(Q42285607)

English

The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration".

scientific article published on 7 April 2006

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scholarly article

1 reference

Europe PubMed Central

19 October 2017

The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration". (English)

1 reference

Europe PubMed Central

19 October 2017

object named as

Evan T Powers

1

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author name string

David L Powers

2

1 reference

Europe PubMed Central

19 October 2017

language of work or name

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publication date

7 April 2006

1 reference

Europe PubMed Central

19 October 2017

Biophysical Journal

1 reference

Europe PubMed Central

19 October 2017

91

1 reference

Europe PubMed Central

19 October 2017

122-132

1 reference

Europe PubMed Central

19 October 2017

1

1 reference

Europe PubMed Central

19 October 2017

Influence of the N-terminal domain on the aggregation properties of the prion protein

1 reference

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Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus

1 reference

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Mechanism of prion propagation: amyloid growth occurs by monomer addition

1 reference

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Therapeutic approaches to protein-misfolding diseases

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Folding proteins in fatal ways

1 reference

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Protein folding and misfolding

1 reference

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A perspective on mechanisms of protein tetramer formation

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Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases?

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Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation

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1 reference

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Nucleated conformational conversion and the replication of conformational information by a prion determinant

1 reference

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Review: history of the amyloid fibril

1 reference

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Quantifying the kinetic parameters of prion replication.

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Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates

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Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway

1 reference

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

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Diffusion-controlled macromolecular interactions

1 reference

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Cooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy

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Polymerization of actin and actin-like systems: evaluation of the time course of polymerization in relation to the mechanism.

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Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism.

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Kinetics of the cooperative association of actin to actin filament

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Transthyretin aggregation under partially denaturing conditions is a downhill polymerization

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Interpretation of concentration-dependence in aggregation kinetics.

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Assembly of amyloid protofibrils via critical oligomers--a novel pathway of amyloid formation

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Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis.

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Analysis of protein aggregation kinetics.

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The kinetics of protein-protein recognition.

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The kinetics of actin nucleation and polymerization

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

On one-dimensional nucleation and growth of "living" polymers I. Homogeneous nucleation

1 reference

https://pubmed.ncbi.nlm.nih.gov/16603497

12 December 2020

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inferred from PubMed ID database lookup

The measurement of cooperative protein self-assembly by turbidity and other techniques

1 reference

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inferred from PubMed ID database lookup

1 reference

https://pubmed.ncbi.nlm.nih.gov/16603497

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

1 reference

https://pubmed.ncbi.nlm.nih.gov/16603497

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based on heuristic

inferred from PubMed ID database lookup

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1 reference

https://pubmed.ncbi.nlm.nih.gov/16603497

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based on heuristic

inferred from PubMed ID database lookup

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1529/BIOPHYSJ.105.073767

1 reference

Europe PubMed Central

19 October 2017

1 reference

Europe PubMed Central

19 October 2017

1 reference

Europe PubMed Central

19 October 2017

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