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Christopher N. Mayhew

Researcher at Cincinnati Children's Hospital Medical Center

Publications -  62
Citations -  6052

Christopher N. Mayhew is an academic researcher from Cincinnati Children's Hospital Medical Center. The author has contributed to research in topics: Induced pluripotent stem cell & Cell cycle. The author has an hindex of 30, co-authored 57 publications receiving 4996 citations. Previous affiliations of Christopher N. Mayhew include RMIT University & University of Cincinnati.

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Directed differentiation of human pluripotent stem cells into intestinal tissue in vitro

TL;DR: A robust and efficient process is established to direct the differentiation of human PSCs into intestinal tissue in vitro using a temporal series of growth factor manipulations to mimic embryonic intestinal development and indicates that human intestinal stem cells form de novo during development.
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Modelling human development and disease in pluripotent stem-cell-derived gastric organoids

TL;DR: The de novo generation of three-dimensional human gastric tissue in vitro through the directed differentiation of human pluripotent stem cells is reported, describing a new and robust in vitro system for elucidating the mechanisms underlying human stomach development and disease.
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In vitro generation of human pluripotent stem cell derived lung organoids

TL;DR: It is shown that HLOs are remarkably similar to human fetal lung based on global transcriptional profiles, suggesting that HL Os are an excellent model to study human lung development, maturation and disease.
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An in vivo model of human small intestine using pluripotent stem cells

TL;DR: This model of the human small intestine may pave the way for studies of intestinal physiology, disease and translational studies and a role for circulating factors in the intestinal adaptive response is suggested.
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Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification.

TL;DR: It is reported that HSF1 undergoes stress-induced modification at lysine 298 by the small ubiquitin-related protein called SUMO-1, which implicates SUMO -1 modification as an important modulator of HSF 1 function in response to stress.