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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...
Pharmacogenetics of Drug Targets: β₂-Adrenergic Receptors, Apo E, Thymidylate Synthase01:11

Pharmacogenetics of Drug Targets: β₂-Adrenergic Receptors, Apo E, Thymidylate Synthase

Genetic polymorphisms in drug targets have emerged as critical determinants of interindividual variability in drug response and toxicity. Pharmacogenomic investigations increasingly focus on identifying these variations to personalize and optimize therapeutic interventions. A drug target may be a receptor, enzyme, or signaling protein involved in pharmacologic responses or disease-related pathways. While early pharmacogenetic studies focused primarily on drug metabolism, current research...
Pharmacogenetic Phenotypes: Alterations in Pharmacokinetics, Drug Targets and Biologic Milieu01:29

Pharmacogenetic Phenotypes: Alterations in Pharmacokinetics, Drug Targets and Biologic Milieu

Genetic variations significantly influence drug response through pharmacokinetics, receptor interactions, and biologic milieu modifications. Pharmacokinetic alterations impact drug metabolism and clearance, affecting efficacy and toxicity. Variants in drug-metabolizing enzymes, such as CYP2C9 and CYP2C19, alter drug activation and elimination. For example, CYP2C9 loss-of-function variants require lower warfarin doses to prevent excessive bleeding, while CYP2C19 variants reduce clopidogrel...
Multiple Allele Traits01:49

Multiple Allele Traits

The Concept of Multiple Allelism

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Related Experiment Video

Updated: May 29, 2026

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

Molecular basis for amyloid-beta polymorphism.

Jacques-Philippe Colletier1, Arthur Laganowsky, Meytal Landau

  • 1Howard Hughes Medical Institute, Department of Biological Chemistry and Chemistry and Biochemistry, UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 28, 2011
PubMed
Summary
This summary is machine-generated.

Alzheimer's disease research reveals amyloid-beta (Aβ) structural diversity. New microcrystal structures of Aβ segments show various self-association modes, aiding understanding of plaque formation and disease mechanisms.

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Related Experiment Videos

Last Updated: May 29, 2026

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Amyloid-beta (Aβ) aggregates form senile plaques, a hallmark of Alzheimer's disease.
  • The polymorphic nature of Aβ structures complicates biophysical characterization and understanding of its pathology.

Purpose of the Study:

  • To elucidate the atomic-level polymorphism of amyloid-beta (Aβ).
  • To provide molecular models for the diverse structures of Aβ.

Main Methods:

  • Determined eight new microcrystal structures of fiber-forming Aβ segments.
  • Analyzed structures revealing steric zipper formations and various self-association modes.
  • Integrated new structural data with previous NMR studies.

Main Results:

  • Identified diverse modes of Aβ self-association through steric zipper structures.
  • Revealed atomic details of Aβ polymorphism.
  • Proposed multiple molecular models for Aβ fibers based on combined structural and NMR data.

Conclusions:

  • The study provides fundamental insights into the polymorphic nature of Aβ.
  • Developed molecular models that advance the understanding of Aβ pathogenesis in Alzheimer's disease.
  • Characterized the structural variability of amyloid aggregates.