نتایج جستجو برای: bax protein

تعداد نتایج: 1240252  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2008
Avigail D Amsel Moran Rathaus Noam Kronman Haim Y Cohen

The DNA end-joining protein Ku70 is one of several proteins that inhibit apoptosis by sequestering the proapoptotic factor Bax from the mitochondria. However, the molecular mechanism underlying Ku70-dependent inhibition of Bax is not fully understood. Here, we show that the absence of Ku70 results in the accumulation of ubiquitylated Bax. Under normal growth conditions, Bax ubiquitylation promo...

Journal: :Molecular cell 2011
Sean P Cullen Conor M Henry Seamus J Martin

Much debate surrounds how prosurvival members of the BCL-2 family repress opening of the BAX/BAK channel to block apoptosis; in this issue Llambi et al. (2011) identify two modes of apoptosis inhibition that exhibit surprisingly different behavior upon repeat proapoptotic challenges by BH3-only proteins.

Journal: :The Journal of biological chemistry 1998
M Zhou S D Demo T N McClure R Crea C M Bitler

Cell death plays an important role in a number of physiological processes in all complex multicellular organisms. One of the molecules that regulates this process is BAX, an integral membrane protein, that promotes apoptosis. The function of BAX is countered by BCL-2 and BCL-XL. The differential expression of these proteins can influence the ability of the cell to die or survive. In this paper,...

2015
Jose Manuel Bravo-San Pedro Yongjie Wei Valentina Sica Maria Chiara Maiuri Zhongju Zou Guido Kroemer Beth Levine

Disruption of the complex of BECN1 with BCL2 or BCL2L1/BCL-XL is an essential switch that turns on cellular autophagy in response to environmental stress or treatment with BH3 peptidomimetics. Recently, it has been proposed that BCL2 and BCL2L1/BCL-XL may inhibit autophagy indirectly through a mechanism dependent on the proapoptotic BCL2 family members, BAX and BAK1. Here we report that the BH3...

  Background and Objective: As apoptotic cell death is extremely involved in physiological development and many pathological situations such as cancer and neurodegenerative diseases, the understanding of its molecular machinery can be useful in designing new therapeutic strategies. The present study investigated the temporal expression of the proapoptotic protein Bax in adult spinal motoneuron...

Journal: :Journal of virology 2009
Logan Banadyga Kirstin Veugelers Stephanie Campbell Michele Barry

Apoptosis is a potent immune barrier against viral infection, and many viruses, including poxviruses, encode proteins to overcome this defense. Interestingly, the avipoxviruses, which include fowlpox and canarypox virus, are the only poxviruses known to encode proteins with obvious Bcl-2 sequence homology. We previously characterized the fowlpox virus protein FPV039 as a Bcl-2-like antiapoptoti...

Journal: :The Biochemical journal 2006
Michela Capano Martin Crompton

The cytosolic protein Bax plays a key role in apoptosis by migrating to mitochondria and releasing proapoptotic proteins from the mitochondrial intermembrane space. The present study investigates the movement of Bax in isolated rat neonatal cardiomyocytes subjected to simulated ischaemia (minus glucose, plus cyanide), using green fluorescent protein-tagged Bax as a means of imaging Bax movement...

Journal: :The Biochemical journal 2000
B Antonsson S Montessuit S Lauper R Eskes J C Martinou

Bax is a Bcl-2-family protein with pro-apoptotic activity that can form channels in lipid membranes. The protein has been shown to trigger cytochrome c release from mitochondria both in vitro and in vivo. Recombinant human Bax isolated in the presence of detergent was found to be present as an oligomer with an apparent molecular mass of approx. 160000 Da on gel filtration. When Bax was isolated...

Journal: :Biochemistry 2003
Cecília M P Rodrigues Susana Solá Juanita C Sharpe José J G Moura Clifford J Steer

Bax is a potent pro-apoptotic member of the Bcl-2 protein family that localizes to the mitochondrial membrane during apoptosis. Tauroursodeoxycholic acid (TUDCA) modulates the apoptotic threshold, in part, by preventing Bax translocation both in vitro and in vivo. The mechanisms by which Bax induces and TUDCA inhibits release of cytochrome c are unclear. We show here that recombinant Bax protei...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1999
A R Khaled K Kim R Hofmeister K Muegge S K Durum

IL-7 functions as a trophic factor during T lymphocyte development by a mechanism that is partly based on the induction of Bcl-2, which protects cells from apoptosis. Here we report a mechanism by which cytokine withdrawal activates the prodeath protein Bax. On loss of IL-7 in a dependent cell line, Bax protein translocated from the cytosol to the mitochondria, where it integrated into the mito...

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