Enhancers with cooperative Notch binding sites are more resistant to regulation by the Hairless co-repressor

Autor: Brian Gebelein, Ellen K. Gagliani, Raphael Kopan, Natanel Eafergan, Rhett A. Kovall, Yi Kuang, Matthew T. Weirauch, Anna Pyo, Brittany Cain, Lisa M. Gutzwiller, Ofri Axelrod, David Sprinzak

Publikováno v: PLoS Genetics, Vol 17, Iss 9, p e1009039 (2021)
PLoS Genetics

Notch signaling controls many developmental processes by regulating gene expression. Notch-dependent enhancers recruit activation complexes consisting of the Notch intracellular domain, the Cbf/Su(H)/Lag1 (CSL) transcription factor (TF), and the Mast

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de114790586f27d05d91e1e85e0921ad
https://doaj.org/article/46e826c091ea4d9db920f08826b85963

Side-by-side comparison of Notch- and C83 binding to γ-secretase in a complete membrane model at physiological temperature

Autor: Kasper Planeta Kepp, Ning Tang, Budheswar Dehury, Tom L. Blundell, Rukmankesh Mehra

Publikováno v: Dehury, B, Tang, N, Mehra, R, Blundell, T L & Kepp, K P 2020, ' Side-by-side comparison of Notch-And C83 binding to γ-secretase in a complete membrane model at physiological temperature ', RSC Advances, vol. 10, no. 52, pp. 31215-31232 . https://doi.org/10.1039/d0ra04683c

γ-Secretase cleaves the C99 fragment of the amyloid precursor protein, leading to formation of aggregated β-amyloid peptide central to Alzheimer's disease, and Notch, essential for cell regulation. Recent cryogenic electron microscopy (cryo-EM) str

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a80622a1751d918d4e41d58eda0d028d
https://pubmed.ncbi.nlm.nih.gov/35520661

Inhibition of Delta-induced Notch signaling using fucose analogs

Autor: Huilin Hao, Lars Ulrik Nordstrøm, Hideyuki Takeuchi, Robert S. Haltiwanger, Michael Schneider, Vincent C. Luca, Vivek Kumar, Peng Wu, Lei Feng, K. Christopher Garcia, Pamela Stanley

Publikováno v: Nature Chemical Biology. 14:65-71

Notch is a cell-surface receptor that controls cell-fate decisions and is regulated by O-glycans attached to epidermal growth factor-like (EGF) repeats in its extracellular domain. Protein O-fucosyltransferase 1 (Pofut1) modifies EGF repeats with O-f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c72cb1993955dfd8fc92e8ed7fa6021
https://doi.org/10.1038/nchembio.2520

Membrane dynamics of Notch-bound γ-secretase produces two distinct Notch conformations

Autor: Budheswar Dehury, Kasper Planeta Kepp, Ning Tang

Cleavage of Notch by the major intramembrane aspartyl protease complex γ-secretase is a central event in cell regulation and is also important to Alzheimer’s disease, with more than 200 mutations in the catalytic subunit of γ-secretase (PS1) caus

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e557562023e50a9fc4b83651dbbcf95

Enhanced Delta-Notch Lateral Inhibition Model Incorporating Intracellular Notch Heterogeneity and Tension-Dependent Rate of Delta-Notch Binding that Reproduces Sprouting Angiogenesis Patterns

Autor: Yen Ling Koon, Songjing Zhang, Keng-Hwee Chiam, Cheng-Gee Koh, Muhammad Bakhait Rahmat

Publikováno v: Scientific Reports, Vol 8, Iss 1, Pp 1-15 (2018)
Scientific Reports

Endothelial cells adopt unique cell fates during sprouting angiogenesis, differentiating into tip or stalk cells. The fate selection process is directed by Delta-Notch lateral inhibition pathway. Classical Delta-Notch models produce a spatial pattern

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::723e39d1557f326b22c5feac50315cea
https://doi.org/10.1038/s41598-018-27645-1