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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...
Microbial Fermentation01:23

Microbial Fermentation

Fermentation is a crucial anaerobic metabolic process that enables microbes to derive energy from sugar without relying on oxygen or an electron transport chain. This process is fundamental to various biological and industrial applications and is classified based on the metabolic products generated.Role of Pyruvate in FermentationPyruvate and its derivatives serve as key electron acceptors in fermentative pathways. The oxidation of NADH to regenerate NAD+ is essential for the continuation of...
Diversity of Archaea I01:30

Diversity of Archaea I

Archaea, a domain of single-celled microorganisms, are classified into five major phyla based on genetic and biochemical characteristics: Euryarchaeota, Crenarchaeota, Thaumarchaeota, Korarchaeota, and Nanoarchaeota. Among these, the phylum Euryarchaeota is notable for its remarkable diversity in morphology, metabolism, and ecological adaptations.Morphological and Metabolic DiversityMembers of Euryarchaeota exhibit a variety of cellular shapes, including rods and cocci. Their metabolic pathways...
Diversity of Archaea IV01:29

Diversity of Archaea IV

Hyperthermophilic archaea are a group of extremophiles thriving at temperatures above 80°C, often in hydrothermal vents and volcanic soils where conditions surpass the boiling point of water. At such temperatures, proteins, membranes, and DNA in most organisms degrade, but hyperthermophiles have evolved remarkable adaptations to maintain stability and function.Unique Cellular FeaturesHyperthermophilic membranes are composed of a monolayer of biphytanyl tetraether lipids, which resist thermal...
Amino Acid Catabolism01:18

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...

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Related Experiment Video

Updated: May 26, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Diversity, biogenesis and function of microbial amyloids.

Luz P Blanco1, Margery L Evans, Daniel R Smith

  • 1Department of Molecular Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

Trends in Microbiology
|December 27, 2011
PubMed
Summary

Functional amyloids, found in microbes, are assembled through directed pathways for beneficial cellular roles. Studying these functional amyloids offers new insights into disease-associated amyloid formation.

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Last Updated: May 26, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Area of Science:

  • Biochemistry
  • Microbiology
  • Cellular Biology

Background:

  • Amyloids, protein structures with beta-sheet folds, are linked to neurodegenerative diseases like Alzheimer's.
  • Traditionally viewed as products of protein misfolding, amyloids are now recognized as integral to normal cellular functions.
  • Microbial functional amyloids exemplify productive roles of amyloid structures in cellular life.

Purpose of the Study:

  • To review functional microbial amyloids, focusing on curli fibers.
  • To highlight the directed assembly and physiological functions of microbial amyloids.
  • To explore how microbial amyloid pathways inform our understanding of disease-associated amyloidogenesis.

Main Methods:

  • Review of existing literature on functional microbial amyloids.
  • Emphasis on curli fibers as a model system.
  • Analysis of amyloid assembly and disassembly pathways in microbes.

Main Results:

  • Functional amyloids are assembled via dedicated, directed pathways in microbes.
  • Microbial amyloids perform essential physiological functions, aiding in biofilm formation and community behaviors.
  • Microbial amyloid biogenesis pathways offer insights into productive amyloid assembly.

Conclusions:

  • Functional amyloids are widespread in cellular biology and crucial for microbial life.
  • Understanding microbial amyloid formation provides a novel perspective on disease-associated amyloidogenesis.
  • Curli fibers serve as a key example of functional microbial amyloids with significant roles.