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Sergey Leikin
Researcher at National Institutes of Health
Publications - 96
Citations - 7562
Sergey Leikin is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Type I collagen & Osteogenesis imperfecta. The author has an hindex of 45, co-authored 92 publications receiving 6109 citations. Previous affiliations of Sergey Leikin include University of Maryland, Baltimore & Russian Academy of Sciences.
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Journal ArticleDOI
In utero transplantation of adult bone marrow decreases perinatal lethality and rescues the bone phenotype in the knockin murine model for classical, dominant osteogenesis imperfecta
Cristina Panaroni,Roberta Gioia,Anna Lupi,Roberta Besio,Steven A. Goldstein,Jaclynn M. Kreider,Sergey Leikin,Juan Carlos Vera,Edward L. Mertz,Egon Perilli,Fabio Baruffaldi,Isabella Villa,Aurora Farina,M. Casasco,Giuseppe Cetta,Antonio Rossi,Annalisa Frattini,Joan C. Marini,Paolo Vezzoni,Antonella Forlino +19 more
TL;DR: It is suggested that the engrafted cells form bone with higher efficiency than the endogenous cells, supporting IUT as a promising approach for the treatment of genetic bone diseases.
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Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta.
Elena Makareeva,Edward L. Mertz,Natalia V. Kuznetsova,Mary Beth Sutter,Angela M. DeRidder,Wayne A. Cabral,Aileen M. Barnes,Daniel J. McBride,Joan C. Marini,Sergey Leikin +9 more
TL;DR: Two large, flexible regions deduced from the ΔTm map aligned with the regions important for collagen fibril assembly and ligand binding, and one of these regions also aligned with a lethal region for Gly substitutions in the α1(I) chain.
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Electrostatic interaction between helical macromolecules in dense aggregates: An impetus for DNA poly- and meso-morphism
TL;DR: It is shown that the structural changes upon the B-to-A transition reduce the electrostatic energy by approximately kcal/mol per base pair, at a random adsorption of counter ions.
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Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix.
TL;DR: As in Ehlers-Danlos syndrome (EDS) VIIA/B, fibrils containing pN-collagen are thinner and weaker causing EDS-like laxity of large and small joints and paraspinal ligaments, however, distinct structural consequences of N-anchor destabilization result in a distinct alpha1(I)-osteogenesis imperfecta (OI)/EDS phenotype.
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Measured entropy and enthalpy of hydration as a function of distance between DNA double helices.
TL;DR: Measured forces show an abrupt transition between regions of interactions with quite different characteristic decay lengths, with a discontinuous change in interhelical spacing, but both the entropic and enthalpic components of the interaction free-energy maintain smooth single-exponential variation across this transition.