LEADER 03628nam 2200649 a 450 001 9910830473703321 005 20230421044538.0 010 $a1-282-34797-7 010 $a9786612347979 010 $a0-470-51492-2 010 $a0-470-51493-0 035 $a(CKB)1000000000377216 035 $a(EBL)470493 035 $a(SSID)ssj0000304052 035 $a(PQKBManifestationID)11275948 035 $a(PQKBTitleCode)TC0000304052 035 $a(PQKBWorkID)10278879 035 $a(PQKB)11530548 035 $a(MiAaPQ)EBC470493 035 $a(OCoLC)181181768 035 $a(EXLCZ)991000000000377216 100 $a19960424d1996 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 04$aThe nature and origin of amyloid fibrils$b[electronic resource] /$f[editors, Gregory R. Bock (Organizer) and Jamie A. Goode] 210 $aChichester ;$aNew York $cWiley$d1996 215 $a1 online resource (268 p.) 225 1 $aCiba Foundation symposium ;$v199 300 $a"Symposium on The nature and origin of amyloid fibrils, held at the Pala?cio dos Marqueses de Pombal, Oeiras, Portugal, 23-25 October 1995"--Contents. 311 $a0-471-96361-5 320 $aIncludes bibliographical references and indexes. 327 $aTHE NATURE AND ORIGIN OF AMYLOID FIBRILS; Contents; Participants; Preface; Introduction; In memoriam; A molecular model of the amyloid fibril; Refined fibril structures: the hydrophobic core in Alzheimer's amyloid b-protein and prion as revealed by X-ray diffraction; General discussion I; Modulating conformational factors in transthyretin amyloid; Proteoglycans and amyloid fibrillogenesis; Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy; General discussion II; Metabolism of amyloid proteins 327 $aAlzheimer's disease: genesis of amyloidApolipoprotein E and amyloidogenesis; Interaction of transthyretin with amyloid B-protein: binding and inhibition of amyloid formation; General discussion III; B-amyloid precursor protein and early-o nset Alzheimer's disease; Prion protein amyloid: separation of scrapie infectivity from PrP polymers; General discussion IV; Ageing and amyloid fibrillogenesis: lessons from apolipoprotein Al, transthyretin and islet amyloid polypeptide; General discussion V 327 $aFAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formationIndex of contributors; Subject index 330 $aAmyloid fibrils are associated with a range of pathological disorders including Alzheimer's Disease, Down's syndrome, diabetes, cardiomyopathies, and transmissible spongiform encephalopathies. 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