Literature DB >> 22528087

X-ray fibre diffraction studies of amyloid fibrils.

Kyle L Morris1, Louise C Serpell.   

Abstract

Amyloid fibrils are polymeric assemblies of normally soluble proteins or peptides. To investigate their structure, it is generally not possible to use conventional methods of crystallography and solution nuclear magnetic resonance. To examine the repeating crystalline structure along the fibre axis, X-ray fibre diffraction has been a useful tool. Here we discuss the methods by which amyloid-like fibrils may be prepared to form a sample suitable for structural analysis and describe how data may be collected and then analysed to arrive at a potential model structure.

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Year:  2012        PMID: 22528087     DOI: 10.1007/978-1-61779-551-0_9

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


  35 in total

1.  [Refractory pseudofollicular conjunctivitis].

Authors:  R Khatib; H Göbel; C Kurschat; C Röcken; C Cursiefen; P Steven; L M Heindl
Journal:  Ophthalmologe       Date:  2016-07       Impact factor: 1.059

Review 2.  Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.

Authors:  Jessica Nasica-Labouze; Phuong H Nguyen; Fabio Sterpone; Olivia Berthoumieu; Nicolae-Viorel Buchete; Sébastien Coté; Alfonso De Simone; Andrew J Doig; Peter Faller; Angel Garcia; Alessandro Laio; Mai Suan Li; Simone Melchionna; Normand Mousseau; Yuguang Mu; Anant Paravastu; Samuela Pasquali; David J Rosenman; Birgit Strodel; Bogdan Tarus; John H Viles; Tong Zhang; Chunyu Wang; Philippe Derreumaux
Journal:  Chem Rev       Date:  2015-03-19       Impact factor: 60.622

3.  Modulation of Amyloid-β42 Conformation by Small Molecules Through Nonspecific Binding.

Authors:  Chungwen Liang; Sergey N Savinov; Jasna Fejzo; Stephen J Eyles; Jianhan Chen
Journal:  J Chem Theory Comput       Date:  2019-09-04       Impact factor: 6.006

Review 4.  The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.

Authors:  Zahraa S Al-Garawi; Kyle L Morris; Karen E Marshall; Jutta Eichler; Louise C Serpell
Journal:  Interface Focus       Date:  2017-10-20       Impact factor: 3.906

Review 5.  Mechanical Properties and Failure of Biopolymers: Atomistic Reactions to Macroscale Response.

Authors:  GangSeob Jung; Zhao Qin; Markus J Buehler
Journal:  Top Curr Chem       Date:  2015

Review 6.  High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease.

Authors:  Bikash R Sahoo; Sarah J Cox; Ayyalusamy Ramamoorthy
Journal:  Chem Commun (Camb)       Date:  2020-04-17       Impact factor: 6.222

7.  Antiparallel β-Sheet Structure within the C-Terminal Region of 42-Residue Alzheimer's Amyloid-β Peptides When They Form 150-kDa Oligomers.

Authors:  Danting Huang; Maxwell I Zimmerman; Patricia K Martin; A Jeremy Nix; Terrone L Rosenberry; Anant K Paravastu
Journal:  J Mol Biol       Date:  2015-04-16       Impact factor: 5.469

8.  Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.

Authors:  Lothar Gremer; Daniel Schölzel; Carla Schenk; Elke Reinartz; Jörg Labahn; Raimond B G Ravelli; Markus Tusche; Carmen Lopez-Iglesias; Wolfgang Hoyer; Henrike Heise; Dieter Willbold; Gunnar F Schröder
Journal:  Science       Date:  2017-09-07       Impact factor: 47.728

Review 9.  Half a century of amyloids: past, present and future.

Authors:  Pu Chun Ke; Ruhong Zhou; Louise C Serpell; Roland Riek; Tuomas P J Knowles; Hilal A Lashuel; Ehud Gazit; Ian W Hamley; Thomas P Davis; Marcus Fändrich; Daniel Erik Otzen; Matthew R Chapman; Christopher M Dobson; David S Eisenberg; Raffaele Mezzenga
Journal:  Chem Soc Rev       Date:  2020-07-07       Impact factor: 54.564

Review 10.  Interactions in bacterial biofilm development: a structural perspective.

Authors:  James A Garnett; Steve Matthews
Journal:  Curr Protein Pept Sci       Date:  2012-12       Impact factor: 3.272

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