ $$aNachtrag$$y2006
000056130 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000056130 9201_ $$0I:(DE-Juel1)VDB31$$d31.12.2006$$gIFF$$kIFF-TH-II$$lTheorie II$$x1
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000056130 981__ $$aI:(DE-Juel1)IBI-5-20200312
000056130 981__ $$aI:(DE-Juel1)IAS-2-20090406
000056130 981__ $$aI:(DE-Juel1)ICS-2-20110106