Special Issue "Protein Aggregation"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology".

Deadline for manuscript submissions: closed (30 November 2011)

Special Issue Editor

Guest Editor
Prof. Dr. Ludmilla A. Morozova-Roche
Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, SE 90781, Sweden
Website: http://www.medchem.umu.se/english/research/principal-investigators/morozova-roche/
E-Mail: ludmilla.morozova-roche@medchem.umu.se
Phone: +46907865283
Fax: +46 90 786 9795
Interests: amyloid; protein folding; neurodegeneration; inflammation; amyloid diseases

Special Issue Information

Dear Colleagues,

Protein aggregation is the most common and problematic manifestation of protein instability encountered during all stages of protein purification and applications. The formation of unstructured aggregates effectively reduces the quantity of functional compounds in solutions. If protein aggregates are not eliminated by clearance mechanisms from the body, the accumulation of protein deposits is associated with growing number of protein conformational diseases. Among proteins aggregates the structured aggregation involving the formation of cross-beta-sheet containing amyloid fibrils and oligomers received particular attention being a leading course of age-related degenerative amyloid diseases. Evidence accumulated that in some cases the regulated protein aggregation can fulfill useful functions of polypeptide storage or sequestration and minimization of diffusion of highly reactive and toxic species. As a result the protein aggregation became the central theme of much current research aimed at understanding the mechanisms underlying this process and measures increasing proteins stability and reducing the propensity of the spontaneous and often undesirable aggregation. Here we present the collection of articles presenting the broad overview of the state of this rapidly developing field and the challenges met by using current knowledge of the mechanisms of protein molecular assemblies and stability.

Prof. Dr. Ludmilla A. Morozova-Roche
Guest Editor

Keywords

  • protein aggregation
  • amyloid formation
  • self-assembly
  • stability
  • conformational plasticity
  • nucleation
  • inhibition

Published Papers (8 papers)

Int. J. Mol. Sci. 2012, 13(3), 3801-3819; doi:10.3390/ijms13033801
Received: 9 February 2012; in revised form: 10 March 2012 / Accepted: 13 March 2012 / Published: 21 March 2012
Show/Hide Abstract | Cited by 6 | PDF Full-text (413 KB) | HTML Full-text | XML Full-text

Int. J. Mol. Sci. 2012, 13(3), 3038-3072; doi:10.3390/ijms13033038
Received: 20 December 2011; in revised form: 9 February 2012 / Accepted: 23 February 2012 / Published: 7 March 2012
Show/Hide Abstract | Cited by 11 | PDF Full-text (1511 KB) | HTML Full-text | XML Full-text

Int. J. Mol. Sci. 2012, 13(3), 2893-2917; doi:10.3390/ijms13032893
Received: 9 January 2012; in revised form: 21 February 2012 / Accepted: 22 February 2012 / Published: 5 March 2012
Show/Hide Abstract | Cited by 7 | PDF Full-text (704 KB) | HTML Full-text | XML Full-text

Int. J. Mol. Sci. 2012, 13(2), 1461-1480; doi:10.3390/ijms13021461
Received: 16 November 2011; in revised form: 11 January 2012 / Accepted: 13 January 2012 / Published: 1 February 2012
Show/Hide Abstract | Cited by 3 | PDF Full-text (528 KB) | HTML Full-text | XML Full-text

Int. J. Mol. Sci. 2011, 12(12), 9369-9388; doi:10.3390/ijms12129369
Received: 22 October 2011; in revised form: 6 December 2011 / Accepted: 12 December 2011 / Published: 14 December 2011
Show/Hide Abstract | Cited by 2 | PDF Full-text (621 KB) | HTML Full-text | XML Full-text | Supplementary Files

Int. J. Mol. Sci. 2011, 12(12), 9277-9295; doi:10.3390/ijms12129277
Received: 28 October 2011; in revised form: 17 November 2011 / Accepted: 24 November 2011 / Published: 13 December 2011
Show/Hide Abstract | Cited by 3 | PDF Full-text (3581 KB) | HTML Full-text | XML Full-text
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Int. J. Mol. Sci. 2011, 12(11), 8275-8287; doi:10.3390/ijms12118275
Received: 12 October 2011; in revised form: 11 November 2011 / Accepted: 11 November 2011 / Published: 22 November 2011
Show/Hide Abstract | Cited by 8 | PDF Full-text (557 KB) | HTML Full-text | XML Full-text

Int. J. Mol. Sci. 2011, 12(9), 5844-5852; doi:10.3390/ijms12095844
Received: 2 August 2011; in revised form: 30 August 2011 / Accepted: 30 August 2011 / Published: 9 September 2011
Show/Hide Abstract | Cited by 13 | PDF Full-text (328 KB) | HTML Full-text | XML Full-text

Last update: 26 February 2014

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert