Literature DB >> 21842955

Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations.

Samuel I A Cohen1, Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles.   

Abstract

Nucleated polymerisation processes are involved in many growth phenomena in nature, including the formation of cytoskeletal filaments and the assembly of sickle hemoglobin and amyloid fibrils. Closed form rate equations have, however, been challenging to derive for these growth phenomena in cases where secondary nucleation processes are active, a difficulty exemplified by the highly non-linear nature of the equation systems that describe monomer dependent secondary nucleation pathways. We explore here the use of fixed point analysis to provide self-consistent solutions to such growth problems. We present iterative solutions and discuss their convergence behaviour. We establish a range of closed form results for linear growth processes, including the scaling behaviours of the maximum growth rate and of the reaction end-point. We further show that a self-consistent approach applied to the master equation of filamentous growth allows the determination of the evolution of the shape of the length distribution including the mean, the standard deviation, and the mode. Our results highlight the power of fixed-point approaches in finding closed form self-consistent solutions to growth problems characterised by the highly non-linear master equations.

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Year:  2011        PMID: 21842955      PMCID: PMC5036541          DOI: 10.1063/1.3608917

Source DB:  PubMed          Journal:  J Chem Phys        ISSN: 0021-9606            Impact factor:   3.488


  33 in total

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3.  Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.

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Review 4.  Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature.

Authors:  Aimee M Morris; Murielle A Watzky; Richard G Finke
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Review 5.  Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?

Authors:  J T Jarrett; P T Lansbury
Journal:  Cell       Date:  1993-06-18       Impact factor: 41.582

6.  Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques.

Authors:  F A Ferrone; J Hofrichter; W A Eaton
Journal:  J Mol Biol       Date:  1985-06-25       Impact factor: 5.469

7.  Kinetic analysis of actin assembly suggests that tropomyosin inhibits spontaneous fragmentation of actin filaments.

Authors:  A Wegner
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Review 8.  Games played by rogue proteins in prion disorders and Alzheimer's disease.

Authors:  Adriano Aguzzi; Christian Haass
Journal:  Science       Date:  2003-10-31       Impact factor: 47.728

9.  Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism.

Authors:  F A Ferrone; J Hofrichter; H R Sunshine; W A Eaton
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

10.  Mechanism of prion propagation: amyloid growth occurs by monomer addition.

Authors:  Sean R Collins; Adam Douglass; Ronald D Vale; Jonathan S Weissman
Journal:  PLoS Biol       Date:  2004-09-21       Impact factor: 8.029

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  49 in total

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Authors:  Nitin S Tiwari; Koen Merkus; Paul van der Schoot
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2.  Protein Polymerization into Fibrils from the Viewpoint of Nucleation Theory.

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Journal:  Biophys J       Date:  2015-11-17       Impact factor: 4.033

3.  Molecular mechanisms of protein aggregation from global fitting of kinetic models.

Authors:  Georg Meisl; Julius B Kirkegaard; Paolo Arosio; Thomas C T Michaels; Michele Vendruscolo; Christopher M Dobson; Sara Linse; Tuomas P J Knowles
Journal:  Nat Protoc       Date:  2016-01-07       Impact factor: 13.491

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Review 5.  Physical and structural basis for polymorphism in amyloid fibrils.

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Journal:  Protein Sci       Date:  2014-09-13       Impact factor: 6.725

6.  Pseudo-one-dimensional nucleation in dilute polymer solutions.

Authors:  Lingyun Zhang; Jeremy D Schmit
Journal:  Phys Rev E       Date:  2016-06-29       Impact factor: 2.529

7.  Strain conformation controls the specificity of cross-species prion transmission in the yeast model.

Authors:  Anastasia V Grizel; Aleksandr A Rubel; Yury O Chernoff
Journal:  Prion       Date:  2016-07-03       Impact factor: 3.931

8.  Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.

Authors:  Erin Bove-Fenderson; Ryo Urano; John E Straub; David A Harris
Journal:  J Biol Chem       Date:  2017-08-23       Impact factor: 5.157

9.  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

10.  N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42.

Authors:  Olga Szczepankiewicz; Björn Linse; Georg Meisl; Eva Thulin; Birgitta Frohm; Carlo Sala Frigerio; Michael T Colvin; Angela C Jacavone; Robert G Griffin; Tuomas Knowles; Dominic M Walsh; Sara Linse
Journal:  J Am Chem Soc       Date:  2015-11-17       Impact factor: 15.419

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