scispace - formally typeset
J

Judith A. Steen

Researcher at Boston Children's Hospital

Publications -  73
Citations -  6117

Judith A. Steen is an academic researcher from Boston Children's Hospital. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 31, co-authored 62 publications receiving 5227 citations. Previous affiliations of Judith A. Steen include Harvard University & Interdisciplinary Center for Scientific Computing.

Papers
More filters
Journal ArticleDOI

PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility

TL;DR: It is proposed that PINK1 phosphorylation of substrates triggers the subsequent action of Parkin and the proteasome, and the PINK/Parkin pathway may quarantine damaged mitochondria prior to their clearance.
Journal ArticleDOI

Brain-Specific Phosphorylation of MeCP2 Regulates Activity-Dependent Bdnf Transcription, Dendritic Growth, and Spine Maturation

TL;DR: It is shown that neuronal activity and subsequent calcium influx trigger the de novo phosphorylation of MeCP2 at serine 421 (S421) by a CaMKII-dependent mechanism, which controls the ability of Me CP2 to regulate dendritic patterning, spine morphogenesis, and the activity-dependent induction of Bdnf transcription.
Journal ArticleDOI

The Angelman Syndrome Protein Ube3A Regulates Synapse Development by Ubiquitinating Arc

TL;DR: It is found that disruption of Ube3A function in neurons leads to an increase in Arc expression and a concomitant decrease in the number of AMPA receptors at excitatory synapses, and it is proposed that this deregulation ofAMPA receptor expression at synapses may contribute to the cognitive dysfunction that occurs in Angelman Syndrome and possibly other ASDs.

The Angelman Syndrome protein Ube3A regulates synapse development by ubiquitinating arc

TL;DR: In this article, experience-driven neuronal activity induces Ube3A transcription and that it regulates excitatory synapse development by controlling the degradation of Arc, a synaptic protein that promotes the internalization of the AMPA subtype of glutamate receptors.