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Aris N. Economides

Researcher at Regeneron

Publications -  207
Citations -  16298

Aris N. Economides is an academic researcher from Regeneron. The author has contributed to research in topics: Bone morphogenetic protein & Noggin. The author has an hindex of 57, co-authored 195 publications receiving 14176 citations. Previous affiliations of Aris N. Economides include University of Cantabria.

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Bone morphogenetic proteins, their antagonists, and the skeleton.

TL;DR: A large number of extracellular proteins that bind BMPs and prevent their binding to signaling receptors have emerged, indicating the existence and need of local feedback mechanisms to temper BMP cellular activities.
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Neural induction by the secreted polypeptide noggin

TL;DR: Noggin has the expression pattern and activity expected of an endogenous neural inducer and acts at the appropriate stage to be an endogenous Neural inducing signal in Xenopus.
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The Xenopus Dorsalizing Factor Gremlin Identifies a Novel Family of Secreted Proteins that Antagonize BMP Activities

TL;DR: Gremlin belongs to a novel gene family that includes the head-inducing factor Cerberus and the tumor suppressor DAN and it is proposed that Gremlin, Cerberus, and DAN control diverse processes in growth and development by selectively antagonizing the activities of different subsets of the TGF beta ligands.
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High-throughput engineering of the mouse genome coupled with high-resolution expression analysis

TL;DR: The development of a high-throughput and largely automated process that uses targeting vectors based on bacterial artificial chromosomes (BACs) that permits genetic alteration with nucleotide precision, is not limited by the size of desired deletions, does not depend on isogenicity or on positive–negative selection, and can precisely replace the gene of interest with a reporter that allows for high-resolution localization of target-gene expression.
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Structural basis of BMP signalling inhibition by the cystine knot protein Noggin

TL;DR: The crystal structure of the antagonist Noggin bound to BMP-7 is reported, which shows that Nogsgin inhibits BMP signalling by blocking the molecular interfaces of the binding epitopes for both type I and type II receptors.