Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Christie V. Papagiannis"'
Autor:
James L. Yen, Karin Flick, Peter K. Kaiser, Ikram Ouni, Christie V. Papagiannis, Lan Huang, An Tyrrell, Radhika Mathur, Robyn M. Kaake
Publikováno v:
Molecular Cell. 48(2):288-297
Summary A large group of E3 ubiquitin ligases is formed by the multisubunit SCF complex, whose core complex (Rbx1/Cul1-Cdc53/Skp1) binds one of many substrate recruiting F-box proteins to form an array of SCF ligases with diverse substrate specificit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c180f02e80c016c55ab7c3356018bc16
Publikováno v:
Journal of Biological Chemistry. 283:11615-11624
Met30 is the substrate recognition subunit of the essential ubiquitin ligase SCF(Met30). The essential function of Met30 is the inactivation of the Saccharomyces cerevisiae transcription factor Met4, because fully activated Met4 induces a cell cycle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9edb8ec65b4a1f35c47291d656505964
https://doi.org/10.1074/jbc.m708230200
https://doi.org/10.1074/jbc.m708230200
Autor:
Daniel Yoo, Robert T. Clubb, Mohamad A. Abbani, Christie V. Papagiannis, Reid C. Johnson, Duilio Cascio, My D. Sam
Publikováno v:
Journal of Molecular Biology. 367:328-343
The phage-encoded Xis protein is the major determinant controlling the direction of recombination in phage lambda. Xis is a winged-helix DNA binding protein that cooperatively binds to the attR recombination site to generate a curved microfilament, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f4e6ce50fe0ad206bfb711d510aae5e
https://doi.org/10.1016/j.jmb.2006.12.071
https://doi.org/10.1016/j.jmb.2006.12.071
Autor:
Duilio Cascio, Robert T. Clubb, Reid C. Johnson, Mohamad A. Abbani, Christie V. Papagiannis, My D. Sam
Publikováno v:
Proceedings of the National Academy of Sciences. 104:2109-2114
The DNA architectural protein Xis regulates the construction of higher-order nucleoprotein intasomes that integrate and excise the genome of phage lambda from the Escherichia coli chromosome. Xis modulates the directionality of site-specific recombin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4f1ab59e8300318bb20685c78daab85
https://doi.org/10.1073/pnas.0607820104
https://doi.org/10.1073/pnas.0607820104
Autor:
Arthur Landy, Hideki Aihara, Tom Ellenberger, Reid C. Johnson, Marco A. Azaro, Simone E. Nunes-Düby, Radhakrishna S. Tirumalai, Christie V. Papagiannis, Dibyendu Sarkar
Publikováno v:
Journal of Molecular Biology. 324:775-789
The site-specific recombinase (Int) of bacteriophage lambda is a heterobivalent DNA-binding protein that binds two different classes of DNA-binding sites within its recombination target sites. The several functions of Int are apportioned between a la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22320e7e0fff19cabcdfa66c38caab2b
https://doi.org/10.1016/s0022-2836(02)01199-3
https://doi.org/10.1016/s0022-2836(02)01199-3
Autor:
Jonathan M. Wojciak, Leah Corselli, James R. Lee, Christie V. Papagiannis, My D. Sam, Junji Iwahara, Robert T. Clubb, Martin L. Phillips, Kevin M. Connolly, Reid C. Johnson
Publikováno v:
Journal of Molecular Biology. 324:791-805
Upon induction of a bacteriophage λ lysogen, a site-specific recombination reaction excises the phage genome from the chromosome of its bacterial host. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63f18faa47740e7a38bc279fdcdbfab6
https://doi.org/10.1016/s0022-2836(02)01150-6
https://doi.org/10.1016/s0022-2836(02)01150-6