[NMR paper] NMR analysis of the correlation of metabolic changes in blood and cerebrospinal fluid in Alzheimer model male and female mice
NMR analysis of the correlation of metabolic changes in blood and cerebrospinal fluid in Alzheimer model male and female mice
The development of effective therapies as well as early, molecular diagnosis of Alzheimer's disease is impeded by the lack of understanding of the underlying pathological mechanisms. Metabolomics studies of body fluids as well as brain tissues have shown major changes in metabolic profiles of Alzheimer's patients. However, with analysis performed at the late stages of the disease it is not possible to distinguish causes and consequence. The mouse model APP/PS1...
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05-11-2021 08:10 AM
[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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03-16-2021 06:18 AM
[ASAP] Comparative Analysis of the Conformation, Aggregation, Interaction, and Fibril Morphologies of Human a-, ß-, and ?-Synuclein Proteins
Comparative Analysis of the Conformation, Aggregation, Interaction, and Fibril Morphologies of Human a-, ß-, and ?-Synuclein Proteins
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00343/20180612/images/medium/bi-2018-00343q_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00343
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/TOjFPcISiQs
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06-13-2018 05:09 PM
Magic angle spinning NMR below 6 K with a computational fluid dynamics analysis of fluid flow and temperature gradients
From The DNP-NMR Blog:
Magic angle spinning NMR below 6 K with a computational fluid dynamics analysis of fluid flow and temperature gradients
This article is not specifically about DNP spectroscopy. However, magic angle spinning at 6K is definitely of interest to DNP, especially when using low-power, solid-state microwave sources.
Sesti, E.L., et al., Magic angle spinning NMR below 6 K with a computational fluid dynamics analysis of fluid flow and temperature gradients. J. Magn. Reson., 2018. 286(Supplement C): p. 1-9.
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01-17-2018 07:00 PM
Upcoming Webinar Fluid Business: Could â??Liquidâ?? Protein Herald Neurodegeneration? - Alzforum
Upcoming Webinar Fluid Business: Could â??Liquidâ?? Protein Herald Neurodegeneration? - Alzforum
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Upcoming Webinar Fluid Business: Could â??Liquidâ?? Protein Herald Neurodegeneration?
Alzforum
Paul Taylor and colleagues recently reported that the amyotrophic lateral sclerosis (ALS)-linked protein hnRNPA1 condenses into liquid droplets to promote assembly of stress granules. In another study, Nicolas Fawzi and colleagues detail the structure ...
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10-09-2015 04:49 PM
[NMR paper] A molecular dynamics simulations-based interpretation of NMR multidimensional heteronuclear spectra of alpha-synuclein/dopamine adducts.
A molecular dynamics simulations-based interpretation of NMR multidimensional heteronuclear spectra of alpha-synuclein/dopamine adducts.
Related Articles A molecular dynamics simulations-based interpretation of NMR multidimensional heteronuclear spectra of alpha-synuclein/dopamine adducts.
Biochemistry. 2013 Aug 21;
Authors: Dibenedetto D, Rossetti G, Caliandro R, Carloni P
Abstract
Multidimensional heteronuclear NMR spectroscopy provides valuable structural information on adducts between naturally unfolded proteins and their ligands....
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08-24-2013 04:53 PM
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Structures Behind the Amyloid Aggregation of ?-Synuclein: An NMR Based Approach.
Curr Protein Pept Sci. 2011 Feb 24;
Authors: Orcellet ML, Fernández CO
The misfolding of proteins into a toxic conformation is proposed to be at the molecular foundation of a number of neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Evidence that ?-synuclein amyloidogenesis plays a causative role in the development of Parkinson's disease is furnished by a...
Cerebrospinal fluid lipoproteins inhibit ?-synuclein aggregation by ... - Molecular Neurodegeneration
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