Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Meenu N. Perera"'
Publikováno v:
Food Microbiology. 52:42-48
ListShield™, a commercially available bacteriophage cocktail that specifically targets Listeria monocytogenes, was evaluated as a bio-control agent for L. monocytogenes in various Ready-To-Eat foods. ListShield™ treatment of experimentally contam
Publikováno v:
Biophysical Journal. 101(9):2163-2169
When activated, the proapoptotic protein Bax permeabilizes the mitochondrial outer membrane, allowing the release of proteins into the cytosol and thus initiating the execution phase of apoptosis. When activated Bax was reconstituted into phospholipi
Autor:
Vidyaramanan Ganesan, Meenu N. Perera, Debra Datskovskiy, David Colombini, Marco Colombini, Kirti Chadha
Publikováno v:
Apoptosis. 15:553-562
A critical step in apoptosis is mitochondrial outer membrane permeabilization (MOMP), releasing proteins critical to downstream events. While the regulation of this process by Bcl-2 family proteins is known, the role of ceramide, which is known to be
Autor:
Marco Colombini, Vidyaramanan Ganesan, Zdzislaw M. Szulc, Meenu N. Perera, Robert Bittman, Leah J. Siskind, Alicja Bielawska
Publikováno v:
Chemistry and physics of lipids. 194
A ceramide commonly found in mammalian cells, C16-ceramide (N-palmitoyl-d-erythro-sphingosine), is capable of forming large, protein-permeable channels in the mitochondrial outer membrane (MOM). However, C16-ceramide is unable to permeabilize the pla
Autor:
Meenu N. Perera, Johnny Stiban
Publikováno v:
Biochimica et biophysica acta. 1848(2)
Mitochondria mediate both cell survival and death. The intrinsic apoptotic pathway is initiated by the permeabilization of the mitochondrial outer membrane to pro-apoptotic inter-membrane space (IMS) proteins. Many pathways cause the egress of IMS pr
Autor:
Shang H. Lin, Marco Colombini, Yuri K. Peterson, Alicja Bielawska, Zdzislaw M. Szulc, Meenu N. Perera, Robert Bittman
Publikováno v:
The Biochemical journal. 445(1)
The present study demonstrates the important structural features of ceramide required for proper regulation, binding and identification by both pro-apoptotic and anti-apoptotic Bcl-2 family proteins. The C-4=C-5 trans-double bond has little influence
Publikováno v:
Biophysical Journal. 102(3)
The sphingolipid, ceramide can self-assemble in phospholipid membranes to form large channels capable of translocating proteins through membranes. Electronmicroscopic visualization and electrophysiological measurements reveal a range of pore sizes wi
Publikováno v:
Biophysical Journal. 100(3)
Ceramide is a sphingolipid that has been shown to play a vital role in the commitment of a cell to apoptosis. There is increasing evidence that ceramide channels may be the pathway through which cytochrome c is released from mitochondria, a critical
Publikováno v:
Biophysical Journal. 100(3)
The sphingolipid, ceramide, forms channels capable of translocating proteins through membranes. These channels can form in the mitochondrial outer membrane at ceramide levels found to be present in that membrane early in apoptosis. For these channels
Publikováno v:
Biophysical Journal. 98(3)
The pro-apoptotic protein, Bax, and the sphingolipid, ceramide, can individually form channels in phospholipid membranes. When combined, they permeabilize membranes in a synergistic way, indicating the formation of a combined channel structure. Nanom