E
Eric H. Schroeter
Researcher at Washington University in St. Louis
Publications - 21
Citations - 8748
Eric H. Schroeter is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Notch signaling pathway & Notch proteins. The author has an hindex of 17, co-authored 21 publications receiving 8462 citations. Previous affiliations of Eric H. Schroeter include Pasteur Institute.
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Journal ArticleDOI
A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain.
Bart De Strooper,Wim Annaert,Philippe Cupers,Paul Saftig,Katleen Craessaerts,Jeff S. Mumm,Eric H. Schroeter,Vincent Schrijvers,Michael S. Wolfe,William J. Ray,Alison Goate,Raphael Kopan +11 more
TL;DR: It is reported that, in mammalian cells, PS1 deficiency also reduces the proteolytic release of NICD from a truncated Notch construct, thus identifying the specific biochemical step of the Notch signalling pathway that is affected by PS1.
Journal ArticleDOI
Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain.
TL;DR: It is shown that signalling by a constitutively active membrane-bound Notch-1 protein requires the proteolytic release of the Notch intracellular domain (NICD), which interacts preferentially with CSL.
Journal ArticleDOI
Signalling downstream of activated mammalian Notch.
Sophie Jarriault,Christel Brou,Frédérique Logeat,Eric H. Schroeter,Raphael Kopan,Alain Israël +5 more
TL;DR: It is shown that activated forms of mNotch associate with the human analogue of Su(H), KBF2/RBP-JK and act as transcriptional activators through theKBF2-binding sites of the HES-1 promoter and block MyoD-induced myogenesis5-7.
Journal ArticleDOI
A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1
Jeff S. Mumm,Eric H. Schroeter,Meera T. Saxena,Adam Griesemer,Xiaolin Tian,Duojia Pan,William J. Ray,Raphael Kopan +7 more
TL;DR: It is demonstrated that ligand binding facilitates cleavage at a novel site (S2), within the extracellular juxtamembrane region, which serves to release ectodomain repression of NICD production.
Journal ArticleDOI
Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain
TL;DR: It is demonstrated that a mNotch1 mutant protein that lacks its extracellular domain but retains its membrane-spanning region becomes proteolytically processed on its intracellular surface and, as a result, the activated intrACEllular domain (mNotchIC) is released and can move to the nucleus.