English
Related papers

Related papers: A Kinetic Model for Cell Damage Caused by Oligomer…

200 papers

We develop a general theory for three states of equilibrium of amyloid peptides: the monomer, oligomer, and fibril. We assume that the oligomeric state is a disordered micelle-like collection of a few peptide chains held together loosely by…

Soft Condensed Matter · Physics 2015-05-19 Jeremy Schmit , Kingshuk Ghosh , Ken Dill

Proteinaceous aggregation occurs through self-assembly-- a process not entirely understood. In a recent article [1], an analytical theory for amyloid fibril growth via secondary rather than primary nucleation was presented. Remarkably, with…

Biological Physics · Physics 2010-06-16 Barry D. Ganapol

Amyloid fibers are aggregates of proteins. They are built out of a peptide called $\beta$--amyloid (A$\beta$) containing between 41 and 43 residues, produced by the action of an enzyme which cleaves a much larger protein known as the…

Biomolecules · Quantitative Biology 2009-11-10 G. Tiana , F. Simona , R. A. Broglia , G. Colombo

A severe application of stress on articular cartilage can initiate a cascade of biochemical reactions that can lead to the development of osteoarthritis. We constructed a multiscale mathematical model of the process with three components:…

Tissues and Organs · Quantitative Biology 2023-02-14 Georgi I. Kapitanov , Xiayi Wang , Bruce P. Ayati , Marc J. Brouillette , James A. Martin

Amyloid fibrillation is a protein self-assembly phenomenon that is intimately related to well-known human neurodegenerative diseases. During the past few decades, striking advances have been achieved in our understanding of the physical…

Biomolecules · Quantitative Biology 2017-09-06 Liu Hong , Chiu Fan Lee , Ya Jing Huang

Protein oligomers have been implicated as toxic agents in a wide range of amyloid-related diseases. Yet it has remained unsolved whether the oligomers are a necessary step in the formation of amyloid fibrils, or just a dangerous by-product.…

Biomolecules · Quantitative Biology 2014-12-03 Anđela Šarić , Yassmine C. Chebaro , Tuomas P. J. Knowles , Daan Frenkel

We present a model of articular cartilage lesion formation to simulate the effects of cyclic loading. This model extends and modifies the reaction-diffusion-delay model by Graham et al. 2012 for the spread of a lesion formed though a single…

Tissues and Organs · Quantitative Biology 2023-02-14 Xiayi Wang , Bruce P. Ayati , Marc J. Brouillete , Jason M. Graham , Prem S. Ramakrishnan , James A. Martin

Elongation is a fundament process in amyloid fiber growth, which is normally characterized by a linear relationship between the fiber elongation rate and the monomer concentration. However, in high concentration regions, a sub-linear…

Quantitative Methods · Quantitative Biology 2020-11-13 Liu Hong , Xizhou Liu , Thomas C. T. Michaels , Tuomas P. J. Knowles

Recent experiments with amyloid-beta (Abeta) peptide suggest that formation of toxic oligomers may be an important contribution to the onset of Alzheimer's disease. The toxicity of Abeta oligomers depends on their structure, which is…

Biological Physics · Physics 2009-11-10 B. Urbanc , L. Cruz , F. Ding , D. Sammond , S. Khare , S. V. Buldyrev , H. E. Stanley , N. V. Dokholyan

Living systems produce copies of information-carrying molecules such as DNA by assembling monomer units into finite-length oligomer (short polymer) copies. We explore the role of initiation and termination of the copy process in the…

Subcellular Processes · Quantitative Biology 2021-08-11 Jenny Marie Poulton , Thomas Edward Ouldridge

The need to understand the assembly kinetics of fibril formation has become urgent because of the realization that soluble oligomers of amyloidogenic peptides may be even more neurotoxic than the end product, namely, the amyloid fibrils. In…

Biomolecules · Quantitative Biology 2007-05-23 Ruxandra I. Dima , Bogdan Tarus , John E. Straub , D. Thirumalai

Protein amyloid fibrils are a form of linear protein aggregates that are implicated in many neurodegenerative diseases. Here, we study the dynamics of amyloid fibril elongation by performing Langevin dynamic simulations on a coarse-grained…

Biological Physics · Physics 2009-10-06 Chiu Fan Lee , James Loken , Letitia Jean , David J. Vaux

Using exhaustive Monte Carlo simulations we study the kinetics and mechanism of fibril formation using lattice models as a function of temperature and the number of chains. While these models are, at best, caricatures of peptides, we show…

Biomolecules · Quantitative Biology 2009-11-13 Mai Suan Li , D. K. Klimov , J. E. Straub , D. Thirumalai

The dynamics of cellular pattern formation is crucial for understanding embryonic development and tissue morphogenesis. Recent studies have shown that human dermal fibroblasts cultured on liquid crystal elastomers can exhibit an increase in…

Biological Physics · Physics 2023-08-25 Mengyang Gu , Xinyi Fang , Yimin Luo

The self-assembly of proteins into $\beta$-sheet-rich amyloid fibrils has been observed to occur with sigmoidal kinetics, indicating that the system initially is trapped in a metastable state. Here, we use a minimal lattice-based model to…

Biological Physics · Physics 2016-01-05 Anders Irbäck , Jonas Wessén

Angiogenesis, the development of new vasculature, is a critical process in the growth of new tumors. Driven by a goal to understand this aspect of cancer proliferation, I develop a discrete computationally optimized mathematical model of…

Cell Behavior · Quantitative Biology 2016-02-11 Dibya Jyoti Ghosh

Proteins have been empirically linked to memory. If memory relates to protein structure, then each conformation would_functionally_ code only one bit, making it difficult to explain large memories. Nor is there a simple way to relate memory…

General Physics · Physics 2011-07-22 C. K. Raju

The presence of oligomeric aggregates, which is often observed during the process of amyloid formation, has recently attracted much attention since it has been associated with neurodegenerative conditions such as Alzheimer's and Parkinson's…

Biomolecules · Quantitative Biology 2009-01-14 Stefan Auer , Filip Meersman , Christopher M. Dobson , Michele Vendruscolo

The importance of molecular-scale forces in sculpting biological form and function has been acknowledged for more than a century. Accounting for forces in biology is a problem that lies at the intersection of soft condensed matter physics,…

Soft Condensed Matter · Physics 2025-12-10 K. Vijay Kumar , Mandar M. Inamdar , Pramod A. Pullarkat , Gautam I. Menon

Progressive damage, which eventually leads to failure, is ubiquitous in biological and synthetic polymers. The simplest case to consider is that of elastomeric materials, which can undergo large reversible deformations with negligible rate…

Soft Condensed Matter · Physics 2018-02-14 Brandon Talamini , Yunwei Mao , Lallit Anand
‹ Prev 1 2 3 10 Next ›