L
Leonid Breydo
Researcher at University of South Florida
Publications - 77
Citations - 5239
Leonid Breydo is an academic researcher from University of South Florida. The author has contributed to research in topics: Protein aggregation & Amyloid. The author has an hindex of 30, co-authored 76 publications receiving 4680 citations. Previous affiliations of Leonid Breydo include University of Maryland Biotechnology Institute & University of Missouri.
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Journal ArticleDOI
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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Α-synuclein misfolding and Parkinson's disease.
TL;DR: The molecular basis of PD appears to be tightly coupled to the aggregation of α-synuclein and the factors that affect its conformation, and the influence of environmental and genetic factors on this process is examined.
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Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide.
Emilie Cerf,Rabia Sarroukh,Shiori Tamamizu-Kato,Leonid Breydo,Sylvie Derclaye,Yves F. Dufrêne,Vasanthy Narayanaswami,Vasanthy Narayanaswami,Erik Goormaghtigh,Jean Marie Ruysschaert,Vincent Raussens +10 more
TL;DR: The results are discussed in terms of a possible organization of the antiparallel beta-sheets in Abeta oligomers, which may be related to reported effects of these highly toxic species in the amyloid pathogenesis associated with AD.
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In vitro Conversion of Full-length Mammalian Prion Protein Produces Amyloid Form with Physical Properties of PrPSc
Olga V. Bocharova,Leonid Breydo,Alexander S. Parfenov,Vadim V. Salnikov,Ilia V. Baskakov,Ilia V. Baskakov +5 more
TL;DR: This work supports the protein only hypothesis of prion propagation and demonstrates that formation of the amyloid form that recapitulates key physical properties of PrP(Sc) can be achieved in vitro in the absence of cellular factors or a PrP (Sc) template.
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Accelerated neurodegeneration through chaperone-mediated oligomerization of tau
Laura J. Blair,Bryce A. Nordhues,Shannon E. Hill,K. Matthew Scaglione,John C. O'Leary,Sarah N. Fontaine,Leonid Breydo,Bo Zhang,Pengfei Li,Li Wang,Carl W. Cotman,Henry L. Paulson,Martin Muschol,Vladimir N. Uversky,Torsten Klengel,Elisabeth B. Binder,Rakez Kayed,Todd E. Golde,Nicole C. Berchtold,Chad A. Dickey +19 more
TL;DR: Overexpression of FKBP51 in a tau transgenic mouse model revealed that FK BP51 preserved the species of tau that have been linked to Alzheimer's disease (AD) pathogenesis, blocked amyloid formation, and decreased tangle load in the brain.