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Elizabeth A. Campbell

Researcher at Rockefeller University

Publications -  103
Citations -  8914

Elizabeth A. Campbell is an academic researcher from Rockefeller University. The author has contributed to research in topics: RNA polymerase & Transcription (biology). The author has an hindex of 39, co-authored 91 publications receiving 7538 citations. Previous affiliations of Elizabeth A. Campbell include Wellcome Trust.

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Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase

TL;DR: The crystal structure of Thermus aquaticus core RNAP complexed with Rif explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length.
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Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 Å Resolution

TL;DR: The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a "crab claw"-shaped molecule with a 27 A wide internal channel that places key functional sites, defined by mutational and cross-linking analysis, on the inner walls of the channel in close proximity to the active center Mg2+.
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Structural Basis of Transcription Initiation: An RNA Polymerase Holoenzyme-DNA Complex

TL;DR: The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (α2ββ′ωσA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map.
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Fulminant Jejuno-Ileitis following Ablation of Enteric Glia in Adult Transgenic Mice

TL;DR: It is suggested that enteric glia play an essential role in maintaining the integrity of the bowel and suggest that their loss or dysfunction may contribute to the cellular mechanisms of inflammatory bowel disease.
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Structure of the Bacterial RNA Polymerase Promoter Specificity σ Subunit

TL;DR: Proteolysis of Thermus aquaticus σ A, which occurred in situ during crystallization, reveals three domains, σ 2 , σ 3 , and σ 4 , connected by flexible linkers, and genetic studies correctly predicted that a helix-turn-helix motif in ρ 4 recognizes the −35 element but not the details of the protein-DNA interactions.