Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Brain amyloid--a physicochemical perspective

J E Maggio1, P W Mantyh

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.

Brain Pathology (Zurich, Switzerland)
|April 1, 1996
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The majority of myelinated and unmyelinated sensory nerve fibers that innervate bone express the tropomyosin receptor kinase A.

Neuroscience·2011
Same author

Blockade of nerve sprouting and neuroma formation markedly attenuates the development of late stage cancer pain.

Neuroscience·2010
Same author

Capsaicin-sensitive sensory nerve fibers contribute to the generation and maintenance of skeletal fracture pain.

Neuroscience·2009
Same author

A quantitative analysis of the sensory and sympathetic innervation of the mouse pancreas.

Neuroscience·2006
Same author

The involvement of prostaglandins in tumorigenesis, tumor-induced osteolysis and bone cancer pain.

Journal of musculoskeletal & neuronal interactions·2005
Same author

Bone cancer pain and the role of RANKL/OPG.

Journal of musculoskeletal & neuronal interactions·2004
Same journal

Non-Alzheimer Aβ deposits in the human CNS: Implications with hypoxia and related conditions.

Brain pathology (Zurich, Switzerland)·2026
Same journal

Distinctly altered TRPC3 and TRPC6 expression patterns in human Alzheimer's disease cortex and hippocampus.

Brain pathology (Zurich, Switzerland)·2026
Same journal

Lewy bodies are surrounded by granulovacuolar degeneration bodies in dementia with Lewy bodies.

Brain pathology (Zurich, Switzerland)·2026
Same journal

A 3-year-old girl with a left optic nerve tumor.

Brain pathology (Zurich, Switzerland)·2026
Same journal

Chromosomal and immune dysregulation underlying granular mitosis in glioblastoma.

Brain pathology (Zurich, Switzerland)·2026
Same journal

Nearest-neighbors assisted unsupervised analysis for methylation array profiling for central nervous system tumors.

Brain pathology (Zurich, Switzerland)·2026
See all related articles

Human beta-amyloid peptide (A beta) forms brain amyloid in Alzheimer's disease (AD). Understanding A beta

Area of Science:

  • Biochemistry
  • Neuroscience
  • Physical Chemistry

Background:

  • Alzheimer's disease (AD) is characterized by brain amyloid plaques formed by human beta-amyloid peptide (A beta).
  • The hydrophobic nature and aggregation propensity of A beta have historically hindered research.
  • Recent advancements in synthetic peptides and physical methodologies have opened new avenues for studying A beta.

Purpose of the Study:

  • To investigate the physicochemical characteristics of A beta aggregation and deposition.
  • To explore structure/activity relationships and kinetics of A beta formation.
  • To identify potential therapeutic targets for Alzheimer's disease.

Main Methods:

  • Utilized in vitro model systems for A beta aggregation and deposition.

Related Experiment Videos

  • Employed various spectroscopic methods to determine A beta conformation in solution and solid phases.
  • Quantitatively analyzed structure/activity relationships and kinetics.

    • Main Results:

    • A beta aggregation and deposition are biochemically distinct processes.
    • Vascular and parenchymal amyloid exhibit different A beta peptide forms with distinct physicochemical properties.
    • A significant conformational transition is crucial for A beta's conversion from soluble peptide to fibril.

    Conclusions:

    • A beta's intrinsic ability to form cross-beta fibrils is key to Alzheimer's disease pathology.
    • Distinct conformational states of A beta in solution and fibrillar forms are critical.
    • These findings suggest novel therapeutic strategies targeting A beta's conformational changes.