Author

Carmen Aragón

Consejo Superior de Investigaciones Científicas

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Neuroscience· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:mouse· 1 Organism:rat· 1 Organism:zebrafish· 1

Frequent Co-Authors

Beatriz López‐CorcueraiD· 3 shared Andrés de la Rocha‐MuñoziD· 2 shared Jaime de Juan‐SanziD· 2 shared Anjali Amrapali VishwanathiD· 1 shared Dhanasak DhanasobhoniD· 1 shared Elena MelgarejoiD· 1 shared Enrique Núñez· 1 shared Estefanía NúñeziD· 1 shared

Activity by Year

2017-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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3 shared papersNeuroscience

Beatriz López‐CorcueraORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

The presynaptic glycine transporter GlyT2 is regulated by the Hedgehog pathway in vitro and in vivo

Andrés de la Rocha‐Muñoz, Enrique Núñez, Anjali Amrapali Vishwanath, Sergio Gomez‐Lopez, Dhanasak Dhanasobhon, Nelson Rebola, Beatriz López‐Corcuera, Jaime de Juan‐Sanz, Carmen Aragón

This study identifies the Hedgehog pathway as a regulator of GlyT2 expression and transport activity in vitro and in vivo.

Communications Biology · Oct 18, 2021Peer-reviewedNeuroscience

Rescue of two trafficking-defective variants of the neuronal glycine transporter GlyT2 associated to hyperekplexia

Andrés de la Rocha‐Muñoz, Elena Melgarejo, Carmen Aragón, Beatriz López‐Corcuera

This study identifies N-arachidonoyl glycine as a compound that rescues trafficking defects in two hyperekplexia-associated GlyT2 mutants in cells and neurons.

Neuropharmacology · Mar 29, 2021Peer-reviewedNeuroscience

Ubiquitin ligase LNX1 is a major regulator of glycine recapture by the presynaptic transporter GlyT2

Estefanía Núñez, Esther Arribas-González, Beatriz López‐Corcuera, Carmen Aragón, Jaime de Juan‐Sanz

This study identifies LNX1 as an E3 ubiquitin ligase that regulates GlyT2 ubiquitination, expression, and activity, revealing a novel mechanism for controlling glycinergic neurotransmission.

bioRxiv · Dec 20, 2017 · PreprintNeuroscience