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000059552 0247_ $$2DOI$$a10.1002/jnr.21353
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000059552 041__ $$aeng
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000059552 084__ $$2WoS$$aNeurosciences
000059552 1001_ $$0P:(DE-Juel1)VDB72260$$aLeliveld, S. R.$$b0$$uFZJ
000059552 245__ $$aThe use of conformation-specific ligands and assays to dissect the molecular mechanisms of neurodegenerative diseases
000059552 260__ $$aNew York, NY [u.a.]$$bWiley-Liss$$c2007
000059552 300__ $$a2285 - 2297
000059552 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000059552 440_0 $$018101$$aJournal of Neuroscience Research$$v85$$x0360-4012$$y11
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000059552 520__ $$aThe use of conformation-specific ligands has been closely linked to progress in the molecular characterization of neurodegenerative diseases. Deposition of misfolded or misprocessed proteins is now recognized as a hallmark of all neurodegenerative diseases. Initially, dyes like Congo red and thioflavin T were used as crudely conformation-specific ligands for staining the beta-sheeted protein components of amyloid deposits in neurodegenerative diseases such as Alzheimer disease (AD) and prion disease, the two diseases in which protein conformations were distinguished early on. This conformational characterization of extracellular protein deposits with dyes ultimately led to the identification of key players in the disease processes. The recent discovery of intermediate conformational species, i.e., soluble oligomers for AD and PK-sensitive PrP(Sc) for prion disease, whose conformation and assembly are thought to be distinct from both the physiological and the fibrillar conformational states, replaced the former notion that the microscopic protein deposits themselves caused disease. This insight and the generation of conformation-specific monoclonal antibodies to these conformers further advanced diagnosis and the understanding of molecular mechanisms of AD and are likely to do so in other neurodegenerative diseases. Here we review how conformer distinction performed by a variety of different techniques, including biophysical, biochemical, and antibody-based methods, led to the current molecular concepts of AD and the prion diseases. We provide an outlook on the application of these techniques in advancing the understanding of molecular mechanisms of other neurodegenerative diseases or degenerative brain conditions.
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000059552 650_2 $$2MeSH$$aAmyloid beta-Peptides: chemistry
000059552 650_2 $$2MeSH$$aAnimals
000059552 650_2 $$2MeSH$$aAntibodies, Monoclonal
000059552 650_2 $$2MeSH$$aBrain: pathology
000059552 650_2 $$2MeSH$$aBrain Chemistry
000059552 650_2 $$2MeSH$$aHumans
000059552 650_2 $$2MeSH$$aLigands
000059552 650_2 $$2MeSH$$aNeurodegenerative Diseases: diagnosis
000059552 650_2 $$2MeSH$$aNeurodegenerative Diseases: pathology
000059552 650_2 $$2MeSH$$aPeptides: chemistry
000059552 650_2 $$2MeSH$$aPrPSc Proteins: chemistry
000059552 650_2 $$2MeSH$$aProtein Conformation
000059552 650_7 $$00$$2NLM Chemicals$$aAmyloid beta-Peptides
000059552 650_7 $$00$$2NLM Chemicals$$aAntibodies, Monoclonal
000059552 650_7 $$00$$2NLM Chemicals$$aLigands
000059552 650_7 $$00$$2NLM Chemicals$$aPeptides
000059552 650_7 $$00$$2NLM Chemicals$$aPrPSc Proteins
000059552 650_7 $$2WoSType$$aJ
000059552 65320 $$2Author$$aneurodegeneration
000059552 65320 $$2Author$$aprotein
000059552 65320 $$2Author$$aoligomers
000059552 65320 $$2Author$$aconformation
000059552 7001_ $$0P:(DE-HGF)0$$aKorth, C.$$b1
000059552 773__ $$0PERI:(DE-600)1474904-x$$a10.1002/jnr.21353$$gVol. 85, p. 2285 - 2297$$p2285 - 2297$$q85<2285 - 2297$$tJournal of neuroscience research$$v85$$x0360-4012$$y2007
000059552 8567_ $$uhttp://dx.doi.org/10.1002/jnr.21353
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000059552 9141_ $$y2007
000059552 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000059552 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x1
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