Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
about
Structure of the multimodular endonuclease FokI bound to DNAIdentification of DNA recognition sequences and protein interaction domains of the multiple-Zn-finger protein Roaz.A new approach to the analysis of DNase I footprinting data and its application to the TFIIIA/5S DNA complex.Having it both ways: transcription factors that bind DNA and RNA.Assessment of major and minor groove DNA interactions by the zinc fingers of Xenopus transcription factor IIIAXenopus transcription factor IIIA and the 5S nucleosome: development of a useful in vitro system.Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.TFIIIA induced DNA bending: effect of low ionic strength electrophoresis buffer conditions.Binding of TFIIIA to derivatives of 5S RNA containing sequence substitutions or deletions defines a minimal TFIIIA binding siteDefinition of the binding sites of individual zinc fingers in the transcription factor IIIA-5S RNA gene complex.Ferritin mRNA: interactions of iron regulatory element with translational regulator protein P-90 and the effect on base-paired flanking regions.Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies of native and "aromatic-swap" domains define a "weakly polar switch".Structural polymorphism in the major groove of a 5S RNA gene complements the zinc finger domains of transcription factor IIIARecognition of diverse sequences by class I zinc fingers: asymmetries and indirect effects on specificity in the interaction between CF2II and A+T-rich elementsStereochemical basis of DNA recognition by Zn fingers.HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG.Specific targeting of protein-DNA complexes by DNA-reactive drugs (+)-CC-1065 and pluramycins.Determination of the base recognition positions of zinc fingers from sequence analysis.ATTS, a new and conserved DNA binding domain.Zinc is required for folding and binding of a single zinc finger to DNAPotato Spindle Tuber Viroid RNA-Templated Transcription: Factors and Regulation
P2860
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P2860
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
description
1990 nî lūn-bûn
@nan
1990 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
@ast
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
@en
type
label
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
@ast
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
@en
prefLabel
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
@ast
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
@en
P2093
P2860
P356
P1476
Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
@en
P2093
P2860
P304
P356
10.1073/PNAS.87.14.5528
P407
P577
1990-07-01T00:00:00Z