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Article
Open AccessImmune responses to oligomeric α-synuclein in Parkinson’s disease peripheral blood mononuclear cells
Parkinson’s disease displays clinical heterogeneity, presenting with motor and non-motor symptoms. Heterogeneous phenotypes, named brain-first and body-first, may reflect distinct α-synuclein pathology startin...
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Article
Open AccessRepurposing Pomalidomide as a Neuroprotective Drug: Efficacy in an Alpha-Synuclein-Based Model of Parkinson’s Disease
Marketed drugs for Parkinson’s disease (PD) treat disease motor symptoms but are ineffective in stop** or slowing disease progression. In the quest of novel pharmacological approaches that may target disease...
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Article
Open AccessBackbone NMR assignments of the C-terminal domain of the human prion protein and its disease‐associated T183A variant
Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders associated with the misfolding and aggregation of the human prion protein (huPrP). Despite efforts into investigating the ...
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Article
Open AccessThe docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition
α-Synuclein (αS) is a presynaptic disordered protein whose aberrant aggregation is associated with Parkinson’s disease. The functional role of αS is still debated, although it has been involved in the regulati...
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Article
Open AccessExtent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large conformational space. Certain conformations lead to aggregation prone and non-aggregation prone intermediates, but iden...
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Open AccessThe N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State
The aggregation of α-synuclein (αS), a protein abundant at presynaptic terminals, is associated with a range of highly debilitating neurodegenerative conditions, including Parkinson’s disease (PD), dementia wi...
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Article
Open AccessProbing the dynamic stalk region of the ribosome using solution NMR
We describe an NMR approach based on the measurement of residual dipolar couplings (RDCs) to probe the structural and motional properties of the dynamic regions of the ribosome. Alignment of intact 70S ribosom...
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Article
Cavitation energies can outperform dispersion interactions
The accurate dissection of binding energies into their microscopic components is challenging, especially in solution. Here we study the binding of noble gases (He–Xe) with the macrocyclic receptor cucurbit[5]u...
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Open AccessBackbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers
The HypF protein is involved in the maturation and regulation of hydrogenases. The N-terminal domain of HypF (HypF-N) has served as a key model system to study the pathways of protein amyloid formation and the...
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Article
Open AccessC-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction
Alpha-synuclein is known to bind to small unilamellar vesicles (SUVs) via its N terminus, which forms an amphipathic alpha-helix upon membrane interaction. Here we show that calcium binds to the C terminus of ...
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Article
Open AccessThe PROSECCO server for chemical shift predictions in ordered and disordered proteins
The chemical shifts measured in solution-state and solid-state nuclear magnetic resonance (NMR) are powerful probes of the structure and dynamics of protein molecules. The exploitation of chemical shifts requi...
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Open AccessCorrection: Corrigendum: Structural basis of synaptic vesicle assembly promoted by α-synuclein
Nature Communications 7: Article number: 12563 (2016); Published: 19 September 2016; Updated 11 May 2017 In the original version of Supplementary Data 1 associated with this Article, the FastPeakFind.m functio...
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Open AccessStructural basis of synaptic vesicle assembly promoted by α-synuclein
α-synuclein (αS) is an intrinsically disordered protein whose fibrillar aggregates are the major constituents of Lewy bodies in Parkinson’s disease. Although the specific function of αS is still unclear, a gen...
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Article
Open AccessStructural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity
A detailed characterisation of the molecular determinants of membrane binding by α-synuclein (αS), a 140-residue protein whose aggregation is associated with Parkinson’s disease, is of fundamental significance...
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Article
Open AccessElectrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones
Polypeptide aggregation into amyloid is linked with several debilitating human diseases. Despite the inherent risk of aggregation-induced cytotoxicity, bacteria control the export of amyloid-prone subunits and...
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Article
Open AccessAccurate Determination of Conformational Transitions in Oligomeric Membrane Proteins
The structural dynamics governing collective motions in oligomeric membrane proteins play key roles in vital biomolecular processes at cellular membranes. In this study, we present a structural refinement appr...
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Article
Open AccessThe inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments
The free energy landscape theory has been very successful in rationalizing the folding behaviour of globular proteins, as this representation provides intuitive information on the number of states involved in ...
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Article
Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour
α-synuclein (αS) is a protein involved in neurotransmitter release in presynaptic terminals, and whose aberrant aggregation is associated with Parkinson’s disease. In dopaminergic neurons, αS exists in a tight...
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Article
New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics
Residual dipolar couplings (RDCs) can provide exquisitely detailed information about the structure and dynamics of proteins. It is challenging, however, to extract such information from RDC measurements in con...
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Article
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings
Residual dipolar couplings (RDCs) have the potential of providing detailed information about the conformational fluctuations of proteins. It is very challenging, however, to extract such information because of...
