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Article

A cytoplasmic dynein tail mutation impairs motor processivity.

Nature cell biology - 1 Dec 2010

Ori-McKenney Kassandra M, Xu Jing, Gross Steven P, Vallee Richard B

Abstract excerpt

Mutations in the tail of the cytoplasmic dynein molecule have been reported to cause neurodegenerative disease in mice. The mutant mouse strain Legs at odd angles (Loa) has impaired retrograde axonal transport, but the molecular deficiencies in the mutant dynein molecule, and how they contribute...

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Identifiers

PMID: 21102439
DOI: 10.1038/ncb2127
PMCID: PMC3385513

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21102439-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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A cytoplasmic dynein tail mutation impairs motor processivity.PMID 21102439Read ↗

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The legs at odd angles (Loa) mutation in cytoplasmic dynein ameliorates mitochondrial function in SOD1G93A mouse model for motor neuron disease.Semantic proximity Read ↗

A mutation in dynein rescues axonal transport defects and extends the life span of ALS mice.Semantic proximity Read ↗

DYNC1H1 mutation alters transport kinetics and ERK1/2-cFos signalling in a mouse model of distal spinal muscular atrophy.Semantic proximity Read ↗

A point mutation in the dynein heavy chain gene leads to striatal atrophy and compromises neurite outgrowth of striatal neuronsSemantic proximity Read ↗

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