Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Coordinate control of axon defasciculation and myelination by laminin-2 and -8

7 Feb 2005

Abstract excerpt

Schwann cells form basal laminae (BLs) containing laminin-2 (Ln-2; heterotrimer alpha2beta1gamma1) and Ln-8 (alpha4beta1gamma1). Loss of Ln-2 in humans and mice carrying alpha2-chain mutations prevents developing Schwann cells from fully defasciculating axons, resulting in partial amyelination. The principal pathogenic mechanism is thought to derive from structural defects in Schwann cell BLs, which Ln-2...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Adhesion Molecules Research
Share to Galectins and Cancer Biology
Share to Signaling Pathways in Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15699217
DOI: 10.1083/jcb.200411158

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Coordinate control of axon defasciculation and myelination by laminin-2 and -8PMID 15699217Read ↗

LAMA2 Neuropathies: Human Findings and Pathomechanisms From Mouse ModelsSemantic proximity Read ↗

Laminin is required for Schwann cell morphogenesis.Semantic proximity Read ↗

Integrin-linked kinase is required for laminin-2-induced oligodendrocyte cell spreading and CNS myelination.Semantic proximity Read ↗

Peripheral myelin protein 22 is in complex with alpha6beta4 integrin, and its absence alters the Schwann cell basal lamina.Semantic proximity Read ↗

Laminin-deficient muscular dystrophy: Molecular pathogenesis and structural repair strategies.Semantic proximity Read ↗

Laminin isoforms in development and disease.Semantic proximity Read ↗

The Neurobiology of Schwann CellsSemantic proximity Read ↗

The extracellular matrix protein laminin α2 regulates the maturation and function of the blood-brain barrier.Semantic proximity Read ↗

Schwann cell-specific ablation of laminin gamma1 causes apoptosis and prevents proliferation.Semantic proximity Read ↗

Laminin Polymerization and Inherited Disease: Lessons From GeneticsSemantic proximity Read ↗

Laminins and human disease.Semantic proximity Read ↗

A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.