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 features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy.

The Journal of biological chemistry - 9 Jan 2015

Yap Thai Leong, Jiang Zhiping, Heinrich Frank, Gruschus James M, Pfefferkorn Candace M, Barros Marilia, Curtis Joseph E, Sidransky Ellen, Lee Jennifer C

Abstract excerpt

Mutations in glucocerebrosidase (GCase), the enzyme deficient in Gaucher disease, are a common genetic risk factor for the development of Parkinson disease and related disorders, implicating the role of this lysosomal hydrolase in the disease etiology. A specific physical interaction exists between the Parkinson disease-related protein α-synuclein (α-syn) and GCase both in solution and on the lipid membrane,...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Synuclein
Share to Gaucher Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucosylceramidase

Share to Lipid Bilayers

Share to Parkinson Disease

Share to Spectrometry, Fluorescence

Share to Surface Plasmon Resonance

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 25429104
DOI: 10.1074/jbc.M114.610584
PMCID: PMC4295019

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy.PMID 25429104Read ↗

Glucocerebrosidase rescues alpha-synuclein from amyloid formationSemantic proximity Read ↗

Alpha-synuclein and familial variants affect the chain order and the thermotropic phase behavior of anionic lipid vesicles.Semantic proximity Read ↗

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers.Semantic proximity Read ↗

Saposin C protects glucocerebrosidase against α-synuclein inhibition.Semantic proximity Read ↗

Unfolding Sequence-Specific Enigma in Monomeric α-Synuclein: Implications for Parkinson's Disease.Semantic proximity Read ↗

The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than millisecondsSemantic proximity Read ↗

α-Synuclein insertion into supported lipid bilayers as seen by in situ X-ray reflectivity.Semantic proximity Read ↗

Interaction of Alpha-Synuclein and Its Mutants with Rigid Lipid Vesicle Mimics of Varying Surface Curvature.Semantic proximity Read ↗

High-resolution NMR spectroscopy of proteins in intact mitochondriaSemantic proximity Read ↗

Interaction of alpha-synuclein with lipids.Semantic proximity Read ↗

Membrane Interactions of α-Synuclein Revealed by Multiscale Molecular Dynamics Simulations, Markov State Models, and NMRSemantic proximity Read ↗

Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains.Semantic proximity Read ↗

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