Aberrant aggregation of the transactive response DNA-binding protein (TDP-43) is associated with several lethal neurodegenerative diseases, including amyotrophic lateral sclerosis and frontotemporal dementia. Cytoplasmic neuronal inclusions of TDP-43 are enriched in various fragments of the low-complexity C-terminal domain and are associated with different neurotoxicity. Here we dissect the structural basis of TDP-43 polymorphism using magic-angle spinning solid-state NMR spectroscopy in...
[NMR paper] Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Human PrP (huPrP) is a high-affinity receptor for oligomeric amyloid-? (A?) protein aggregates. Binding of A? oligomers to membrane-anchored huPrP has been suggested to trigger neurotoxic cell signaling in Alzheimer's disease, while an N-terminal soluble fragment of huPrP can sequester A? oligomers and reduce their toxicity. Synthetic oligomeric A? species are known to be heterogeneous, dynamic and transient, rendering their structural investigation particularly...
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03-07-2021 07:38 AM
[NMR paper] Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.
Nat Commun. 2017 Sep 29;8(1):753
Authors: Theint T, Nadaud PS, Aucoin D, Helmus JJ, Pondaven SP, Surewicz K, Surewicz WK, Jaroniec CP
Abstract
One of the most puzzling aspects of the prion diseases is the intricate relationship between prion strains and interspecies transmissibility barriers....
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10-01-2017 09:32 PM
[NMR paper] Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
Structural Polymorphism of Alzheimer's ?-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
J Am Chem Soc. 2016 Jul 14;
Authors: Elkins MR, Wang T, Nick M, Jo H, Lemmin T, Prusiner SB, DeGrado WF, Stoehr J, Hong M
Abstract
The amyloid-? (A?) peptide of the Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer scale and molecular scale. Various fibril growth conditions have been...
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07-16-2016 04:54 AM
Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High ResolutionFourier Transform Ion Cyclotron Resonance Mass Spectrometry
Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High ResolutionFourier Transform Ion Cyclotron Resonance Mass Spectrometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01095/20160401/images/medium/bi-2015-01095d_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01095
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04-02-2016 09:29 AM
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00164/20160323/images/medium/bi-2016-00164v_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00164
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03-24-2016 04:18 AM
[NMR paper] Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.
Biochemistry. 2016 Mar 21;
Authors: Lim KH, Dasari AK, Hung I, Gan Z, Kelly JW, Wemmer DE
Abstract
Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural...
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03-22-2016 01:46 PM
[NMR paper] New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
FEBS J. 2014 Dec 11;
Authors: Elazari-Shalom H, Shaked H, Esteban-Martin S, Salvatella X, Barda-Saad M, Chill JH
Abstract
WASp-interacting protein (WIP) is an intrinsically disordered 503-residue polypeptide with a key role in actin polymerization in activated T cells. Its interaction with actin is mediated...
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12-17-2014 09:43 PM
[NMR paper] Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
J Biol Chem. 2014 Apr 4;289(14):9998-10010
Authors: Parthasarathy S, Yoo B, McElheny D, Tay W,...
Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR
Linear Mode
