Transcription: building an initiation machine (Q41045750)

26 September 2017

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title

Transcription: building an initiation machine (English)

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26 September 2017

Travers A

1

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26 September 2017

language of work or name

English

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publication date

1 April 1996

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26 September 2017

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26 September 2017

volume

6

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26 September 2017

issue

4

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26 September 2017

page(s)

401-403

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The role of activators in assembly of RNA polymerase II transcription complexes

26 September 2017

cites work

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Crystal structure of a yeast TBP/TATA-box complex

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Co-crystal structure of TBP recognizing the minor groove of a TATA element

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Near-zero linking difference upon transcription factor IID binding to promoter DNA.

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Underwinding of DNA on binding of yeast TFIID to the TATA element

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Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex

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Structural basis for DNA bending by the architectural transcription factor LEF-1

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Differences in the DNA-Binding Properties of the Hmg-Box Domains of HMG1 and the Sex-Determining Factor SRY

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A novel form of the DNA double helix imposed on the TATA-box by the TATA-binding protein

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Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein

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Crystal structure of a TFIIB-TBP-TATA-element ternary complex

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Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

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The N-terminal domain of TFIIB from Pyrococcus furiosus forms a zinc ribbon

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Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

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Interaction between an acidic activator and transcription factor TFIIB is required for transcriptional activation

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Protease footprinting reveals a surface on transcription factor TFIIB that serves as an interface for activators and coactivators

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A variety of DNA-binding and multimeric proteins contain the histone fold motif.

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The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization

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A histone octamer-like structure within TFIID

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Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID

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Identifiers

DOI

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26 September 2017

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