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Elena S. Klimtchuk

Researcher at Boston University

Publications -  17
Citations -  323

Elena S. Klimtchuk is an academic researcher from Boston University. The author has contributed to research in topics: Amyloidosis & Transthyretin. The author has an hindex of 7, co-authored 13 publications receiving 270 citations.

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The critical role of the constant region in thermal stability and aggregation of amyloidogenic immunoglobulin light chain.

TL;DR: A paradigm shift in AL fibrillogenesis is suggested and the role of C(L) region is suggested as a potential therapeutic target.
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The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugation

TL;DR: Fluorescence-detected sedimentation velocity is used to determine the effect of S-sulfonate and S-cysteine on the quaternary structural stability of fluorophore-conjugated recombinant TTR under nondenaturing conditions and report the direct observation of tetramer stabilization by the potential therapeutic compound diflunisal.
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Interactions between fatty acids and α-synuclein

TL;DR: It is concluded that αS is not likely to act as an intracellular FA carrier, however, binding to negatively charged membranes appears to be an intrinsic property of αS that is most likely related to its physiological role(s) in the cell.
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Solution structure and backbone dynamics of human liver fatty acid binding protein: fatty acid binding revisited.

TL;DR: The structure and dynamics of human L-FABP with and without bound ligands by means of heteronuclear NMR revealed no evidence for an "open-cap" conformation or a "swivel-back" mechanism of the K90 side chain upon ligand binding, as proposed for rat L-fABP, and it is postulate that the lipid binding process in L- FABP is associated with backbone dynamics.
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Expression, purification, and in vitro cysteine-10 modification of native sequence recombinant human transthyretin

TL;DR: This is the first report detailing an effective and useful method for producing rTTR containing an amino acid sequence identical to human TTR, and describes the thiol modification of the recombinant protein to achieve exact replication of the several prominent post-translationally modified forms of TTR that have been identified in human serum.