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

ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its β-sandwich fold into lipid-interacting helical conformations.

Biochemical and biophysical research communications - 15 Feb 2013

Qin Haina, Wang Wei, Song Jianxing

Abstract excerpt

P56S mutation on VAPB MSP domain causes a familial ALS, characteristic of severe aggregation both in vivo and in vitro. We previously showed that P56S rendered the MSP domain to be predominantly disordered in water. Unexpectedly, here we reveal that P56S-MSP transforms into a highly helical conformation in a membrane environment. This chameleon transformation is shared by a splicing variant VAPB-3 with a...

Read the complete abstract on PubMed

Topics

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

Share to Alternative Splicing
Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cloning, Molecular

Share to Lipids

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Vesicular Transport Proteins

Source

Identifiers

PMID: 23333387
DOI: 10.1016/j.bbrc.2013.01.039

Genes

VAPB

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its β-sandwich fold into lipid-interacting helical conformations.PMID 23333387Read ↗

Elimination of the Native Structure and Solubility of the hVAPB MSP Domain by the Pro56Ser Mutation That Causes Amyotrophic Lateral SclerosisSemantic proximity Read ↗

Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesSemantic proximity Read ↗

A mutation in human VAP-B--MSP domain, present in ALS patients, affects the interaction with other cellular proteins.Semantic proximity Read ↗

Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulations.Semantic proximity Read ↗

Human VAPA and the yeast VAP Scs2p with an altered proline distribution can phenocopy amyotrophic lateral sclerosis-associated VAPB(P56S).Semantic proximity Read ↗

The amyotrophic lateral sclerosis 8 protein, VAP, is required for ER protein quality control.Semantic proximity Read ↗

A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum.Semantic proximity Read ↗

Secretion of endoplasmic reticulum protein VAPB/ALS8 requires topological inversion.Semantic proximity Read ↗

Beyond Static Tethering at Membrane Contact Sites: Structural Dynamics and Functional Implications of VAP ProteinsSemantic proximity Read ↗

Neuro-glial lipid imbalance in a <i>Drosophila</i> model of Amyotrophic Lateral Sclerosis 8Semantic proximity Read ↗

Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8).Semantic proximity Read ↗

Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies.Semantic proximity Read ↗

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