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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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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Protein aggregation and misfolding: good or evil?

Annalisa Pastore1, Pierandrea Temussi

  • 1MRC NIMR, The Ridgeway, London, UK. apastor@nimr.mrc.ac.uk

Journal of Physics. Condensed Matter : an Institute of Physics Journal
|May 19, 2012
PubMed
Summary

Protein aggregation, a key process in medicine and material science, is increasingly studied. This review summarizes factors driving protein aggregation and cellular defense mechanisms, opening new research perspectives.

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08:59

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Area of Science:

  • Biochemistry and Molecular Biology
  • Biophysics
  • Materials Science

Background:

  • Protein aggregation and misfolding are implicated in diverse fields including medicine, biology, nanotechnology, and material science.
  • Research interest in protein aggregation has grown exponentially over the past two decades, with numerous publications exploring various perspectives.
  • Understanding protein aggregation is crucial for advancements in multiple scientific disciplines.

Purpose of the Study:

  • To summarize key findings from recent studies on protein aggregation.
  • To introduce the topical issue of protein aggregation and its implications.
  • To discuss factors influencing protein aggregation and cellular defense strategies.

Main Methods:

  • Literature review and synthesis of existing research on protein aggregation.
  • Analysis of factors contributing to protein aggregation.
  • Examination of cellular mechanisms involved in preventing or responding to protein aggregation.

Main Results:

  • Identified key factors that promote protein aggregation.
  • Detailed cellular strategies evolved to defend against protein aggregation.
  • Highlighted the interdisciplinary nature of protein aggregation research.

Conclusions:

  • Accumulated knowledge on protein aggregation opens new avenues for research and applications.
  • Understanding aggregation mechanisms is vital for therapeutic and technological innovations.
  • Continued investigation into protein aggregation and cellular defenses is warranted.