Title : Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein.

Pub. Date : 2013 Oct 8

PMID : 24033133






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 In contrast, tau amyloids formed with heparin as an inducing agent-a common biochemical model of tau misfolding-are structurally distinct from brain-derived PHFs. Heparin microtubule associated protein tau Homo sapiens
2 In contrast, tau amyloids formed with heparin as an inducing agent-a common biochemical model of tau misfolding-are structurally distinct from brain-derived PHFs. Heparin microtubule associated protein tau Homo sapiens
3 Tau fibrils produced by incubating recombinant tau with heparin had significantly narrower fibrils with a longer periodicity, higher chemical stability, and distinct secondary structure compared to AD PHFs. Heparin microtubule associated protein tau Homo sapiens
4 Tau fibrils produced by incubating recombinant tau with heparin had significantly narrower fibrils with a longer periodicity, higher chemical stability, and distinct secondary structure compared to AD PHFs. Heparin microtubule associated protein tau Homo sapiens
5 The addition of heparin to the reaction of recombinant tau and AD PHFs also corrupted the templating process, resulting in a mixture of fibril conformations. Heparin microtubule associated protein tau Homo sapiens