{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T05:52:02Z","timestamp":1789451522724,"version":"build-2803163510"},"reference-count":104,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"5646","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2003,10,31]]},"abstract":"<jats:p>\n            The incidence of Alzheimer's disease (AD) and that of prion disorders (PrD) could not be more different. One-third of octogenarians succumb to AD, whereas Creutzfeldt-Jakob disease typically affects one individual in a million each year. However, these diseases have many common features impinging on the metabolism of neuronal membrane proteins: the amyloid precursor protein APP in the case of AD, and the cellular prion protein PrP\n            <jats:sup>C<\/jats:sup>\n            in PrD. APP begets the A\u03b2 peptide, whereas PrP\n            <jats:sup>C<\/jats:sup>\n            begets the malignant prion protein PrP\n            <jats:sup>Sc<\/jats:sup>\n            . Both A\u03b2 and PrP\n            <jats:sup>Sc<\/jats:sup>\n            are associated with disease, but we do not know what triggers their accumulation and neurotoxicity. A great deal has been learned, however, about protein folding, misfolding, and aggregation; an entirely new class of intramembrane proteases has been identified; and unsuspected roles for the immune system have been uncovered. There is reason to expect that prion research will profit from advances in the understanding of AD, and vice versa.\n          <\/jats:p>","DOI":"10.1126\/science.1087348","type":"journal-article","created":{"date-parts":[[2003,10,31]],"date-time":"2003-10-31T01:25:22Z","timestamp":1067563522000},"page":"814-818","source":"Crossref","is-referenced-by-count":195,"title":["Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease"],"prefix":"10.1126","volume":"302","author":[{"given":"Adriano","family":"Aguzzi","sequence":"first","affiliation":[{"name":"Institute of Neuropathology, University Hospital of Zurich, Schmelzbergstrasse 12, CH-8091 Zurich, Switzerland."},{"name":"Department of Biochemistry, Adolf-Butenandt-Institute, Laboratory for Alzheimer's and Parkinson's Disease Research, Ludwig-Maximilians-University, Schillerstrasse 44, Munich, Germany."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Haass","sequence":"additional","affiliation":[{"name":"Institute of Neuropathology, University Hospital of Zurich, Schmelzbergstrasse 12, CH-8091 Zurich, Switzerland."},{"name":"Department of Biochemistry, Adolf-Butenandt-Institute, Laboratory for Alzheimer's and Parkinson's Disease Research, Ludwig-Maximilians-University, Schillerstrasse 44, Munich, Germany."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/375754a0"},{"key":"e_1_3_1_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/19077"},{"key":"e_1_3_1_4_2","unstructured":"D. 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