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Nibaldo C. Inestrosa

Researcher at Pontifical Catholic University of Chile

Publications -  422
Citations -  23270

Nibaldo C. Inestrosa is an academic researcher from Pontifical Catholic University of Chile. The author has contributed to research in topics: Wnt signaling pathway & Acetylcholinesterase. The author has an hindex of 74, co-authored 409 publications receiving 20854 citations. Previous affiliations of Nibaldo C. Inestrosa include University of New South Wales & Andrés Bello National University.

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Journal ArticleDOI

Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme

Nibaldo C. Inestrosa, +8 more
- 01 Apr 1996 - 
TL;DR: It is reported here that bovine brain AChE, as well as the human and mouse recombinant enzyme, accelerates amyloid formation from wild-type A beta and a mutant A beta peptide, which alone produces few amyloids-like fibrils.
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Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid Cu-DEPENDENT CATALYTIC CONVERSION OF DOPAMINE, CHOLESTEROL, AND BIOLOGICAL REDUCING AGENTS TO NEUROTOXIC H2O2

Carlos Opazo, +11 more
- 25 Oct 2002 - 
TL;DR: It is reported that microregional catalytic H( 2)O(2) production, combined with the exhaustion of reducing agents, may mediate the neurotoxicity of Abeta in Alzheimer's disease, and inhibitors of this novel activity may be of therapeutic value.
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Emerging roles of Wnts in the adult nervous system

Nibaldo C. Inestrosa, +1 more
- 01 Feb 2010 - 
TL;DR: The latest insights into the function of Wnt signalling in the adult nervous system and therapeutic opportunities for neurodegenerative diseases such as Alzheimer's and Parkinson's disease are discussed.
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Settlement of benthic marine invertebrates

Sebastián Rodríguez, +2 more
- 01 Jan 1993 - 
TL;DR: This review analyses the settlement process, attempting to integrate aspects related to different levels of organization (i.e. ecological-physiological-molecular) and using the use of artificial inducers in studying settlement induction, until more effective natural inducers are isolated and characterized.
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A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation

G. V. De Ferrari, +6 more
- 04 Sep 2001 - 
TL;DR: Evidence is presented for the structural motif of AChE involved in the interaction with the amyloid beta-peptide (Abeta), which indicates that the homologous human A ChE motif is capable of accelerating Abeta fibrillogenesis.