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Article

Folding anomalies of neuroligin3 caused by a mutation in the alpha/beta-hydrolase fold domain.

Chemico-biological interactions - 6 Sept 2010

De Jaco Antonella, Dubi Noga, Comoletti Davide, Taylor Palmer

Abstract excerpt

Proteins of the alpha/beta-hydrolase fold family share a common structural fold, but perform a diverse set of functions. We have been studying natural mutations occurring in association with congenital disorders in the alpha/beta-hydrolase fold domain of neuroligin (NLGN), butyrylcholinesterase (BChE), acetylcholinesterase (AChE). Starting from the autism-related R451C mutation in the alpha/beta-hydrolase fold...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 20227402
DOI: 10.1016/j.cbi.2010.03.012
PMCID: PMC5582339

Genes

NLGN3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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