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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...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

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Related Experiment Video

Updated: Jul 4, 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

AMYPdb: a database dedicated to amyloid precursor proteins.

Sandrine Pawlicki1, Antony Le Béchec, Christian Delamarche

  • 1Université de Rennes I and CNRS UMR 6026, Equipe Structure et Dynamique des Macromolécules, Campus de Beaulieu, Nb 13, 35042 RENNES Cedex, France. sandrine.pawlicki@laposte.net

BMC Bioinformatics
|June 12, 2008
PubMed
Summary

A new online database, AMYPdb, centralizes amyloid protein data. Analysis revealed specific sequence patterns linked to protein misfolding and aggregation, aiding disease research.

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Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
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Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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Related Experiment Videos

Last Updated: Jul 4, 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

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
15:23

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Area of Science:

  • Biochemistry
  • Bioinformatics
  • Structural Biology

Background:

  • Protein misfolding and aggregation are implicated in severe diseases like Alzheimer's and type II diabetes.
  • In silico methods are crucial for studying protein conformational changes but require centralized, accurate data.
  • Existing data on amyloid precursors are scattered across multiple generalist databases.

Purpose of the Study:

  • To create a centralized, comprehensive online database for amyloid precursor proteins.
  • To facilitate in silico investigation of protein misfolding and aggregation mechanisms.
  • To identify novel sequence patterns associated with amyloid formation.

Main Methods:

  • Development of the AMYPdb (Amyloid Precursor Protein database) online resource.
  • Large-scale sequence analysis of integrated protein data.
  • Generation and analysis of amino acid sequence patterns using bioinformatics tools.

Main Results:

  • AMYPdb integrates data for 1,705 proteins across 31 families from nearly 600 organisms.
  • The database links to over 2,300 references and 1,200 3D structures.
  • Analysis identified 3,621 sequence patterns, including highly specific ones for amyloid families and those involved in misfolding.

Conclusions:

  • AMYPdb offers a centralized bioinformatic resource for all amyloid proteins and precursors.
  • Sequence pattern discovery highlights regions critical for protein misfolding and aggregation.
  • The database is freely accessible, promoting research and collaboration.