Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Christopher D. Freel"'
Autor:
Joshua L. Andersen, Kenkyo Matsuura, Carrie E. Johnson, Jiyeon Kim, Manabu Kurokawa, Sally Kornbluth, Amanda B. Parrish, Christopher D. Freel
Publikováno v:
The EMBO Journal. 31:1279-1292
Many pro-apoptotic signals trigger mitochondrial cytochrome c release, leading to caspase activation and ultimate cellular breakdown. Cell survival pathways, including the mitogen-activated protein kinase (MAPK) cascade, promote cell viability by imp
Autor:
Chih-Sheng Yang, Christopher B. Newgard, Wanli Tang, Jonathan L. Coloff, Erika Segear Johnson, Christopher D. Freel, Jie An, Jeffrey C. Rathmell, Judy Qiju Wu, Olga Ilkayeva, Sarah R. Horn, Sally Kornbluth, Michael J. Thomenius
Publikováno v:
Molecular Biology of the Cell
Mitochondria form an interconnected network that undergoes dynamin-related protein 1 (Drp1)-dependent fission during mitosis. We demonstrate that changes in mitochondrial dynamics as cells exit mitosis are driven through ubiquitylation of Drp1 by the
Autor:
S Balasundaram, Christopher D. Freel, R Cannon, Michael J. Thomenius, Kristin White, Ronald J. Krieser, Sally Kornbluth, Eltyeb Abdelwahid, Sarah R. Horn
Publikováno v:
Cell Death and Differentiation
In most multicellular organisms, the decision to undergo programmed cell death in response to cellular damage or developmental cues is typically transmitted through mitochondria. It has been suggested that an exception is the apoptotic pathway of Dro
Autor:
Judy Qiju Wu, Christopher D. Freel, Wanli Tang, Chih-Sheng Yang, Sally Kornbluth, Chen Chen, Jessie Yanxiang Guo
Publikováno v:
Molecular Biology of the Cell
The anaphase-promoting complex/cyclosome (APC/C) inhibitor Emi2 contains a destruction box (D-box) found in APC/C substrates, but does not appear to inhibit the APC/C by a “pseudosubstrate” mechanism. Rather, it inhibits transfer of ubiquitin fro
Publikováno v:
Cell death and differentiation
Factors influencing apoptosis of vertebrate eggs and early embryos have been studied in cell-free systems and in intact embryos by analyzing individual apoptotic regulators or caspase activation in static samples. Described here is a novel method for
Autor:
Leta K, Nutt, Marisa R, Buchakjian, Eugene, Gan, Rashid, Darbandi, Sook-Young, Yoon, Judy Q, Wu, Yuko J, Miyamoto, Jennifer A, Gibbons, Jennifer A, Gibbon, Josh L, Andersen, Christopher D, Freel, Wanli, Tang, Changli, He, Manabu, Kurokawa, Yongjun, Wang, Seth S, Margolis, Rafael A, Fissore, Sally, Kornbluth
Publikováno v:
Developmental Cell. 16:856-866
Xenopus oocyte death is partly controlled by the apoptotic initiator, caspase-2. We reported previously that oocyte nutrient depletion activates caspase-2 upstream of mitochondrial cytochrome c release. Conversely, nutrient-replete oocytes inhibit ca
Autor:
Chen Chen, Wanli Tang, Angus C. Nairn, Sally Kornbluth, Chih-Sheng Yang, Christopher D. Freel, Jessie Yanxiang Guo, Judy Qiju Wu
Publikováno v:
Nature Cell Biology. 11:644-651
Loss of cell division cycle 2 (Cdc2, also known as Cdk1) activity after cyclin B degradation is necessary, but not sufficient, for mitotic exit. Proteins phosphorylated by Cdc2 and downstream mitotic kinases must be dephosphorylated. We report here t
Autor:
Judy Qiju Wu, Christopher D. Freel, Jennifer A. Perry, Leta K. Nutt, Sally Kornbluth, Peter K. Jackson, David V. Hansen, Yanxiang Guo, Wanli Tang
Publikováno v:
Molecular Biology of the Cell. 19:3536-3543
The transition of oocytes from meiosis I (MI) to meiosis II (MII) requires partial cyclin B degradation to allow MI exit without S phase entry. Rapid reaccumulation of cyclin B allows direct progression into MII, producing a cytostatic factor (CSF)-a
Autor:
D. Ashley Richardson, Christopher D. Freel, Sally Kornbluth, Michael R. Olson, Eugene C. Gan, Michael J. Thomenius, Sarah R. Horn
Publikováno v:
Journal of Biological Chemistry. 283:367-379
Morphological hallmarks of apoptosis result from activation of the caspase family of cysteine proteases, which are opposed by a pro-survival family of inhibitors of apoptosis proteins (IAPs). In Drosophila, disruption of IAP function by Reaper, HID,
Autor:
Daniel J. Lew, Trevin R. Zyla, Johannes Rudolph, Mignon A. Keaton, Christopher D. Freel, Elaine S.G. Bardes, Aron R. Marquitz
Publikováno v:
Current Biology. 17:1181-1189
Summary Background Several checkpoint pathways employ Wee1-mediated inhibitory tyrosine phosphorylation of cyclin-dependent kinases (CDKs) to restrain cell-cycle progression. Whereas in vertebrates this strategy can delay both DNA replication and mit