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Article

ALS-causing mutations in profilin-1 alter its conformational dynamics: A computational approach to explain propensity for aggregation.

Scientific reports - 30 Aug 2018

Kiaei Mahmoud, Balasubramaniam Meenakshisundaram, Govind Kumar Vivek, Shmookler Reis Robert J, Moradi Mahmoud, Varughese Kottayil I

Abstract excerpt

Profilin-1 (PFN1) is a 140-amino-acid protein with two distinct binding sites-one for actin and one for poly-L-proline (PLP). The best-described function of PFN1 is to catalyze actin elongation and polymerization. Thus far, eight DNA mutations in the PFN1 gene encoding the PFN1 protein are associated with human amyotrophic lateral sclerosis (ALS). We and others recently showed that two of these mutations...

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Source

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Identifiers

PMID: 30166578
DOI: 10.1038/s41598-018-31199-7
PMCID: PMC6117255

Genes

PFN1

Variants

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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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