Výsledky vyhledávání - "Joan W. Sellers"

Long-term production and delivery of human growth hormone in vivo

Autor: Antoinette M. Zuliani, Michael W. Heartlein, Victoria A. Roman, Richard F. Selden, Douglas A. Treco, Ji-Lei Jiang, Joan W. Sellers

Publikováno v: Proceedings of the National Academy of Sciences. 91:10967-10971

The application of somatic cell gene therapy to large patient populations will require the development of safe and practical approaches to the generation and characterization of genetically manipulated cells. Transkaryotic implantation is a gene ther

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e912d8c77ae0589e2fd71df3b14727b9
https://doi.org/10.1073/pnas.91.23.10967

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Role of the conserved leucines in the leucine zipper dimerization motif of yeast GCN4

Autor: Joan W. Sellers, Willem J. van Heeckeren, Kevin Struhl

Publikováno v: Nucleic Acids Research. 20:3721-3724

Yeast GCN4 belongs to the class of eukaryotic transcription factors whose bZIP DNA-binding domains dimerize via a leucine zipper motif that structurally resembles a coiled coil. The leucine zipper contains 4-5 highly conserved leucine residues spaced

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a98522575bdabaad6add16229924ec66
https://doi.org/10.1093/nar/20.14.3721

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Mutations That Define the Optimal Half-Site for Binding Yeast GCN4 Activator Protein and Identify an ATF/CREB-Like Repressor That Recognizes Similar DNA Sites

Autor: Joan W. Sellers, Kevin Struhl, A C Vincent

Publikováno v: Molecular and Cellular Biology. 10:5077-5086

The yeast GCN4 transcriptional activator protein binds as a dimer to a dyad-symmetric sequence, indicative of a protein-DNA complex in which two protein monomers interact with adjacent half-sites. However, the optimal GCN4 recognition site, ATGA(C/G)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75edba582c18dc02a9475978c167b4ad
https://doi.org/10.1128/mcb.10.10.5077-5086.1990

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Changing fos oncoprotein to a jun-independent DNA binding protein with GCN4 dimerization specificity by swapping 'leucine zippers'

Autor: Joan W. Sellers, Kevin Struhl

Publikováno v: Nature. 341(6237)

A structural motif for DNA-binding proteins, the 'leucine zipper', has been proposed for the jun, fos and myc gene products, the yeast transcriptional activator GCN4, and the C/EBP enhancer-binding protein. These proteins all contain a region with fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c74350a8456deda05e8288f44ccb563e
https://pubmed.ncbi.nlm.nih.gov/2505087

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