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Keywords: caspase
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Biosci Rep (2022) 42 (6): BSR20220119.
Published: 17 June 2022
...Liqi Yao; A. Clay Clark All caspases evolved from a common ancestor and subsequently developed into two general classes, inflammatory or apoptotic caspases. The caspase-hemoglobinase fold has been conserved throughout nearly one billion years of evolution and is utilized for both the monomeric...
Includes: Supplementary data
Biosci Rep (2021) 41 (1): BSR20203495.
Published: 29 January 2021
...Liqi Yao; Paul Swartz; Paul T. Hamilton; A. Clay Clark Caspase (or cysteinyl-aspartate specific proteases) enzymes play important roles in apoptosis and inflammation, and the non-identical but overlapping specificity profiles (that is, cleavage recognition sequence) direct cells to different fates...
Includes: Supplementary data
Biosci Rep (2019) 39 (1): BSR20180992.
Published: 18 January 2019
... License 4.0 (CC BY) . Apoptosis Apoptotic bodies caspase Death receptors drug design intercellular communication Apoptosis is a highly regulated process of cell death. Unlike necrosis which is a traumatic version of cell death, apoptosis is a rational and active decision made...
Biosci Rep (2018) 38 (3): BSR20180503.
Published: 31 May 2018
... of apoptosis, which was followed by release of mitochondrial cytochrome c to cytosol, activation of caspase-3 and -9, as well as cleaved PARP. Moreover, Western blot results confirmed that Piperine (8, 16, and 20 μM) decreased phosphorylation of JNK and p38 MAPK in A2780 cells. In addition, caspase-3 inhibitor...
Biosci Rep (2014) 34 (2): e00100.
Published: 25 March 2014
...Tanja Kitevska; Sarah J. Roberts; Delara Pantaki-Eimany; Sarah E. Boyd; Fiona L. Scott; Christine J. Hawkins Caspase-2 is an evolutionarily conserved but enigmatic protease whose biological role remains poorly understood. To date, research into the functions of caspase-2 has been hampered...
Includes: Supplementary data
Biosci Rep (2012) 32 (4): 401–411.
Published: 28 June 2012
...Jad Walters; Joshua L. Schipper; Paul Swartz; Carla Mattos; A. Clay Clark A mutation in the allosteric site of the caspase 3 dimer interface of Val 266 to histidine abolishes activity of the enzyme, and models predict that the mutation mimics the action of small molecule allosteric inhibitors...
Includes: Supplementary data
Biosci Rep (2012) 32 (3): 305–313.
Published: 12 March 2012
...Hyo Jin Kang; Young-mi Lee; Myeong Seon Jeong; Moonil Kim; Kwang-Hee Bae; Seung Jun Kim; Sang J. Chung Various apoptotic signals can activate caspases 3 and 7 by triggering the L2 loop cleavage of their proenzymes. These two enzymes have highly similar structures and functions, and serve...