G
Grace Gill
Researcher at Tufts University
Publications - 45
Citations - 5510
Grace Gill is an academic researcher from Tufts University. The author has contributed to research in topics: Transcription factor & General transcription factor. The author has an hindex of 30, co-authored 45 publications receiving 5252 citations. Previous affiliations of Grace Gill include Harvard University.
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SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?
TL;DR: The small ubiquitin-related modifier SUMO posttranslationally modifies many proteins with roles in diverse processes including regulation of transcription, chromatin structure, and DNA repair, yielding new insights into regulation of gene expression, genome maintenance, and signal transduction.
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Negative effect of the transcriptional activator GAL4
Grace Gill,Mark Ptashne +1 more
TL;DR: It is suggested that this inhibition, which the authors call squelching, reflects titration of a transcription factor by the activating region of GAL4, and that more efficient activators inhibit more strongly and that inhibition does not depend on the DNA-binding domain.
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Separation of DNA binding from the transcription-activating function of a eukaryotic regulatory protein.
TL;DR: These and related findings support the idea that GAL4 activates transcription by touching other DNA-bound proteins.
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Something about SUMO inhibits transcription.
TL;DR: It is suggested that one consequence of SUMOylation is to promote the interaction of transcription factors with co-repressors, suggesting that complex crosstalk between acetylation and SUMOolation is important for gene regulation.
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The hPLIC Proteins May Provide a Link between the Ubiquitination Machinery and the Proteasome
Maurits F. Kleijnen,Alan H. Shih,Pengbo Zhou,Sushant Kumar,Raymond E. Soccio,Nancy Kedersha,Grace Gill,Peter M. Howley +7 more
TL;DR: These findings raise the possibility that the hPLIC proteins, and possibly related ubiquitin-like family members, may functionally link the ubiquitination machinery to the proteasome to affect in vivo protein degradation.