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These proteins initiate and execute the actual process of cell demolition.
Executioner caspases such as Caspase-3 and Caspase-7 have long been recognised as the key proteases involved in cell demolition during apoptosis.
Activation of Bax and Bak causes permeabilization of the mitochondrial outer membrane, leading to release of cytochrome c, activation of caspase-9 and ultimately cell demolition.
This family of proteins maintains a subtle survival/cell-death balance by regulating mitochondrial integrity, caspase activation, and consequent cell demolition.
These pores are compatible with promoting release of ions as well as proteinaceous components, suggesting that membrane-integrated Bax monomers in the presence of Bid BH3 peptides are key functional units for the activation of the cell demolition machinery.
In mammals, cell death can proceed via the 'intrinsic' (also called 'BCL-2 regulated', 'mitochondrial' or 'stress') or the 'extrinsic' (also called 'death receptor') pathway, both converging upon the activation of caspases that mediate cell demolition.
Similar(6)
Apoptosis is a fundamental biologic process that could be described as controlled demolition of cell and is inherent in every cells and plays vital roles in numerous medical disorders [ 1, 2].
Death receptor activation leads to the formation of death receptor signaling platforms, resulting in the demolition of the cell.
Effector caspases (caspase-3, -6 and -7) are responsible for demolition of the cell during apoptosis [ 20].
Caspase 3 (CASP3) was first described in 1995 and once activated, is considered to be responsible for the actual demolition of the cell during apoptosis [ 9, 10].
Active caspase-8 heterotetramers p102-p182 initiate the apoptotic cascade by cleavage and activation of the effector caspases, which in turn leads to the demolition of the cell.
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