Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Rory K. Geyer"'
Publikováno v:
Molecular Cell. 12(3):783-790
Cullins (CULs) are subunits of a prominent class of RING ubiquitin ligases. Whereas the subunits and substrates of CUL1-associated SCF complexes and CUL2 ubiquitin ligases are well established, they are largely unknown for other cullin family members
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5381a11277d6e80d110cad8d93b02a96
Publikováno v:
Oncogene. 19:5892-5897
Wild-type p53 is stabilized and accumulates in the nucleus of DNA damaged cells. The effect of stabilizing p53 is to inhibit cell growth, either through a G1 cell cycle arrest or apoptotic cell death. MDM2 can inhibit p53 activity, in part, by promot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfde348002891eeb05b402bdb7acdf59
https://doi.org/10.1038/sj.onc.1203980
https://doi.org/10.1038/sj.onc.1203980
Publikováno v:
Nature cell biology. 7(4)
The COP9 signalosome (CSN) is known to bind cullin-RING ubiquitin ligases (CRLs) and to promote their activity in vivo. The mechanism of this stimulation has remained enigmatic because CSN's intrinsic and associated enzymatic activities paradoxically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8390f656faf86dcc58ddec5064aeef0d
https://pubmed.ncbi.nlm.nih.gov/15793566
https://pubmed.ncbi.nlm.nih.gov/15793566
Publikováno v:
The Journal of biological chemistry. 276(48)
MDM2 can bind the N terminus of p53 and promote its ubiquitination and export from the nucleus to the cytoplasm, where p53 can then be degraded by cytoplasmic proteasomes. Several studies have reported that an intact MDM2 binding domain is necessary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9d39b63cb76d78b85c6ea6e57e8190e
https://pubmed.ncbi.nlm.nih.gov/11572869
https://pubmed.ncbi.nlm.nih.gov/11572869
Publikováno v:
Nature cell biology. 2(9)
MDM2 can bind to p53 and promote its ubiquitination and subsequent degradation by the proteasome. Current models propose that nuclear export of p53 is required for MDM2-mediated degradation, although the function of MDM2 in p53 nuclear export has not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ba2df49bd14f2170176b13c75389f1e
https://pubmed.ncbi.nlm.nih.gov/10980696
https://pubmed.ncbi.nlm.nih.gov/10980696
Autor:
Rory K. Geyer, Dieter A. Wolf
Publikováno v:
Cell. 114:532-533
Polyubiquitylation is a complex but poorly understood biochemical reaction catalyzed by E3 ubiquitin ligases. In this issue of Cell, Deffenbaugh et al. provide experimental support for a model in which the dynamic release of the ubiquitin-charged E2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::356f3b00786a89cf05bc2ab7cb5686c8
https://doi.org/10.1016/s0092-8674(03)00682-2
https://doi.org/10.1016/s0092-8674(03)00682-2
Autor:
Volker Seibert, Chunshui Zhou, Rory K. Geyer, Svetlana Lyapina, Raymond J. Deshaies, Greg Cope, Dieter A. Wolf, Edward Rhee
Publikováno v:
BMC Biochemistry. 2:7
Background: The function of the fission yeast cullins Pcu1p and Pcu4p requires modification by the ubiquitin-related peptide Ned8p. A recent report by Lyapina et al. shows that the COP9/ signalosome (CSN), a multifunctional eight subunit complex, reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f9b9c533b1667204a79c751b58a15ed
https://doi.org/10.1186/1471-2091-2-7
https://doi.org/10.1186/1471-2091-2-7
Publikováno v:
FEBS Letters. (3):196-201
p53 is stabilized in response to DNA damaging stress. This stabilization is thought to result from phosphorylation in the N-terminus of p53, which inhibits p53:MDM2 binding, and prevents MDM2 from promoting p53 ubiquitination. In this report, the DNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51822bf937e1ffbf73c40f9ea2dbda6b