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

Structural basis for the Trembler-J phenotype of Charcot-Marie-Tooth disease.

Structure (London, England : 1993) - 10 Aug 2011

Sakakura Masayoshi, Hadziselimovic Arina, Wang Zhen, Schey Kevin L, Sanders Charles R

Abstract excerpt

Mutations in peripheral myelin protein 22 (PMP22) can result in the common peripheral neuropathy Charcot-Marie-Tooth disease (CMTD). The Leu16Pro mutation in PMP22 results in misassembly of the protein, which causes the Trembler-J (TrJ) disease phenotype. Here we elucidate the structural defects...

Read the complete abstract on PubMed

Topics

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

Share to Charcot-Marie-Tooth Disease
Share to Circular Dichroism
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Myelin Proteins

Share to Protein Folding

Share to Protein Stability

Share to Proteolysis

Source

Open in PubMed Open full text

Identifiers

PMID: 21827951
DOI: 10.1016/j.str.2011.05.009
PMCID: PMC3154623

Genes

PMP22

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21827951-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for the Trembler-J phenotype of Charcot-Marie-Tooth disease.PMID 21827951Read ↗

Conformational changes associated with L16P and T118M mutations in the membrane-embedded PMP22 protein, consequential in CMT-1A.Semantic proximity Read ↗

How T118M peripheral myelin protein 22 predisposes humans to Charcot-Marie-Tooth disease.Semantic proximity Read ↗

Peripheral myelin protein 22 alters membrane architecture.Semantic proximity Read ↗

Navigating the Landscape of CMT1B: Understanding Genetic Pathways, Disease Models, and Potential Therapeutic Approaches.Semantic proximity Read ↗

Many facets of the peripheral myelin protein PMP22 in myelination and disease.Semantic proximity Read ↗

Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and DiseaseSemantic proximity Read ↗

Transport of Trembler-J mutant peripheral myelin protein 22 is blocked in the intermediate compartment and affects the transport of the wild-type protein by direct interaction.Semantic proximity Read ↗

The homology model of PMP22 suggests mutations resulting in peripheral neuropathy disrupt transmembrane helix packing.Semantic proximity Read ↗

Disrupting the transmembrane domain interface between PMP22 and MPZ causes peripheral neuropathySemantic proximity Read ↗

Charcot-Marie-Tooth disease type 1E: Clinical Natural History and Molecular Impact of <i>PMP22</i> VariantsSemantic proximity Read ↗

Human myelin protein P2: From crystallography to time-lapse membrane imaging and neuropathy-associated variantsSemantic proximity Read ↗

Structural insights into Charcot-Marie-Tooth disease-linked mutations in human GDAP1.Semantic proximity Read ↗

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