M
Mihaela Necula
Researcher at University of California, Irvine
Publications - 6
Citations - 1851
Mihaela Necula is an academic researcher from University of California, Irvine. The author has contributed to research in topics: Amyloid & Fibril. The author has an hindex of 5, co-authored 6 publications receiving 1752 citations.
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Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
Rakez Kayed,Elizabeth Head,Floyd Sarsoza,Tommy Saing,Carl W. Cotman,Mihaela Necula,Lawrence Margol,Jessica W. Wu,Leonid Breydo,Jennifer L. Thompson,Suhail Rasool,Tatyana Gurlo,Peter C. Butler,Charles G. Glabe +13 more
TL;DR: Since the fibril specific antibodies are conformation dependent, sequence-independent, and recognize epitopes that are distinct from those present in prefibrillar oligomers, they may have broad utility for detecting and characterizing the accumulation of amyloid fibrils and fibrillare type oligomers in degenerative diseases.
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Small Molecule Inhibitors of Aggregation Indicate That Amyloid β Oligomerization and Fibrillization Pathways Are Independent and Distinct
TL;DR: The results indicate that oligomers are not an obligate intermediate in the fibril formation pathway and suggest that small molecule inhibitors are useful for clarifying the mechanisms underlying protein aggregation and may represent potential therapeutic agents that target fundamental disease mechanisms.
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Methylene blue inhibits amyloid Aβ oligomerization by promoting fibrillization
Mihaela Necula,Leonid Breydo,Saskia Milton,Rakez Kayed,Wytze E. van der Veer,Paul Tone,Charles G. Glabe +6 more
TL;DR: The data show that Abeta oligomer formation is inhibited by promoting fibril formation, which suggests that the relative pathological significance of oligomers and fibrils may be tested in vivo using methylene blue.
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Anti-Aβ1–11 Antibody Binds to Different β-Amyloid Species, Inhibits Fibril Formation, and Disaggregates Preformed Fibrils but Not the Most Toxic Oligomers
Grigor Mamikonyan,Mihaela Necula,Mikayel Mkrtichyan,Anahit Ghochikyan,Irina Petrushina,Nina Movsesyan,Erene Mina,Anatoly Kiyatkin,Charles G. Glabe,David H. Cribbs,Michael G. Agadjanyan +10 more
TL;DR: In vitro observations suggest that preventive vaccination may protect from AD or may delay the onset of the disease, whereas therapeutic vaccination cannot disrupt the toxic oligomers and may only minimally alleviate preexisting AD pathology.
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Methylene Blue Modulates Huntingtin Aggregation Intermediates and Is Protective in Huntington's Disease Models
Emily M. Sontag,Gregor P. Lotz,Namita Agrawal,A. Tran,Rebecca Aron,G. Yang,Mihaela Necula,A. Lau,Steven Finkbeiner,Charles G. Glabe,J.L. Marsh,Paul J. Muchowski,Leslie M. Thompson +12 more
TL;DR: Methylene blue, which is well tolerated and used in humans, has therapeutic potential for Huntington's disease and inhibited recombinant protein aggregation in vitro, even when added to preformed oligomers and fibrils.