Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Shawn B Bratton"'
Autor:
Indra M Mahajan, Miao-Der Chen, Israel Muro, John D Robertson, Casey W Wright, Shawn B Bratton
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e84388 (2014)
Acute heat shock can induce apoptosis through a canonical pathway involving the upstream activation of caspase-2, followed by BID cleavage and stimulation of the intrinsic pathway. Herein, we report that the BH3-only protein BIM, rather than BID, is
Externí odkaz:
https://doaj.org/article/acdf2b2e1df24255811ce8e53f0223da
Autor:
Daric J. Wible, Zalak Parikh, Eun Jeong Cho, Miao-Der Chen, Collene R. Jeter, Somshuvra Mukhopadhyay, Kevin N. Dalby, Shankar Varadarajan, Shawn B. Bratton
Publikováno v:
Cell Death and Disease, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract p38 mitogen-activated protein kinases (MAPKs) participate in autophagic signaling; and previous reports suggest that pyridinyl imidazole p38 MAPK inhibitors, including SB203580 and SB202190, induce cell death in some cancer cell-types throug
Externí odkaz:
https://doaj.org/article/d44578e962124c259e90c2981820c4c4
Autor:
Daric J. Wible, Zalak Parikh, Eun Jeong Cho, Miao-Der Chen, Somshuvra Mukhopadhyay, Kevin N. Dalby, Shankar Varadarajan, Shawn B. Bratton
Publikováno v:
bioRxiv
p38 mitogen-activated protein kinases (MAPKs) regulate early endocytic trafficking, but their effects on late endocytic trafficking remain unclear. Herein, we report that the pyridinyl imidazole p38 MAPK inhibitors, SB203580 and SB202190, induce a ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f5935cfa3ec0f1a31dda007460eaa2e
https://europepmc.org/articles/PMC10054966/
https://europepmc.org/articles/PMC10054966/
The Apaf-1 apoptosome induces formation of caspase-9 homo- and heterodimers with distinct activities
Autor:
Chu-Chiao Wu, Sunhee Lee, Srinivas Malladi, Miao-Der Chen, Nicholas J. Mastrandrea, Zhiwen Zhang, Shawn B. Bratton
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Apoptotic initiator caspases are thought to be activated through homodimerization but this remains controversial. Here the authors demonstrate that caspase-9 can adopt two distinct conformations within the Apaf-1 apoptosome, each with distinct proper
Externí odkaz:
https://doaj.org/article/3d0127db2c6e47c1b48d6022cb92b4e4
Autor:
Chu-Chiao Wu, Shawn B. Bratton
Publikováno v:
Molecular & Cellular Oncology, Vol 4, Iss 2 (2017)
For nearly 2 decades, investigators have debated whether cysteinyl-aspartate-specific protease 9 (caspase-9) is activated within the apoptotic protease-activating factor 1 (Apaf-1) apoptosome through proximity-induced homodimerization or through form
Externí odkaz:
https://doaj.org/article/0671edd1f492485dad4269c119a1a81b
Publikováno v:
Cell Discovery
Cell Discovery, Vol 5, Iss 1, Pp 1-19 (2019)
Cell Discovery, Vol 5, Iss 1, Pp 1-19 (2019)
Autophagy is critical for maintaining cellular homeostasis during times of stress, and is thought to play important roles in both tumorigenesis and tumor cell survival. Formation of autophagosomes, which mediate delivery of cytoplasmic cargo to lysos
The Apaf-1 apoptosome induces formation of caspase-9 homo- and heterodimers with distinct activities
Autor:
Sunhee Lee, Nicholas J. Mastrandrea, Chu Chiao Wu, Srinivas Malladi, Zhiwen Zhang, Shawn B. Bratton, Miao Der Chen
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Nature Communications
Nature Communications
According to dogma, initiator caspases are activated through proximity-induced homodimerization, but some studies infer that during apoptosis caspase-9 may instead form a holoenzyme with the Apaf-1 apoptosome. Using several biochemical approaches, in
Autor:
Shawn B. Bratton, Daric J. Wible
Publikováno v:
Current opinion in toxicology. 7
Reactive oxygen species (ROS) are important signaling molecules that mediate oxidative stress and cellular damage when improperly regulated. ROS and oxidative stress can activate autophagy, which generally serves as a cytoprotective negative feedback
Publikováno v:
Seminars in Cell & Developmental Biology. 30:27-35
The ubiquitination of proteins is a post-translational modification that was first described as a means to target misfolded or unwanted proteins for degradation by the proteasome. It is now appreciated that the ubiquitination of proteins also serves
Autor:
Shawn B. Bratton, Chu Chiao Wu
Publikováno v:
Antioxidants & Redox Signaling. 19:546-558
Significance: The intrinsic apoptosis pathway is conserved from worms to humans and plays a critical role in the normal development and homeostatic control of adult tissues. As a result, numerous diseases from cancer to neurodegeneration are associat