Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Samuel Benchimol"'
Autor:
David Miller, Kyra Kerkhofs, Farnoosh Abbas-Aghababazadeh, Sahib Singh Madahar, Mark D. Minden, Josée Hébert, Benjamin Haibe-Kains, Mark A. Bayfield, Samuel Benchimol
Publikováno v:
Cell Death and Disease, Vol 14, Iss 8, Pp 1-15 (2023)
Abstract Erythropoietin (EPO) suppresses drug-induced apoptosis in EPO-receptor-positive leukemia cells and allows cells to persist after drug treatment by promoting cellular senescence. Importantly a small proportion of senescent cells can re-enter
Externí odkaz:
https://doaj.org/article/394704a1b29e49fa9d8a6266ec257a51
Autor:
Anne Hakem, Miyuki Bohgaki, Bénédicte Lemmers, Elisabeth Tai, Leonardo Salmena, Elzbieta Matysiak-Zablocki, Yong-Sam Jung, Jana Karaskova, Lilia Kaustov, Shili Duan, Jason Madore, Paul Boutros, Yi Sheng, Marta Chesi, P Leif Bergsagel, Bayardo Perez-Ordonez, Anne-Marie Mes-Masson, Linda Penn, Jeremy Squire, Xinbin Chen, Igor Jurisica, Cheryl Arrowsmith, Otto Sanchez, Samuel Benchimol, Razqallah Hakem
Publikováno v:
PLoS Genetics, Vol 7, Iss 11, p e1002360 (2011)
Ubiquitylation is fundamental for the regulation of the stability and function of p53 and c-Myc. The E3 ligase Pirh2 has been reported to polyubiquitylate p53 and to mediate its proteasomal degradation. Here, using Pirh2 deficient mice, we report tha
Externí odkaz:
https://doaj.org/article/ceeccf61e253499a91010ab5fb3e09e2
Autor:
Tak Wah Mak, Samuel Benchimol, Christopher D. Richardson, Robert Rottapel, Marees Harris-Brandts, Annick Itie-YouTen, Alexandra Ho, Kathrin Zaugg, Masami Hirota-Tsuchihara, Lauren Brown, Hitoshi Okada, Christopher Bakal, Valentina Lapin, Katsuya Tsuchihara
Supplementary Figures 1-4 from Ckap2 Regulates Aneuploidy, Cell Cycling, and Cell Death in a p53-Dependent Manner
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00040f3d755f34167f5370451e99154d
https://doi.org/10.1158/0008-5472.22363320
https://doi.org/10.1158/0008-5472.22363320
Autor:
Tak Wah Mak, Samuel Benchimol, Christopher D. Richardson, Robert Rottapel, Marees Harris-Brandts, Annick Itie-YouTen, Alexandra Ho, Kathrin Zaugg, Masami Hirota-Tsuchihara, Lauren Brown, Hitoshi Okada, Christopher Bakal, Valentina Lapin, Katsuya Tsuchihara
We used DNA microarray screening to identify Ckap2 (cytoskeleton associated protein 2) as a novel p53 target gene in a mouse erythroleukemia cell line. DNA damage induces human and mouse CKAP2 expression in a p53-dependent manner and p53 activates th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e0e1daa8971436483fc28863c43c00e
https://doi.org/10.1158/0008-5472.c.6493653.v1
https://doi.org/10.1158/0008-5472.c.6493653.v1
Autor:
Tak Wah Mak, Samuel Benchimol, Christopher D. Richardson, Robert Rottapel, Marees Harris-Brandts, Annick Itie-YouTen, Alexandra Ho, Kathrin Zaugg, Masami Hirota-Tsuchihara, Lauren Brown, Hitoshi Okada, Christopher Bakal, Valentina Lapin, Katsuya Tsuchihara
Supplementary Methods from Ckap2 Regulates Aneuploidy, Cell Cycling, and Cell Death in a p53-Dependent Manner
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::381889fc056e2a75bbe78128d7610f84
https://doi.org/10.1158/0008-5472.22363317
https://doi.org/10.1158/0008-5472.22363317
Autor:
Tinatin Chabrashvili, Asen Bagashev, Samuel Benchimol, Shongshan Fan, Bassel E. Sawaya, Pier Paolo Claudio, Ruma Mukerjee, Roger P Leng
Publikováno v:
Scopus-Elsevier
Several reports have pointed to the negative involvement of p53 in transcriptional regulation of the human immunodeficiency virus type 1 long-terminal repeat (HIV-1 LTR). We recently demonstrated that through their physical interaction, cdk9 phosphor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e21ebcebeb2f56a7846ad83d105b06b
https://doi.org/10.4161/cc.24733
https://doi.org/10.4161/cc.24733
ROS-Mediated p53 Induction of Lpin1 Regulates Fatty Acid Oxidation in Response to Nutritional Stress
Autor:
Wanli Xuan, Daniel A. Rubinger, Keith Wheaton, Wissam Assaily, Lauren Brown-Endres, Weili Ma, Katsuya Tsuchihara, Tak W. Mak, Samuel Benchimol, Yunping Lin
Publikováno v:
Molecular Cell. 44:491-501
The p53 protein is activated by stress signals and exhibits both protective and death-promoting functions that are considered important for its tumor suppressor function. Emerging evidence points toward an additional role for p53 in metabolism. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fca140a6cd54b8f0dbd5802afffd3b8
https://doi.org/10.1016/j.molcel.2011.08.038
https://doi.org/10.1016/j.molcel.2011.08.038
Publikováno v:
Aging Cell. 9:747-760
Cellular senescence limits the replicative capacity of normal cells and acts as an intrinsic barrier that protects against the development of cancer. Telomere shortening-induced replicative senescence is dependent on the ATM-p53-p21 pathway but addit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ae01e9e84ee95ab7f64cee27b245875
https://doi.org/10.1111/j.1474-9726.2010.00601.x
https://doi.org/10.1111/j.1474-9726.2010.00601.x
Publikováno v:
British Journal of Cancer
Background: Tumour necrosis factor (TNF) is capable of activating the cell death pathway, and has been implicated in killing transformed cells. However, TNF also activates survival signals, including NF-κB activation and the subsequent expression of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b66ad91b9f658c2ab3aedfdfcd78734
https://doi.org/10.1038/sj.bjc.6605352
https://doi.org/10.1038/sj.bjc.6605352
Autor:
Lauren Brown, Samuel Benchimol
Publikováno v:
Journal of Biological Chemistry. 281:3832-3840
The effect of ERK, p38, and JNK signaling on p53-dependent apoptosis and cell cycle arrest was investigated using a Friend murine erythroleukemia virus (FVP)-transformed cell line that expresses a temperature-sensitive p53 allele, DP16.1/p53ts. In re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f28af08a771b69b6e6ce65e447ca1f6
https://doi.org/10.1074/jbc.m507951200
https://doi.org/10.1074/jbc.m507951200