Amyloid fibrils are involved in a number of diseases and notably play a role in neurodegeneration, where they are present in plaques in the brain. Their structure determination might help in finding ways to interfere with their formation, and ultimately prevent disease, by revealing the structure-function relationship and helping to design molecules targeting initial assembly steps and further propagation. Here, we describe the different steps in NMR protocols which allowed the 3D structure...
[ASAP] Constraints on the Structure of Fibrils Formed by a Racemic Mixture of Amyloid-? Peptides from Solid-State NMR, Electron Microscopy, and Theory
Constraints on the Structure of Fibrils Formed by a Racemic Mixture of Amyloid-? Peptides from Solid-State NMR, Electron Microscopy, and Theory
Jevgenij A. Raskatov, Alejandro R. Foley, John M. Louis, Wai-Ming Yau, and Robert Tycko
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c06339/20210810/images/medium/ja1c06339_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.1c06339
http://feeds.feedburner.com/~r/acs/jacsat/~4/icEctWA9HQc
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08-11-2021 07:41 PM
[NMR paper] Solid-State-NMR-Structure-Based Inhibitor Design to Achieve Selective Inhibition of the Parallel-in-Register ?-Sheet versus Antiparallel Iowa Mutant ?-Amyloid Fibrils.
Solid-State-NMR-Structure-Based Inhibitor Design to Achieve Selective Inhibition of the Parallel-in-Register ?-Sheet versus Antiparallel Iowa Mutant ?-Amyloid Fibrils.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Solid-State-NMR-Structure-Based Inhibitor Design to Achieve Selective Inhibition of the Parallel-in-Register ?-Sheet versus Antiparallel Iowa Mutant ?-Amyloid Fibrils.
J Phys Chem B. 2017 06 08;121(22):5544-5552
Authors: Cheng Q, Qiang W
Abstract
...
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05-09-2018 02:49 AM
[NMR paper] 3D Structure Determination of Amyloid Fibrils using Solid-State NMR Spectroscopy.
3D Structure Determination of Amyloid Fibrils using Solid-State NMR Spectroscopy.
3D Structure Determination of Amyloid Fibrils using Solid-State NMR Spectroscopy.
Methods. 2018 Apr 05;:
Authors: Loquet A, El Mammeri N, Stanek J, Berbon M, Bardiaux B, Pintacuda G, Habenstein B
Abstract
The amyloid fold is structurally characterized by a typical cross-? architecture, which is under debate to represent an energy-favourable folding state that many globular or natively unfolded proteins can adopt. Being initially solely associated...
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04-09-2018 11:12 AM
[NMR paper] Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Emerging Structural Understanding of Amyloid Fibrils by Solid-State NMR.
Trends Biochem Sci. 2017 Oct;42(10):777-787
Authors: Meier BH, Riek R, Böckmann A
Abstract
Amyloid structures at atomic resolution have remained elusive mainly because of their extensive polymorphism and because their polymeric properties have hampered...
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10-12-2017 02:58 PM
[NMR paper] Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Acc Chem Res. 2013 May 10;
Authors: Tang M, Comellas G, Rienstra CM
Abstract
Solid-state NMR (SSNMR) spectroscopy has become an important technique for studying the biophysics and structure biology of proteins. This technique is especially useful for insoluble membrane proteins and amyloid fibrils, which are essential for...
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[NMR paper] Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Related Articles Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Annu Rev Biophys. 2013 Mar 22;
Authors: Comellas G, Rienstra CM
Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable...
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Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Sudhakar Parthasarathy, Fei Long, Yifat Miller, Yiling Xiao, Dan McElheny, Kent Thurber, Buyong Ma, Ruth Nussinov and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1072178/aop/images/medium/ja-2010-072178_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1072178
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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02-22-2011 11:06 PM
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
J Am Chem Soc. 2010 Oct 6;132(39):13765-75
Authors: Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH
We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s...