Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Hayley I. Muendlein"'
Autor:
David Jetton, Hayley I. Muendlein, Wilson M. Connolly, Zoie Magri, Irina Smirnova, Rebecca Batorsky, Joan Mecsas, Alexei Degterev, Alexander Poltorak
Publikováno v:
Cell Reports, Vol 43, Iss 8, Pp 114641- (2024)
Summary: Caspase-8-dependent pyroptosis has been shown to mediate host protection from Yersinia infection. For this mode of cell death, the kinase activity of receptor-interacting protein kinase 1 (RIPK1) is required, but the autophosphorylation site
Externí odkaz:
https://doaj.org/article/8f76fc38478046edb57e8621e9f53391
Autor:
Hayley I. Muendlein, Wilson M. Connolly, Zoie Magri, Irina Smirnova, Vladimir Ilyukha, Avishekh Gautam, Alexei Degterev, Alexander Poltorak
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Yersiania YopJ protein has been shown to drive caspase-8-mediated pyroptosis. Here the authors show a precise mechanism of this non-canonical cell death pathway that is controlled by a TRIF-dependent complex of FADD, RIPK1, caspase-8 and ZBP1.
Externí odkaz:
https://doaj.org/article/c23eacb750254746b5eeb2cdfdaf0689
Autor:
Hayley I. Muendlein, Joseph Sarhan, Beiyun C. Liu, Wilson M. Connolly, Stephen A. Schworer, Irina Smirnova, Amy Y. Tang, Vladimir Ilyukha, Jodie Pietruska, Soroush Tahmasebi, Nahum Sonenberg, Alexei Degterev, Alexander Poltorak
Publikováno v:
Cell Reports, Vol 30, Iss 3, Pp 699-713.e4 (2020)
Summary: Receptor-interacting protein kinase 1 (RIPK1) and 3 (RIPK3) are well known for their capacity to drive necroptosis via mixed-lineage kinase-like domain (MLKL). Recently, RIPK1/3 kinase activity has been shown to drive inflammation via activa
Externí odkaz:
https://doaj.org/article/b14db846e8cc4f8c8f65d98ff6c63481
Autor:
Beiyun C. Liu, Joseph Sarhan, Alexander Panda, Hayley I. Muendlein, Vladimir Ilyukha, Jörn Coers, Masahiro Yamamoto, Ralph R. Isberg, Alexander Poltorak
Publikováno v:
Cell Reports, Vol 24, Iss 1, Pp 155-168.e5 (2018)
Summary: Legionella pneumophila elicits caspase-11-driven macrophage pyroptosis through guanylate-binding proteins (GBPs) encoded on chromosome 3. It has been proposed that microbe-driven IFN upregulates GBPs to facilitate pathogen vacuole rupture an
Externí odkaz:
https://doaj.org/article/217eebaf70ed4ee88874c232373dfad4
Autor:
Hayley I. Muendlein, Wilson M. Connolly, James Cameron, David Jetton, Zoie Magri, Irina Smirnova, Edouard Vannier, Xudong Li, Amanda J. Martinot, Rebecca Batorsky, Alexander Poltorak
Publikováno v:
Sci Immunol
TNF mediates a variety of biological processes including cellular proliferation, inflammatory responses, and cell death and is therefore associated with numerous pathologies including autoinflammatory diseases and septic shock. The inflammatory and c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae9307eb3fde09c39761121d8bf642ad
https://doi.org/10.1126/sciimmunol.add0665
https://doi.org/10.1126/sciimmunol.add0665
Autor:
Hayley I. Muendlein, Wilson M. Connolly, Zoie Magri, David Jetton, Irina Smirnova, Alexei Degterev, Siddharth Balachandran, Alexander Poltorak
Publikováno v:
Proceedings of the National Academy of Sciences. 119
ZBP1 is widely recognized as a mediator of cell death for its role in initiating necroptotic, apoptotic, and pyroptotic cell death pathways in response to diverse pathogenic infection. Herein, we characterize an unanticipated role for ZBP1 in promoti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56658ecc0d309b1806e4791bec5acaf2
https://doi.org/10.1073/pnas.2113872119
https://doi.org/10.1073/pnas.2113872119
Autor:
Alexander Poltorak, Hayley I. Muendlein, Wilson M. Connolly, Zoie Magri, David Jetton, Keith P. Eidell, Irina Smirnova
Publikováno v:
Science. 367:1379-1384
Macrophages cFLIP out Pathogens have evolved to survive within hosts in part by interfering with host signaling cascades. Yersinia bacteria use the effector protein YopJ to thwart MAP kinase signaling downstream of Toll-like receptor activation. In r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa130518942ad7f7b4e9bcf5841171db
https://doi.org/10.1126/science.aay3878
https://doi.org/10.1126/science.aay3878
Autor:
Vladimir Ilyukha, Alexei Degterev, Wilson M. Connolly, Hayley I. Muendlein, Beiyun C. Liu, Nahum Sonenberg, Jodie R. Pietruska, Alexander Poltorak, Stephen A Schworer, Amy Y. Tang, Irina Smirnova, Joseph Sarhan, Soroush Tahmasebi
Publikováno v:
Cell Reports, Vol 30, Iss 3, Pp 699-713.e4 (2020)
Cell reports
Cell reports
SUMMARY Receptor-interacting protein kinase 1 (RIPK1) and 3 (RIPK3) are well known for their capacity to drive necroptosis via mixed-lineage kinase-like domain (MLKL). Recently, RIPK1/3 kinase activity has been shown to drive inflammation via activat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4a1250365ebdbe7fbf10d5c8e26b77
http://www.sciencedirect.com/science/article/pii/S2211124719317309
http://www.sciencedirect.com/science/article/pii/S2211124719317309
Autor:
Stephen C. Bunnell, Keith P. Eidell, Alenka Lovy, Ken Nguyen, Frank A Scangarello, Michael J. Ophir, Maria-Cristina Seminario, Hayley I. Muendlein, Nicholas R. Sylvain
Publikováno v:
J Cell Sci
Integrin engagement within the immune synapse enhances T cell activation, but our understanding of this process is incomplete. In response to T cell receptor (TCR) ligation, SLP-76 (LCP2), ADAP (FYB1) and SKAP55 (SKAP1) are recruited into microcluste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f73da64d285143d725616f1cbc35730e
https://doi.org/10.1242/jcs.258602
https://doi.org/10.1242/jcs.258602
Publikováno v:
Curr Protoc
A large protein complex, containing RIPK1, RIPK3, and caspase-8 and known as Complex II, has emerged as one of the key mediators of cell death downstream from a range of innate immune triggers. This regulatory mechanism plays a prominent role in macr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91505a5390ef6b2d53377e2aa444ba54
https://doi.org/10.1002/cpz1.156
https://doi.org/10.1002/cpz1.156