Literature DB >> 16515454

Amyloid under the atomic force microscope.

Walraj S Gosal1, Sarah L Myers, Sheena E Radford, Neil H Thomson.   

Abstract

The atomic force microscope (AFM) is a versatile instrument that can be used to image biological samples at nanometre resolution as well as to measure inter and intra-molecular forces in air and liquid environments. This review summarises the use of AFM applied to protein and peptide self-assembly systems involved in amyloid formation. The technical principles of the AFM are outlined and its advantages and disadvantages are highlighted and discussed in the context of the rapidly developing field of amyloid research.

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Year:  2006        PMID: 16515454     DOI: 10.2174/092986606775338498

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  11 in total

1.  Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry.

Authors:  Camelia Vlad; Kathrin Lindner; Christiaan Karreman; Stefan Schildknecht; Marcel Leist; Nick Tomczyk; John Rontree; James Langridge; Karin Danzer; Thomas Ciossek; Alina Petre; Michael L Gross; Bastian Hengerer; Michael Przybylski
Journal:  Chembiochem       Date:  2011-11-07       Impact factor: 3.164

2.  Mass spectrometry and the amyloid problem--how far can we go in the gas phase?

Authors:  Alison E Ashcroft
Journal:  J Am Soc Mass Spectrom       Date:  2010-03-09       Impact factor: 3.109

3.  Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation.

Authors:  Joshua T Berryman; Sheena E Radford; Sarah A Harris
Journal:  Biophys J       Date:  2009-07-08       Impact factor: 4.033

4.  Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.

Authors:  David P Smith; Lucy A Woods; Sheena E Radford; Alison E Ashcroft
Journal:  Biophys J       Date:  2011-09-07       Impact factor: 4.033

5.  Ubiquilin-1 is a molecular chaperone for the amyloid precursor protein.

Authors:  Emily S Stieren; Amina El Ayadi; Yao Xiao; Efraín Siller; Megan L Landsverk; Andres F Oberhauser; José M Barral; Darren Boehning
Journal:  J Biol Chem       Date:  2011-08-18       Impact factor: 5.157

6.  Role of small oligomers on the amyloidogenic aggregation free-energy landscape.

Authors:  Xianglan He; Jason T Giurleo; David S Talaga
Journal:  J Mol Biol       Date:  2009-10-27       Impact factor: 5.469

Review 7.  Folding versus aggregation: polypeptide conformations on competing pathways.

Authors:  Thomas R Jahn; Sheena E Radford
Journal:  Arch Biochem Biophys       Date:  2007-06-08       Impact factor: 4.013

8.  Purification and aggregation of the amyloid precursor protein intracellular domain.

Authors:  Amina El Ayadi; Emily S Stieren; José M Barral; Andres F Oberhauser; Darren Boehning
Journal:  J Vis Exp       Date:  2012-08-28       Impact factor: 1.355

9.  Ultrasonic force microscopy for nanomechanical characterization of early and late-stage amyloid-β peptide aggregation.

Authors:  Claire Tinker-Mill; Jennifer Mayes; David Allsop; Oleg V Kolosov
Journal:  Sci Rep       Date:  2014-02-06       Impact factor: 4.379

10.  Surface effects mediate self-assembly of amyloid-β peptides.

Authors:  Yi-Chih Lin; E James Petersson; Zahra Fakhraai
Journal:  ACS Nano       Date:  2014-09-24       Impact factor: 15.881

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