Elongation complexes of Thermus thermophilus RNA polymerase that possess distinct translocation conformations.
about
Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor proteinYeast DEAD box protein Mss116p is a transcription elongation factor that modulates the activity of mitochondrial RNA polymerase.Kinetic pathway of pyrophosphorolysis by a retrotransposon reverse transcriptase.Transcription elongation. Heterogeneous tracking of RNA polymerase and its biological implications.RNA transcript 3'-proximal sequence affects translocation bias of RNA polymerase.Transcriptional slippage in the positive-sense RNA virus family Potyviridae.Molecular basis of transcriptional fidelity and DNA lesion-induced transcriptional mutagenesis.Multisubunit RNA polymerases melt only a single DNA base pair downstream of the active site.RNA polymerase II transcriptional fidelity control and its functional interplay with DNA modifications.Direct versus limited-step reconstitution reveals key features of an RNA hairpin-stabilized paused transcription complex.Factor-independent transcription pausing caused by recognition of the RNA-DNA hybrid sequence.Maintenance of RNA-DNA hybrid length in bacterial RNA polymerases.Crystallization and preliminary X-ray crystallographic analyses of Thermus thermophilus backtracked RNA polymerase.Crystallization and preliminary X-ray crystallographic analysis of Thermus thermophilus transcription elongation complex bound to Gfh1.Fluorescence-based assay to measure the real-time kinetics of nucleotide incorporation during transcription elongation.Mycobacterial RNA polymerase forms unstable open promoter complexes that are stabilized by CarD.Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.Efficient, ultra-high-affinity chromatography in a one-step purification of complex proteins.Systematic mutagenesis of the thymidine tract of the pyrBI attenuator and its effects on intrinsic transcription termination in Escherichia coli.RNA-DNA and DNA-DNA base-pairing at the upstream edge of the transcription bubble regulate translocation of RNA polymerase and transcription rate.
P2860
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P2860
Elongation complexes of Thermus thermophilus RNA polymerase that possess distinct translocation conformations.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Elongation complexes of Thermu ...... t translocation conformations.
@ast
Elongation complexes of Thermu ...... t translocation conformations.
@en
type
label
Elongation complexes of Thermu ...... t translocation conformations.
@ast
Elongation complexes of Thermu ...... t translocation conformations.
@en
prefLabel
Elongation complexes of Thermu ...... t translocation conformations.
@ast
Elongation complexes of Thermu ...... t translocation conformations.
@en
P2093
P2860
P356
P1476
Elongation complexes of Thermu ...... t translocation conformations.
@en
P2093
Dmitry G Vassylyev
Dmitry Temiakov
Ekaterina Kashkina
Michael Anikin
Sergei N Kochetkov
Tahir H Tahirov
P2860
P304
P356
10.1093/NAR/GKL559
P407
P577
2006-08-16T00:00:00Z