C
Cristian Ionescu-Zanetti
Researcher at University of California, Santa Cruz
Publications - 9
Citations - 2039
Cristian Ionescu-Zanetti is an academic researcher from University of California, Santa Cruz. The author has contributed to research in topics: Fibril & Amyloid. The author has an hindex of 8, co-authored 9 publications receiving 1924 citations. Previous affiliations of Cristian Ionescu-Zanetti include University of California, Santa Barbara.
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Journal ArticleDOI
Mechanism of thioflavin T binding to amyloid fibrils
Ritu Khurana,Chris Coleman,Cristian Ionescu-Zanetti,Sue A. Carter,Vinay Krishna,Rajesh K. Grover,Raja Roy,Shashi Singh +7 more
TL;DR: The data suggests that the micelles of thioflavin T bind amyloid fibrils leading to enhancement of fluorescence emission, which suggests that positive charge on the thioFlavin T molecule has a role in its micelle formation that then bind the amyloids fibril.
Journal ArticleDOI
Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates.
Ritu Khurana,Joel R. Gillespie,Anupam Talapatra,Lauren J. Minert,Cristian Ionescu-Zanetti,Ian S. Millett,Anthony L. Fink +6 more
TL;DR: The data support the hypothesis that amyloid fibril formation involves the ordered self-assembly of partially folded species that are critical soluble precursors of fibrils.
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A General Model for Amyloid Fibril Assembly Based on Morphological Studies Using Atomic Force Microscopy
Ritu Khurana,Cristian Ionescu-Zanetti,Maighdlin Pope,Jie Li,Liza Nielson,Marina Ramirez-Alvarado,Lynn Regan,Anthony L. Fink,Sue A. Carter +8 more
TL;DR: It is proposed that the hierarchical assembly model describes a general mechanism of assembly for all amyloid fibrils.
Journal ArticleDOI
Surface-catalyzed amyloid fibril formation.
TL;DR: In the present investigation, the in vitro assembly of a recombinant amyloidogenic light chain variable domain, SMA, on various surfaces was monitored using atomic force microscopy and the mechanism of fibril formation on the surfaces was significantly different from in solution.
Journal ArticleDOI
Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy
Cristian Ionescu-Zanetti,Ritu Khurana,Joel R. Gillespie,Jay S. Petrick,Lynne C. Trabachino,Lauren J. Minert,Sue A. Carter,Anthony L. Fink +7 more
TL;DR: The fibrils and protofibrils showed a braided structure, suggesting that their formation involves the winding of protofibils and filaments, respectively, which support a model in which two filaments combine to form a protofafibril, two prot ofibrils intertwine toform a type I fibrill, and three filaments form a type II fibril.