[NMR paper] Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Related Articles Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Biophys Rev. 2018 May 31;:
Authors: Martial B, Lefèvre T, Auger M
Abstract
It is well established that amyloid proteins play a primary role in neurodegenerative diseases. Alzheimer's, Parkinson's, type II diabetes, and Creutzfeldt-Jakob's...
[NMR paper] Solid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein.
Solid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein.
Related Articles Solid-state NMR structure of a pathogenic fibril of full-length human ?-synuclein.
Nat Struct Mol Biol. 2016 Mar 28;
Authors: Tuttle MD, Comellas G, Nieuwkoop AJ, Covell DJ, Berthold DA, Kloepper KD, Courtney JM, Kim JK, Barclay AM, Kendall A, Wan W, Stubbs G, Schwieters CD, Lee VM, George JM, Rienstra CM
Abstract
Misfolded ?-synuclein amyloid fibrils are the principal components of Lewy bodies and neurites, hallmarks of...
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03-29-2016 04:59 PM
[NMR paper] Unlike twins: an NMR comparison of two ?-synuclein polymorphs featuring different toxicity.
Unlike twins: an NMR comparison of two ?-synuclein polymorphs featuring different toxicity.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Unlike twins: an NMR comparison of two ?-synuclein polymorphs featuring different toxicity.
PLoS One. 2014;9(3):e90659
Authors: Gath J, Bousset L, Habenstein B, Melki R, Böckmann A, Meier BH
...
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[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] Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.
Nat Protoc. 2013 Jun 27;8(7):1416-1432
Authors: Theillet FX, Rose HM, Liokatis S, Binolfi A, Thongwichian R, Stuiver M, Selenko P
Abstract
We outline NMR protocols for site-specific mapping and time-resolved monitoring of...
?-Synuclein phosphorylation at serine 129 occurs after initial protein deposition and inhibits seeded fibril formation and toxicity - pnas.org
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