Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lei Lei Sengchanthalangsy"'
Autor:
Carrie A. Hughes, Christopher B. Phelps, Elizabeth A. Komives, Dennis Mishler, Tom Huxford, Lei Lei Sengchanthalangsy, Gourisankar Ghosh, De-Bin Huang, Ryan Reeves
Publikováno v:
Journal of Molecular Biology. 324:587-597
IκBα inhibits transcription factor NF-κB activity by specific binding to NF-κB heterodimers composed of p65 and p50 subunits. It binds with slightly lower affinity to p65 homodimers and with significantly lower affinity to homodimers of p50. We h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eeb3d2af13fc5b028ff69191eaff099a
https://doi.org/10.1016/s0022-2836(02)01149-x
https://doi.org/10.1016/s0022-2836(02)01149-x
Publikováno v:
Journal of Biological Chemistry. 275:29840-29846
X-ray crystal structures of the NF-kappa B.I kappa B alpha complex revealed an extensive and complex protein-protein interface involving independent structural elements present in both I kappa B alpha and NF-kappa B. In this study, we employ a gel el
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18c4d301f0974c37e045fcd9e7d47634
https://doi.org/10.1074/jbc.m004899200
https://doi.org/10.1074/jbc.m004899200
Publikováno v:
Journal of Biological Chemistry. 275:24392-24399
The DNA binding of three different NF-kappaB dimers, the p50 and p65 homodimers and the p50/p65 heterodimer, has been examined using a combination of gel mobility shift and fluorescence anisotropy assays. The NF-kappaB p50/p65 heterodimer is shown he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c4ac4d1f8fdcf3d8aee6a48a9d7bc654
https://doi.org/10.1074/jbc.m003784200
https://doi.org/10.1074/jbc.m003784200
Autor:
Chin Hui Hsiang, Daniel S. Straus, Gourisankar Ghosh, Lei Lei Sengchanthalangsy, Christopher K. Glass, Mercedes Ricote, Mei Li, Gabriel Pascual, John S. Welch
Publikováno v:
Proceedings of the National Academy of Sciences. 97:4844-4849
Prostaglandin J 2 (PGJ 2 ) and its metabolites Δ 12 -PGJ 2 and 15-deoxy-Δ 12,14 -PGJ 2 (15d-PGJ 2 ) are naturally occurring derivatives of prostaglandin D 2 that have been suggested to exert antiinflammatory effects in vivo . 15d-PGJ 2 is a high-af
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7a017d29b8a8da8731161666cd8c786
https://doi.org/10.1073/pnas.97.9.4844
https://doi.org/10.1073/pnas.97.9.4844
Publikováno v:
Structure. 8(4):419-428
Background: The NF-κB family of dimeric transcription factors regulates the expression of several genes by binding to a variety of related DNA sequences. One of these dimers, p65(RelA), regulates a subclass of these targets. We have shown previously
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::512e6fbb4ec1a96a02d475e7a875ba28
Autor:
Tom, Huxford, Dennis, Mishler, Christopher B, Phelps, De-Bin, Huang, Lei Lei, Sengchanthalangsy, Ryan, Reeves, Carrie A, Hughes, Elizabeth A, Komives, Gourisankar, Ghosh
Publikováno v:
Journal of molecular biology. 324(4)
IkappaBalpha inhibits transcription factor NF-kappaB activity by specific binding to NF-kappaB heterodimers composed of p65 and p50 subunits. It binds with slightly lower affinity to p65 homodimers and with significantly lower affinity to homodimers
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b260d2a4262775d214e5606bc0749ed8
https://pubmed.ncbi.nlm.nih.gov/12460563
https://pubmed.ncbi.nlm.nih.gov/12460563
Autor:
Lei Lei Sengchanthalangsy, Shrimati Datta, Gourisankar Ghosh, Eric Anderson, De-Bin Huang, Emory H. Braswell
Publikováno v:
Journal of molecular biology. 289(4)
Dimers of the Rel/NFkappaB transcription factor family form with differential stabilities through the combinatorial association of five polypeptides: p50, p52, p65, cRel, and RelB. Here, we have characterized the nature of the monomer-dimer equilibri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e99288dc36e8e33f1b57db9666b9b43
https://pubmed.ncbi.nlm.nih.gov/10369780
https://pubmed.ncbi.nlm.nih.gov/10369780