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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

Protein aggregation: mechanisms and functional consequences.

Gaetano Invernizzi1, Elena Papaleo, Raimon Sabate

  • 1Dipartimento di Biotecnologie e Bioscienze, Università di Milano-Bicocca, Milan, Italy.

The International Journal of Biochemistry & Cell Biology
|June 21, 2012
PubMed
Summary
This summary is machine-generated.

Protein misfolding and aggregation into amyloid fibrils are implicated in neurodegenerative diseases. This study explores their structure, formation, disease roles, and functional aspects, highlighting bioinformatics

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Medical Science

Background:

  • Protein misfolding and aggregation into amyloid structures are critical in cellular function and disease.
  • These processes are linked to major human degenerative disorders such as Alzheimer's, Parkinson's, and Huntington's diseases, and type 2 diabetes.

Purpose of the Study:

  • To investigate the conformational properties and formation pathways of protein aggregates.
  • To elucidate the role of these aggregates in human diseases and their functional implications.
  • To explore the utility of bioinformatics tools in studying protein assemblies.

Main Methods:

  • Review and analysis of existing literature on protein misfolding and aggregation.
  • Examination of conformational properties and formation pathways of amyloid aggregates.
  • Exploration of the functional roles and disease associations of protein assemblies.
  • Assessment of bioinformatics tools for studying these structures.

Main Results:

  • Amyloid aggregates, while detrimental in disease, serve specialized functions across organisms.
  • Understanding aggregate formation is key to comprehending disease mechanisms.
  • Bioinformatics offers valuable approaches for studying complex protein assemblies.

Conclusions:

  • Protein misfolding and aggregation represent a dual-edged sword, crucial in both disease and biological function.
  • Further research into these mechanisms and the application of bioinformatics tools are essential for therapeutic development against protein misfolding diseases.