S100A9 is a pro-inflammatory protein that co-aggregates with other proteins in amyloid fibril plaques. S100A9 can influence the aggregation kinetics and amyloid fibril structure of alpha-synuclein (?-syn), which is involved in Parkinson's disease. Currently, there are limited data regarding their cross-interaction and how it influences the aggregation process. In this work, we analyzed this interaction using solution 19F and 2D ^(15)N-¹H HSQC NMR spectroscopy and studied the aggregation...
[NMR paper] Membrane Interactions of alpha-Synuclein Revealed by Multiscale Molecular Dynamics Simulations, Markov State Models, and NMR
Membrane Interactions of alpha-Synuclein Revealed by Multiscale Molecular Dynamics Simulations, Markov State Models, and NMR
?-Synuclein (?S) is a presynaptic protein that binds to cell membranes and is linked to Parkinson's disease (PD). Binding of ?S to membranes is a likely first step in the molecular pathophysiology of PD. The ?S molecule can adopt multiple conformations, being largely disordered in water, adopting a ?-sheet conformation when present in amyloid fibrils, and forming a dynamic multiplicity of ?-helical conformations when bound to lipid bilayers and related...
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[NMR paper] Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Related Articles Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy.
Biomolecules. 2020 Mar 10;10(3):
Authors: Kim DH, Lee J, Mok KH, Lee JH, Han KH
Abstract
Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as the traditional...
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03-16-2020 04:59 PM
[NMR paper] Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Related Articles Ca(2+) modulating ?-synuclein membrane transient interactions revealed by solution NMR spectroscopy.
Biochim Biophys Acta. 2013 Dec 4;
Authors: Zhang Z, Dai C, Bai J, Xu G, Liu M, Li C
Abstract
?-synuclein is involved in Parkinson's disease and its interaction with cell membrane is crucial to its pathological and physiological functions. Membrane properties, such as curvature, lipid composition have been shown to affect the...
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12-10-2013 05:36 PM
[NMR paper] Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
PLoS One. 2013;8(9):e75018
Authors: Kang L, Janowska MK, Moriarty GM, Baum J
Abstract
Aggregation of ?-synuclein (?Syn), the primary protein component in Lewy body inclusions of patients with Parkinson's disease, arises when the normally soluble intrinsically...
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09-24-2013 10:18 AM
[NMR paper] Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
PLoS One. 2013;8(1):e53487
Authors: ...
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[NMR paper] Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble
Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
Related Articles Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
J Am Chem Soc. 2005 Jan 19;127(2):476-7
Authors: Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM
The intrinsically disordered protein alpha-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of alpha-synuclein...
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11-24-2010 11:14 PM
[NMR paper] NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of i
NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.
Related Articles NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.
EMBO J. 2004 May 19;23(10):2039-46
Authors: Fernández CO, Hoyer W, Zweckstetter M, Jares-Erijman EA, Subramaniam V, Griesinger C, Jovin TM
The aggregation of alpha-synuclein is characteristic of Parkinson's disease (PD) and other neurodegenerative synucleinopathies. The 140-aa protein is natively unstructured; thus,...
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11-24-2010 09:51 PM
[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209
Authors: Carver JA, Lindner RA
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...
Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy
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