نتایج جستجو برای: protein misfolding

تعداد نتایج: 1235138  

1996
Fred H. Irons Donald M. Hummels

Fred H. Irons, Donald M. Hummels, and Cindy ????? Zoldi Department of Electrical and Computer Engineering University of Maine, Orono, Maine USA [email protected] ABSTRACT Procedures have been developed to apply ADC modeling techniques to the diagnosis of high-speed Folding Amplier Interpolating Resistive (FAIR) networks. This paper presents results and describes procedures used to obtain mea...

Journal: :Cold Spring Harbor perspectives in biology 2011
Rebecca C Taylor Andrew Dillin

Aging cells accumulate damaged and misfolded proteins through a functional decline in their protein homeostasis (proteostasis) machinery, leading to reduced cellular viability and the development of protein misfolding diseases such as Alzheimer's and Huntington's. Metabolic signaling pathways that regulate the aging process, mediated by insulin/IGF-1 signaling, dietary restriction, and reduced ...

Journal: :Physical chemistry chemical physics : PCCP 2016
Suzanne K Shoffner Santiago Schnell

Fibrillogenesis, the production or development of protein fibers, has been linked to protein folding diseases. The progress curve of fibrils or aggregates typically takes on a sigmoidal shape with a lag phase, a rapid growth phase, and a final plateau regime. The study of the lag phase and the estimation of its critical timescale provide insight into the factors regulating the fibrillation proc...

Journal: :Revista de Informática Teórica e Aplicada 2021

Protein Structure Prediction (PSP) problem is to determine the three-dimensional structure of a protein only from its primary structure. Misfolding causes human diseases. Thus, knowledge and functionality proteins, combined with prediction their complex challenge for area computational biology. The metaheuristic optimization algorithms are naturally applicable support in solving NP-hard problem...

Journal: :Life 2023

Proteinopathy is characterized by the accumulation of aggregates a specific protein in target organ, tissue, or cell. The aggregation same can cause different pathologies as single adopt various amyloidogenic, disease-specific conformations. conformation governs interaction amyloid with other proteins that are prone to misfolding and, thus, determines spectrum concomitant pathologies. In this r...

Journal: :Cell 2007
R. Luke Wiseman Evan T. Powers Joel N. Buxbaum Jeffery W. Kelly William E. Balch

To provide an integrated view of endoplasmic reticulum (ER) function in protein export, we have described the interdependence of protein folding energetics and the adaptable biology of cellular protein folding and transport through the exocytic pathway. A simplified treatment of the protein homeostasis network and a formalism for how this network of competing pathways interprets protein folding...

Journal: :Journal of Student Research 2023

Transthyretin (TTR) amyloidosis is a protein misfolding disorder where tetramers of TTR dissociate, causing the formation insoluble amyloids leading to organ dysfunction and damage. Worldwide, disease currently affects between 5,000-10,000 people many novel therapeutic techniques are appearing with potential treat amyloidosis. Of non-CRISPR treatments, they can be broken down into three categor...

Journal: :Frontiers in Molecular Neuroscience 2023

Prion diseases are fatal brain disorders characterized by deposition of insoluble isoforms the prion protein (PrP). The normal and pathogenic structures PrP relatively well known after decades studies. Yet our current understanding intrinsic determinants regulating misfolding largely missing. A 3D subdomain comprising β2-α2 loop helix 3 contains high sequence structural variability among animal...

Journal: :International Journal of Biochemistry & Physiology 2020

Journal: :Biochemical and Biophysical Research Communications 2014

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