Literature DB >> 28963701

Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.

Paolo Arosio1.   

Abstract

An increasing amount of findings suggests that the aggregation of soluble peptides and proteins into amyloid fibrils is a relevant upstream process in the complex cascade of events leading to the pathology of Alzheimer's disease and several other neurodegenerative disorders. Nevertheless, several aspects of the correlation between the aggregation process and the onset and development of the pathology remain largely elusive. In this context, biophysical and biochemical studies in test tubes have proven extremely powerful in providing quantitative information about the structure and the reactivity of amyloids at the molecular level. In this review we use selected recent examples to illustrate the importance of such biophysical research to complement phenomenological studies based on cellular and molecular biology, and we discuss the implications for pharmaceutical applications associated with Alzheimer's disease and other neurodegenerative disorders in both academic and industrial contexts.

Entities:  

Keywords:  alzheimer's disease; amyloids; chemical kinetics; drug discovery; protein aggregation

Mesh:

Substances:

Year:  2017        PMID: 28963701     DOI: 10.1007/s11095-017-2266-4

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.200


  96 in total

Review 1.  Protein misfolding and disease: from the test tube to the organism.

Authors:  Leila M Luheshi; Damian C Crowther; Christopher M Dobson
Journal:  Curr Opin Chem Biol       Date:  2008-03-18       Impact factor: 8.822

2.  An analytical solution to the kinetics of breakable filament assembly.

Authors:  Tuomas P J Knowles; Christopher A Waudby; Glyn L Devlin; Samuel I A Cohen; Adriano Aguzzi; Michele Vendruscolo; Eugene M Terentjev; Mark E Welland; Christopher M Dobson
Journal:  Science       Date:  2009-12-11       Impact factor: 47.728

3.  Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease.

Authors:  Johnny Habchi; Sean Chia; Ryan Limbocker; Benedetta Mannini; Minkoo Ahn; Michele Perni; Oskar Hansson; Paolo Arosio; Janet R Kumita; Pavan Kumar Challa; Samuel I A Cohen; Sara Linse; Christopher M Dobson; Tuomas P J Knowles; Michele Vendruscolo
Journal:  Proc Natl Acad Sci U S A       Date:  2016-12-23       Impact factor: 11.205

4.  Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated.

Authors:  Ravindra Kodali; Angela D Williams; Saketh Chemuru; Ronald Wetzel
Journal:  J Mol Biol       Date:  2010-06-18       Impact factor: 5.469

Review 5.  Therapeutic strategies for human amyloid diseases.

Authors:  James C Sacchettini; Jeffery W Kelly
Journal:  Nat Rev Drug Discov       Date:  2002-04       Impact factor: 84.694

6.  Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.

Authors:  Georg Meisl; Xiaoting Yang; Erik Hellstrand; Birgitta Frohm; Julius B Kirkegaard; Samuel I A Cohen; Christopher M Dobson; Sara Linse; Tuomas P J Knowles
Journal:  Proc Natl Acad Sci U S A       Date:  2014-06-17       Impact factor: 11.205

7.  AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.

Authors:  Oscar Conchillo-Solé; Natalia S de Groot; Francesc X Avilés; Josep Vendrell; Xavier Daura; Salvador Ventura
Journal:  BMC Bioinformatics       Date:  2007-02-27       Impact factor: 3.169

8.  Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons.

Authors:  Dorothea Pinotsi; Claire H Michel; Alexander K Buell; Romain F Laine; Pierre Mahou; Christopher M Dobson; Clemens F Kaminski; Gabriele S Kaminski Schierle
Journal:  Proc Natl Acad Sci U S A       Date:  2016-03-18       Impact factor: 11.205

9.  An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.

Authors:  Johnny Habchi; Paolo Arosio; Michele Perni; Ana Rita Costa; Maho Yagi-Utsumi; Priyanka Joshi; Sean Chia; Samuel I A Cohen; Martin B D Müller; Sara Linse; Ellen A A Nollen; Christopher M Dobson; Tuomas P J Knowles; Michele Vendruscolo
Journal:  Sci Adv       Date:  2016-02-12       Impact factor: 14.136

10.  Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.

Authors:  Samuel I A Cohen; Sara Linse; Leila M Luheshi; Erik Hellstrand; Duncan A White; Luke Rajah; Daniel E Otzen; Michele Vendruscolo; Christopher M Dobson; Tuomas P J Knowles
Journal:  Proc Natl Acad Sci U S A       Date:  2013-05-23       Impact factor: 11.205

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