Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Elizabeth J Osterlund"'
Autor:
James M Pemberton, Dang Nguyen, Elizabeth J Osterlund, Wiebke Schormann, Justin P Pogmore, Nehad Hirmiz, Brian Leber, David W Andrews
Publikováno v:
eLife, Vol 12 (2023)
Anti-apoptotic proteins such as BCL-XL promote cell survival by sequestering pro-apoptotic BCL-2 family members, an activity that frequently contributes to tumorigenesis. Thus, the development of small-molecule inhibitors for anti-apoptotic proteins,
Externí odkaz:
https://doaj.org/article/c46858294f8f416e96855c98bce4cf03
Autor:
Xiaoke Chi, Dang Nguyen, James M Pemberton, Elizabeth J Osterlund, Qian Liu, Hetal Brahmbhatt, Zhi Zhang, Jialing Lin, Brian Leber, David W Andrews
Publikováno v:
eLife, Vol 9 (2020)
The Bcl-2 family BH3 protein Bim promotes apoptosis at mitochondria by activating the pore-forming proteins Bax and Bak and by inhibiting the anti-apoptotic proteins Bcl-XL, Bcl-2 and Mcl-1. Bim binds to these proteins via its BH3 domain and to the m
Externí odkaz:
https://doaj.org/article/3930186c3fd04ad4a33907088e2464c2
Autor:
Qian Liu, Elizabeth J Osterlund, Xiaoke Chi, Justin Pogmore, Brian Leber, David William Andrews
Publikováno v:
eLife, Vol 8 (2019)
Tumor initiation, progression and resistance to chemotherapy rely on cancer cells bypassing programmed cell death by apoptosis. We report that unlike other pro-apoptotic proteins, Bim contains two distinct binding sites for the anti-apoptotic protein
Externí odkaz:
https://doaj.org/article/35be500a47c444d396b9241785a6b15f
Autor:
Nehad Hirmiz, Elizabeth J Osterlund, Morgan Richards, David W. Andrews, Qiyin Fang, Anthony Tsikouras
Publikováno v:
IEEE Journal of Selected Topics in Quantum Electronics. 27:1-9
Protein-protein interactions can be measured in live cells, at nanometer scale, using Fluorescence Lifetime Imaging Microscopy (FLIM) enabled Forster Resonance Energy Transfer (FRET). There are growing interests in exploring protein-protein interacti
Fluorescence lifetime imaging microscopy (FLIM) can detect Fӧrster resonance energy transfer (FRET) to measure protein-protein interactions in live cells. Traditional FLIM-FRET uses relative intensities to represent protein expression, consequently
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3882eb55242b985bb0f537024ad6625c
https://doi.org/10.21203/rs.3.pex-1354/v1
https://doi.org/10.21203/rs.3.pex-1354/v1
Autor:
Elizabeth J. Osterlund, Nehad Hirmiz, James M. Pemberton, Adrien Nougarède, Qian Liu, Brian Leber, Qiyin Fang, David W. Andrews
Publikováno v:
Science Advances. 8
Cytoplasmic and membrane-bound BCL-2 family proteins regulate apoptosis, a form of programmed cell death, via dozens of binary protein interactions confounding measurement of the effects of inhibitors in live cells. In cancer, apoptosis is frequently
Autor:
Elizabeth J. Osterlund, Nehad Hirmiz, Dang Nguyen, James M. Pemberton, Qiyin Fang, David W. Andrews
Publikováno v:
Journal of Biological Chemistry. 299:102863
The pro-apoptotic BH3-only endoplasmic reticulum (ER) resident protein BIK, positively regulates mitochondrial outer membrane permeabilization (MOMP), the point-of-no-return in apoptosis. It is generally accepted that BIK functions at a distance from
Autor:
David W. Andrews, Jialing Lin, Qian Liu, Dang Nguyen, Xiaoke Chi, Hetal Brahmbhatt, James M. Pemberton, Brian Leber, Zhi Zhang, Elizabeth J Osterlund
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e5d9195bdd01553fa821926258cef26
https://doi.org/10.7554/elife.44525.sa2
https://doi.org/10.7554/elife.44525.sa2
Publikováno v:
Cell Death and Differentiation
The BCL-2 family of proteins controls cell death primarily by direct binding interactions that regulate mitochondrial outer membrane permeabilization (MOMP) leading to the irreversible release of intermembrane space proteins, subsequent caspase activ