Literature DB >> 15980596

X-ray diffraction studies of amyloid structure.

O Sumner Makin1, Louise C Serpell.   

Abstract

Elucidation of the underlying core structure of amyloid fibrils is essential for understanding the mechanism by which amyloid fibrils are formed and deposited. Conventional methods of X-ray crystallography and NMR cannot be used, since the fibers are insoluble and heterogeneous. X-ray fiber diffraction is one method that has been successfully used to examine the structure of these insoluble fibers. The procedure involves the formation of suitable, ordered amyloid fibrils and characterization (by electron microscopy), partial alignment of fibers, X-ray data collection, data analysis, and finally, model building.

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Year:  2005        PMID: 15980596     DOI: 10.1385/1-59259-874-9:067

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  18 in total

1.  Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature.

Authors:  Zhuqiu Ye; Diane Bayron Poueymiroy; J Javier Aguilera; Saipraveen Srinivasan; Yun Wang; Louise C Serpell; Wilfredo Colón
Journal:  Biochemistry       Date:  2011-10-05       Impact factor: 3.162

2.  Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.

Authors:  Luciana Esposito; Carlo Pedone; Luigi Vitagliano
Journal:  Proc Natl Acad Sci U S A       Date:  2006-07-24       Impact factor: 11.205

Review 3.  Nanotools for megaproblems: probing protein misfolding diseases using nanomedicine modus operandi.

Authors:  Vladimir N Uversky; Alexander V Kabanov; Yuri L Lyubchenko
Journal:  J Proteome Res       Date:  2006-10       Impact factor: 4.466

4.  What determines the structure and stability of KFFE monomers, dimers, and protofibrils?

Authors:  Giovanni Bellesia; Joan-Emma Shea
Journal:  Biophys J       Date:  2009-02       Impact factor: 4.033

Review 5.  Structural basis of infectious and non-infectious amyloids.

Authors:  Ulrich Baxa
Journal:  Curr Alzheimer Res       Date:  2008-06       Impact factor: 3.498

Review 6.  Protein folding and aggregation in bacteria.

Authors:  Raimon Sabate; Natalia S de Groot; Salvador Ventura
Journal:  Cell Mol Life Sci       Date:  2010-04-01       Impact factor: 9.261

7.  sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.

Authors:  Natalya S Katina; Vitalii A Balobanov; Nelly B Ilyina; Victor D Vasiliev; Victor V Marchenkov; Anatoly S Glukhov; Alexey D Nikulin; Valentina E Bychkova
Journal:  Biophys J       Date:  2017-09-05       Impact factor: 4.033

8.  Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation.

Authors:  Minglei Zhao; Duilio Cascio; Michael R Sawaya; David Eisenberg
Journal:  Protein Sci       Date:  2011-05-03       Impact factor: 6.725

9.  Existence of different structural intermediates on the fibrillation pathway of human serum albumin.

Authors:  Josué Juárez; Pablo Taboada; Víctor Mosquera
Journal:  Biophys J       Date:  2009-03-18       Impact factor: 4.033

10.  Molecular modeling to investigate the binding of Congo red toward GNNQQNY protofibril and in silico virtual screening for the identification of new aggregation inhibitors.

Authors:  Jian-Hua Zhao; Hsuan-Liang Liu; Pavadai Elumalai; Wei-Hsi Chen; Lee-Chung Men; Kung-Tien Liu
Journal:  J Mol Model       Date:  2012-07-27       Impact factor: 1.810

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