An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleation
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA798062 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR17646455_1.fastq.gz | Fastqsanger.gz | |||
| SRR17646455_2.fastq.gz | Fastqsanger.gz | |||
| SRR17646456_1.fastq.gz | Fastqsanger.gz | |||
| SRR17646456_2.fastq.gz | Fastqsanger.gz | |||
| SRR17646457_1.fastq.gz | Fastqsanger.gz |
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Project description:Crespo2012 - Kinetics of Amyloid Fibril
Formation
This model is described in the article:
A generic
crystallization-like model that describes the kinetics of
amyloid fibril formation.
Crespo R, Rocha FA, Damas AM,
Martins PM.
J. Biol. Chem. 2012 Aug; 287(36):
30585-30594
Abstract:
Associated with neurodegenerative disorders such as
Alzheimer, Parkinson, or prion diseases, the conversion of
soluble proteins into amyloid fibrils remains poorly
understood. Extensive "in vitro" measurements of protein
aggregation kinetics have been reported, but no consensus
mechanism has emerged until now. This contribution aims at
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crystallization-like model (CLM) that is able to describe the
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importance of the nucleation and growth steps. Using the CLM,
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confirm the CLM as a good approximation to the generalized
underlying principle governing amyloid fibrillization. A
perspective is presented on possible applications of the CLM
during the development of new targets for amyloid disease
therapeutics.
This model is hosted on
BioModels Database
and identified by:
BIOMD0000000531.
To cite BioModels Database, please use:
BioModels Database:
An enhanced, curated and annotated resource for published
quantitative kinetic models.
To the extent possible under law, all copyright and related or
neighbouring rights to this encoded model have been dedicated to
the public domain worldwide. Please refer to
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Public Domain Dedication for more information.
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