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William Inwood
Researcher at Lawrence Berkeley National Laboratory
Publications - 5
Citations - 751
William Inwood is an academic researcher from Lawrence Berkeley National Laboratory. The author has contributed to research in topics: Gene & Bacteriophage. The author has an hindex of 3, co-authored 5 publications receiving 724 citations.
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Journal ArticleDOI
Transcription factors bind thousands of active and inactive regions in the Drosophila blastoderm.
Xiao-Yong Li,Stewart MacArthur,Richard Bourgon,David A. Nix,Daniel A. Pollard,Venky N. Iyer,Aaron Hechmer,Lisa Simirenko,Mark Stapleton,Cris L. Luengo Hendriks,Hou Cheng Chu,Nobuo Ogawa,William Inwood,Victor Sementchenko,Amy Beaton,Richard Weiszmann,Susan E. Celniker,David W. Knowles,Thomas R. Gingeras,Terence P. Speed,Michael B. Eisen,Mark D. Biggin +21 more
TL;DR: Surprisingly, for five of the six factors, their recognition sites are not unambiguously more constrained evolutionarily than the immediate flanking DNA, even in more highly bound and presumably functional regions, indicating that comparative DNA sequence analysis is limited in its ability to identify functional transcription factor targets.
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The chromosome of Shigella flexneri bacteriophage Sf6: Complete nucleotide sequence, genetic mosaicism, and DNA packaging
Sherwood R. Casjens,Danella A. Winn-Stapley,Eddie B. Gilcrease,Renato Morona,Christiane Kühlewein,James E. H. Chua,Paul A. Manning,William Inwood,Alvin J. Clark +8 more
TL;DR: It is predicted that the integrase, early transcription anti-terminator, CI and Cro repressors, and CII protein of Sf6 have DNA binding specificities very similar to the homologous proteins encoded by phages HK620, lambda, 434 and P22, respectively.
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Nucleotide sequence of coliphage HK620 and the evolution of lambdoid phages.
TL;DR: In this paper, a temperate lambdoid bacteriophage that adsorbs to the O-antigen of its host, Escherichia coli H, was identified.
Journal ArticleDOI
Correction: Transcription Factors Bind Thousands of Active and Inactive Regions in the Drosophila Blastoderm
Xiao-Yong Li,Stewart MacArthur,Richard Bourgon,David A. Nix,Daniel A. Pollard,Venky N. Iyer,Aaron Hechmer,Lisa Simirenko,Mark Stapleton,Cris L. Luengo Hendriks,Hou Cheng Chu,Nobuo Ogawa,William Inwood,Victor Sementchenko,Amy Beaton,Richard Weiszmann,Susan E. Celniker,David W. Knowles,Thomas R. Gingeras,Terence P. Speed,Michael B. Eisen,Mark D. Biggin +21 more
TL;DR: The corrected version of the Table below gives the intended information for the enzyme phosphorylated at the C terminus, which is recognized by the H14 monoclonal antibody.
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The RadB protein from Pyrococcus does not complement E. coli recA mutations in vivo.
TL;DR: It is concluded that overexpression of any protein can produce an artificial growth inhibition or stationary phase in recA mutant cells, which allows cells to recover from UV damage due to the action of repair systems that do not require RecA-like activity.