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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
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Proteins: From Genes to Degradation02:11

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
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The Proteasome01:13

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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.
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Regulated Protein Degradation02:58

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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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.
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Updated: Oct 22, 2025

4D Imaging of Protein Aggregation in Live Cells
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Protein Aggregation and Disaggregation in Cells and Development.

Jan S Fassler1, Sydney Skuodas1, Daniel L Weeks2

  • 1Department of Biology, University of Iowa, Iowa City, IA 52242, United States.

Journal of Molecular Biology
|August 27, 2021
PubMed
Summary
This summary is machine-generated.

Protein aggregates, or biomolecular condensates, are crucial for cellular functions and development. This review explores how cells control protein aggregation and disaggregation, highlighting their roles in development and reproduction.

Keywords:
ABCF gene familyRuvBL gene familyamyloidbiomolecular condensatechaperone

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Developmental Biology

Background:

  • Protein aggregation is linked to neurodegenerative diseases.
  • Regulated protein aggregates (condensates) control vital cellular activities.
  • Understanding these dynamic structures is key to cellular function.

Purpose of the Study:

  • To review biological examples of protein aggregates and their functions.
  • To explore cellular strategies for controlling protein aggregation and disaggregation.
  • To highlight the role of biomolecular condensates in development and reproduction.

Main Methods:

  • Literature review of protein aggregation and condensate biology.
  • Analysis of factors influencing aggregate formation, stability, and dissolution.
  • Examination of the roles of protein aggregates in cellular processes.

Main Results:

  • Protein aggregates serve diverse cellular roles, from stress response to gene expression.
  • Cellular strategies involve protein features, environmental factors, and modifications.
  • Biomolecular condensates are increasingly recognized for roles in early development, gametogenesis, and embryogenesis.

Conclusions:

  • Dynamic control of protein aggregation is essential for cellular life.
  • Biomolecular condensates play critical, underappreciated roles in reproduction and development.
  • Further research into disaggregation processes may reveal new therapeutic targets.