[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] Mechanisms of amyloid formation revealed by solution NMR.
Mechanisms of amyloid formation revealed by solution NMR.
Related Articles Mechanisms of amyloid formation revealed by solution NMR.
Prog Nucl Magn Reson Spectrosc. 2015 Aug;88-89:86-104
Authors: Karamanos TK, Kalverda AP, Thompson GS, Radford SE
Abstract
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details...
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08-19-2015 03:24 PM
Mechanisms of amyloid formation revealed by solution NMR
Mechanisms of amyloid formation revealed by solution NMR
Publication date: Available online 26 May 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Theodoros K. Karamanos , Arnout P. Kalverda , Gary S. Thompson , Sheena E. Radford</br>
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. Recent advances in electron microscopy and solid state NMR have allowed the characterization of fibril structures to different extents of refinement. However, structural details about the mechanism of...
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05-28-2015 12:56 AM
[NMR paper] Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.
Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.
Chembiochem. 2013 Sep 23;14(14):1891-7
Authors: Bertini I, Gallo G, Korsak M, Luchinat C, Mao J, Ravera E
Abstract
The accumulation of soluble toxic beta-amyloid (A?)...
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04-24-2014 08:34 PM
[NMR paper] Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Phys Chem Chem Phys. 2013 Oct 21;15(39):16956-64
Authors: Itoh-Watanabe H, Kamihira-Ishijima M,...
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04-22-2014 03:54 PM
[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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03-27-2013 03:33 PM
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
J Biol Chem. 2011 Apr 20;
Authors: Iwasa H, Meshitsuka S, Hongo K, Mizobata T, Kawata Y
Co-chaperonin GroES from E. coli works with chaperonin GroEL to mediate the folding reactions of various proteins. However, under specific conditions, i. e., the...
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04-22-2011 02:00 PM
[NMR paper] Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Related Articles Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
J Biol Chem. 2004 Feb 13;279(7):5699-707
Authors: Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A
The human plasma protein transthyretin (TTR) may form fibrillar protein deposits that are associated with both inherited and idiopathic amyloidosis. The present study utilizes solution nuclear magnetic resonance spectroscopy, in combination with...
Structural Changes Associated with Transthyretin Misfoldingand Amyloid Formation Revealed by Solution and Solid-State NMR
Linear Mode
