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ETTORE MAJORANA FOUNDATION
AND CENTER FOR SCIENTIFIC CULTURE

  • Homepage
  • The Foundation
    • The History
    • Professor Antonino Zichichi
    • The Erice Statement
    • Location And Structures
    • Alberto Gabriele Seismic Network
  • International Schools
    • Astronomy
    • Cultural Heritage
    • Biology
    • Chemistry
    • Law Studies
    • Physics
    • Engineering
    • Computer Engineering
    • Mathematics
    • Medical Studies
    • Earth Sciences
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    • History
  • Seminars
    • Seminars
    • Symposium
    • Workshops
  • News
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  • IT
Menu
  • Homepage
  • The Foundation
    • The History
    • Professor Antonino Zichichi
    • The Erice Statement
    • Location And Structures
    • Alberto Gabriele Seismic Network
  • International Schools
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International Schools > Medical Studies

INTERNATIONAL SCHOOL OF BRAIN DISEASES

Founded in 1996

1st Director John Collinge

The aim of the school is to study degenerative brain diseases. Prion diseases are transmissible neurodegenerative disorders which affect a range of mammalian species. In humans they can be inherited and sporadic as well as acquired by exposure to human prions. Prions appear to be composed principally of a conformational isomer of host-encoded prion protein and propagate by recruitment of cellular prion protein. Recent evidence argues that prion protein can also encode disease phenotypes by differences in its conformation and glycosylation. Such molecular analysis of prion strains suggests that new variant Creutzfeldt-Jakob disease is caused by BSE exposure. The novel biology of prion propagation may not be unique to these rare degenerative brain diseases.

Courses

Past courses

International Schools >Medical Studies

INTERNATIONAL SCHOOL OF BRAIN DISEASES

Founded in 1996

1st Director John Collinge

The aim of the school is to study degenerative brain diseases. Prion diseases are transmissible neurodegenerative disorders which affect a range of mammalian species. In humans they can be inherited and sporadic as well as acquired by exposure to human prions. Prions appear to be composed principally of a conformational isomer of host-encoded prion protein and propagate by recruitment of cellular prion protein. Recent evidence argues that prion protein can also encode disease phenotypes by differences in its conformation and glycosylation. Such molecular analysis of prion strains suggests that new variant Creutzfeldt-Jakob disease is caused by BSE exposure. The novel biology of prion propagation may not be unique to these rare degenerative brain diseases.

Courses

Past Courses

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