scholarly article | Q13442814 |
P356 | DOI | 10.1038/NSB0296-122 |
P698 | PubMed publication ID | 8564536 |
P50 | author | Robert A Scott | Q56124268 |
Christopher M Colangelo | Q56724424 | ||
P2093 | author name string | Zhu W | |
Lewis M | |||
Zeng Q | |||
Summers MF | |||
P2860 | cites work | Zinc mining for protein domains | Q44005805 |
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P433 | issue | 2 | |
P921 | main subject | Pyrococcus furiosus | Q146310 |
P304 | page(s) | 122-124 | |
P577 | publication date | 1996-02-01 | |
P1433 | published in | Nature structural biology | Q26842658 |
P1476 | title | The N-terminal domain of TFIIB from Pyrococcus furiosus forms a zinc ribbon | |
P478 | volume | 3 |
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Q27936096 | Evidence that transcription factor IIB is required for a post-assembly step in transcription initiation |
Q34708554 | Functional analysis of archaeal MBF1 by complementation studies in yeast |
Q40763314 | Functional interaction between TFIIB and the Rpb2 subunit of RNA polymerase II: implications for the mechanism of transcription initiation |
Q27933410 | Genetic analysis of the large subunit of yeast transcription factor IIE reveals two regions with distinct functions |
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Q36573736 | Mutational analysis of the D1/E1 core helices and the conserved N-terminal region of yeast transcription factor IIB (TFIIB): identification of an N-terminal mutant that stabilizes TATA-binding protein-TFIIB-DNA complexes |
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Q27649705 | Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus |
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Q27656951 | Structure of the C-terminal domain of transcription factor IIB from Trypanosoma brucei |
Q27643172 | Structure of the archaeal translation initiation factor aIF2 from Methanobacterium thermoautotrophicum: Implications for translation initiation |
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Q47891418 | The N-terminal region of yeast TFIIB contains two adjacent functional domains involved in stable RNA polymerase II binding and transcription start site selection |
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Q44013210 | The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability |
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