Results 51 to 60 of about 24,233,392 (378)

Caspase-1 activates gasdermin A in non-mammals. [PDF]

open access: yesElife, 2023
Gasdermins oligomerize to form pores in the cell membrane, causing regulated lytic cell death called pyroptosis. Mammals encode five gasdermins that can trigger pyroptosis: GSDMA, B, C, D, and E. Caspase and granzyme proteases cleave the linker regions of and activate GSDMB, C, D, and E, but no endogenous activation pathways are yet known for GSDMA ...
Billman ZP   +5 more
europepmc   +5 more sources

Heat-shock pretreatment inhibits sorbitol-induced apoptosis in K562, U937 and HeLa cells. [PDF]

open access: yes, 2009
The aim of this study was to determine whether heat-shock pretreatment exerted a protective effect against sorbitol-induced apoptotic cell death in K562, U937 and HeLa cell lines and whether such protection was associated with a decreased cytochrome c
Aventaggiato, Michele   +8 more
core   +1 more source

Caspase-1 initiates apoptosis in the absence of gasdermin D

open access: yesNature Communications, 2019
Caspase-1 activated in inflammasomes triggers a programmed necrosis called pyroptosis, which is mediated by gasdermin D (GSDMD). However, GSDMD-deficient cells are still susceptible to caspase-1-mediated cell death.
K. Tsuchiya   +14 more
semanticscholar   +1 more source

Pramanicin induces apoptosis in Jurkat leukemia cells; a role for JNK, p38 and caspase activation [PDF]

open access: yes, 2005
Pramanicin is a novel anti-fungal drug with a wide range of potential application against human diseases. It has been previously shown that pramanicin induces cell death and increases calcium levels in vascular endothelial cells. In the present study, we
Başağa, Hüveyda   +3 more
core   +1 more source

Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1 [PDF]

open access: yesNature, 2012
Inflammasomes are cytosolic multiprotein complexes assembled by intracellular nucleotide-binding oligomerization domain (NOD)-like receptors (NLRs) and they initiate innate immune responses to invading pathogens and danger signals by activating caspase-1 (ref. 1).
Broz, Petr   +6 more
openaire   +4 more sources

The role of cytochrome c in caspase activation in Drosophila melanogaster cells [PDF]

open access: yes, 2002
The release of cytochrome c from mitochondria is necessary for the formation of the Apaf-1 apoptosome and subsequent activation of caspase-9 in mammalian cells.
Cakouros, Dimitrios   +5 more
core   +3 more sources

Regulation of the Apaf-1/Caspase-9 Apoptosome by Caspase-3 and XIAP [PDF]

open access: yesJournal of Biological Chemistry, 2003
The apoptosome is a multiprotein complex comprising Apaf-1, cytochrome c, and caspase-9 that functions to activate caspase-3 downstream of mitochondria in response to apoptotic signals. Binding of cytochrome c and dATP to Apaf-1 in the cytosol leads to the assembly of a heptameric complex in which each Apaf-1 subunit is bound noncovalently to a ...
Junshan Hao   +8 more
openaire   +3 more sources

Pseudomonas aeruginosa pilin activates the inflammasome [PDF]

open access: yes, 2011
IL-1 beta is produced from inactive pro-IL-1 beta by activation of caspase-1 brought about by a multi-subunit protein platform called the inflammasome. Many bacteria can trigger inflammasome activity through flagellin activation of the host protein NLRC4.
Agostini   +54 more
core   +1 more source

Caspase-1 self-cleavage is an intrinsic mechanism to terminate inflammasome activity

open access: yesJournal of Experimental Medicine, 2018
Host-protective caspase-1 activity must be tightly regulated to prevent pathology, but mechanisms controlling the duration of cellular caspase-1 activity are unknown.
D. Boucher   +12 more
semanticscholar   +1 more source

Thy-1 interaction with Fas in lipid rafts regulates fibroblast apoptosis and lung injury resolution. [PDF]

open access: yes, 2017
Thy-1-negative lung fibroblasts are resistant to apoptosis. The mechanisms governing this process and its relevance to fibrotic remodeling remain poorly understood. By using either sorted or transfected lung fibroblasts, we found that Thy-1 expression is
Bradley, John E   +11 more
core   +1 more source

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